So, when we take antibiotics because of a bacterial infection, billions of bacteria are suddenly attacked by antibiotics.

They struggle to repair damage, maintain their structures and continue essential functions just to stay alive.

This ultimately weakens or kills the cells.

And as you can imagine, this is pure stress for the bacteria.

One that we take advantage of.

This article series takes you on a journey through the microscopic war between bacteria and antibiotics. Across five articles, we will explore how antibiotics attack bacteria, how bacteria overcome them, become resistant and how evolution pushes bacteria to survive the antibiotic war.

In this first part of the series, we explore how different classes of antibiotics work, while focusing on the most commonly used antibiotics. Once you understand these mechanisms, you will better understand how and why bacteria fight back, evolve and develop resistance.

Antibiotics attacking bacterial cells by stopping cell division

Bacteria have a rigid cell wall made of peptidoglycan to maintain their shape and internal pressure and to protect them from the environment. Without the ability to build or repair the cell wall, bacteria become fragile and burst easily.

This vulnerability is precisely what antibiotics from the β-lactam family exploit. You have probably heard of penicillin, one of the most well-known members of this class. Other similar antibiotics are amoxicillin and cephalosporins.

How these antibiotics work is pretty simple but devastating to bacterial cells: they block the so-called penicillin-binding proteins. These enzymes sit in the cell wall where they are responsible for building and cross-linking it.

So, when a bacterium gets hit by a β-lactam antibiotic, it loses the ability to divide. Basically, every time it tries to divide, it will burst like a water balloon.

Antibiotics sabotaging bacteria’s genetic machinery

Every bacterial cell carries instructions for life in its DNA, the molecule that stores genetic information. Before dividing, bacteria copy their DNA and then share it with their daughter cells.

Bacteria also make RNA, the molecule that executes the instructions stored in DNA. RNA comes in different types with distinct roles, but it is fundamentally needed to make proteins from DNA.

Some antibiotics exploit this vulnerability by inhibiting one of the cell’s information-processing machineries. This fundamentally interferes with DNA or RNA synthesis. If a bacterium can’t produce DNA or RNA, it can’t divide or maintain its genetic integrity, leading to cell death.

The antibiotic class fluoroquinolones inhibits DNA production. For example, ciprofloxacin freezes the enzymes that help bacteria copy their DNA. When DNA replication stalls, bacteria cannot divide. They accumulate damage and eventually die.

In comparison, rifamycins inhibit RNA synthesis. These antibiotics bind to the RNA polymerase, the enzyme that produces RNA from DNA. They thereby block the first step in protein production.

It’s like cutting electricity to an entire factory; without RNA, the cell cannot produce proteins, halting metabolism and growth. This is highly stressful to bacteria and can quickly kill them.

Antibiotics blocking protein production: The ribosome hijackers

Other antibiotics directly inhibit the protein production step: To build proteins, bacteria produce a temporary working copy of those DNA instructions, the so-called messenger RNA or mRNA.

This molecule travels to the ribosome, which reads the mRNA and makes proteins from it. Since proteins are essential for metabolism, movement, growth and cell division, no cell can function without them.

Some antibiotics, like tetracycline, take advantage of this protein production vulnerability. By interfering with ribosomes, these antibiotics prevent them from producing proteins and eventually the bacterial cells from functioning.

Interestingly, not all protein-production inhibitors kill bacteria in the same way. Some antibiotics are bacteriostatic, which means they freeze growth without immediately killing the cell. The bacteria cannot make new proteins, so they can’t divide or repair themselves. Instead, the existing proteins remain active for a while, allowing the cell to survive in a weakened state.

Others, like aminoglycosides, are bactericidal. Instead of simply blocking ribosomes, they cause the ribosome to make mistakes and produce misfolded proteins. These faulty proteins build up inside the cell and damage essential structures, overwhelming the bacterium, so it eventually dies.

Antibiotics disrupting metabolic pathways

Lastly, some antibiotics target essential metabolic pathways that bacteria need to survive. For example, folate is an essential vitamin that all organisms need to grow and reproduce, and most bacteria have proteins to make their own folate. So, when antibiotics block these folate-producing proteins, the bacterium will eventually run out of folate and lose the ability to grow.

How different antibiotics kill bacteria

As we’ve seen in this post, antibiotics can impact bacteria in many different ways. But they all have the same goal: do the biggest damage possible. Antibiotics can damage a bacterium’s DNA, its protein production machinery, metabolic pathways or the cell envelope.

This damage is essentially stress for the bacterium: they must repair the damage or adapt their metabolisms to it. If they cannot cope with the damage or the stress, they’ll die. And remember, this was basically the antibiotic’s goal from the beginning.

But be aware: this stress can be both lethal and a driving force for bacterial evolution. As they learn to cope with the antibiotic and the stress, they become resistant. And in future articles, we will explore these bacterial learning processes and how they help make bacteria resistant to antibiotics.

The post How Antibiotics Kill: The Weapons We Use Against Bacteria appeared first on Bacterialworld.
Bacterialworld - A blog about bacteria: from scientific studies to vivid stories about the fascinating bacterial world

Those bacteria that call your gut their home are the so-called commensal bacteria. Luckily, they have a special superpower: They can protect us from bacteria that cause infections and make us sick. For this, our commensal gut bacteria developed some extraordinary strategies to defend these pathogens.

So, by nurturing our friendly gut bacteria, you are also strengthening your protection against diseases. Here, we will look at what kind of bacterial wars are going on in your gut and how your gut bacteria defend pathogens and keep you healthy.

Your gut bacteria defend pathogens with toxic molecules

Bacteria have many different means to kill other microbes, competitors or even their own siblings. Often, these bacteria produce molecules that are toxic to their prey, which means they inhibit cellular proteins or machineries. Without these machineries, the prey is then lacking an essential cell function to grow or survive, so that it eventually dies.

Interestingly, gut bacteria produce and deliver many different toxic molecules of various shapes and sizes, functions and even origins.

Gut bacteria produce bacteriocins

Many bacteria produce molecules that are like antibiotics specifically to kill bacteria. These are called bacteriocins.

Some bacteriocins are simple and small molecules, while others can be big and fancy. However, they all have a similar goal: they bind to a specific target in the prey bacterium and prevent that target from working properly.

So, no wonder that many bacteria in our gut microbiome produce bacteriocins that are toxic to pathogenic intruders. Also, we carry a lot of different bacteria in our guts and they all produce different bacteriocins. Hence, incoming pathogens face this huge load of toxic molecules making it really difficult to establish themselves in our intestines.

For example, one bacterium that loves the warmth and lack of oxygen in our gut is the bacterium Ruminococcus gnavus. And this one produces at least two bacteriocins, Ruminococcin A and C, that are toxic against human gut pathogens like Clostridium perfringens.

Other friendly gut bacteria, like Escherichia coli or Blautia producta, also produce bacteriocins that are toxic to pathogens, like Enterococcus faecalis. And some of their bacteriocins can even impact our gut cells by activating and strengthening our immune response.

Gut bacteria produce short chain fatty acids from fibres

Another way to protect against pathogenic gut bacteria is directly related to your diet. When we eat a lot of fibres, which are non-digestible carbohydrates, our friendly gut bacteria break these up. From these fibres, they produce small molecules that are called short-chain fatty acids, which have many positive health benefits for our overall wellbeing.

Interestingly, when we have a lot of these short-chain fatty acids in our intestine, the pH drops. This is already pretty difficult for most pathogenic bacteria, as not many can handle this acidic environment.

Plus, short-chain fatty acids diffuse into pathogenic gut bacteria where the pH drops as well. This can disturb many cellular machineries from functioning properly and not many bacteria have the right tools to defend against this attack, so they’ll die.

Gut bacteria convert bile acids into toxic compounds

To better digest the fats in food, our liver produces bile acids. These molecules bind fatty acids and lipids so that we can take them up better into our bodies.

But some of our friendly gut bacteria can convert these primary bile acids from our liver. For example, one of these bacteria, Clostridium scindens, transforms them into secondary bile acids that can bind the lipids of bacterial membranes.

Like this, secondary bile acids open the membranes of some pathogenic gut bacteria, like Staphylococcus aureus, Bacteroides thetaiotaomicron or Clostridoides difficile. This eventually kills the intruders and keeps our guts pathogen-free.

Killing pathogens with bow and arrow

Yes, also direct bacterial wars are happening in our guts! And they are nasty!

Some bacteria use tiny little bows to shoot deadly arrows into other bacteria. And these arrows can be incredibly toxic so the shot bacterium has barely any chance to survive the attack.

Luckily, our gut bacteria use their bows and arrows to defend against gut pathogens. For example, commensal bacterium Bacteroides fragilis has three different bows and can shoot various arrows. And research showed that this bacterial friend can protect us from bacteria that otherwise cause intestinal diseases.

Interestingly, Bacteroides fragilis is not opposed to hit’n’kill its own toxic bacterial siblings since some members of his family can indeed make us sick. But our friendly Bacteroides fragilis collected many different immunity proteins against its evil siblings so that their toxic arrows cannot harm it. Instead, Bacteroides fragilis keeps shooting and killing until we are safe from the pathogenic sibling.

Keeping nutrients from pathogenic gut bacteria

Another important way how gut bacteria defend pathogens is by keeping nutrients away from them. In all mixed microbial communities, bacteria fight for nutrients, especially for metals like iron, zinc but also sulphur sources.

Luckily, our gut bacteria developed some sneaky ways to steal these metals from gut pathogenic bacteria. By sending out special proteins that bind these metals very tightly, the commensals make sure to keep these metals from the pathogens. And if the pathogenic bacteria don’t have enough of these essential metals, they won’t survive and will eventually die.

Strengthening the mucus layer to block pathogenic gut bacteria

When you think about it, your gut is not part of your body – even though it is inside of you. All the food that we eat, stays within this digestion tube (mouth, oesophagus, stomach, intestines) until it comes out on the other side.

And to protect us from harmful microbes and molecules, we need to have a clear physical barrier from the content of the tube. This barrier is the so-called epithelial layer, which is covered by a slimy mucus on the outside. And this sticky slime helps keep off intruding microbes so that they cannot breach through the epithelial wall and get into our bodies.

Luckily, our helpful gut bacteria help us maintain this slimy defence wall. As bacteria produce SCFAs close to the mucus layer, the epithelial wall produces more slime. And if the slime gets thicker, gut pathogenic bacteria have more difficulties getting into our bodies.

To help the slime grow, some bacteria adapted very well to the conditions within the gut. For example, the friendly gut bacteria Akkermansia muciniphila and Ruminococcus gnavus cut off the very end of the mucus layer and feed themselves with them. This does not harm the mucus itself, but it keeps these bacteria close by. And this in turn triggers the epithelial wall to produce more mucus. So, everyone wins.

How to help your gut bacteria defend pathogens

Now, that you better understand how your gut microbiome defends pathogenic gut bacteria, make sure you support them keeping you healthy. By feeding your gut bacteria the right foods, you will help them be comfortable and happy in your gut. And when the right bacteria grow within you, they will gratefully protect you from nasty intruders!

Another idea for researchers is to use what they have learned to keep you healthy. The idea is to develop probiotics or prebiotics that help us defend against nasty pathogens. For example, you might take pills containing toxins against pathogenic gut bacteria or probiotics with bacteria that can fight off pathogens.

Whatever it may be, you can always help your gut bacteria be happy in your intestines by eating the right things. That means lots of fibre and veggies! ?

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Bacterialworld - A blog about bacteria: from scientific studies to vivid stories about the fascinating bacterial world

And more and more people become aware that a plant-based diet is not only better for your health, but also for our planet. Hence, the focus on agriculture right now is to become more sustainable to grow enough plant-based food for everyone.

This means that we need to find better ways to support plant growth and protect plants from diseases. Unfortunately, several plants pathogens make plants sick, so they die or do not grow enough crops.

Currently, we use fertilizers and pesticides to protect plants from pathogens. However, these chemicals are bad for the environment long-term as they contaminate the soil and water.

Hence, we need to find ways to protect plants by either getting rid of dangerous intruders or by strengthening the immune systems of plants.

Enter bacteria and their superpowers.

They do both.

What is biocontrol?

Some bacteria that live in or on plants are called biocontrol agents. These organisms are harmless to the plant and have two main functions: They protect the plant from pests and diseases and support its growth and crops.

Some of these organisms additionally strengthen the plant’s immune system or resistance – again to protect the plant from disease and help it grow.

One such biocontrol agent is the bacterium Pseudomonas putida. It grows near the roots of many plants where it produces helpful molecules for the plant.

And plants are clever too as they make sure that only the right types of bacteria grow near them. For this, several plants release specific molecules through their roots that help Pseudomonas putida grow. The bacterium senses these molecules so that they activate the bacterium’s chemotaxis system.

Now, Pseudomonas putida uses its flagellum to swim towards these molecules. This movement ultimately leads the bacterium to the plant that released the molecules.

Pseudomonas putida as a biocontrol agent

Once the bacterium “found” the plant, it settles down near it and starts building biofilms. Within these biofilms, the bacteria are connected with each other and with the plant. Like this, they can easily exchange molecules and information with each other and with the plant and build close relationships.

Pseudomonas putida now produces molecules to help the plant grow. For example, some molecules extend the tips of the roots so that the plant can better take up nutrients from the soil.

Pseudomonas putida also breaks down complex nutrients in the soil that the plant use. This basically feeds the plant the needed nutrients. Other molecules from the bacterium activate the overall immune system of plants so that plant pathogens have a harder time infecting the plant.

Altogether, Pseudomonas putida has similar features as biofertilizers that help plants grow.

How does bacterial biocontrol protect plants against intruders?

Pseudomonas putida can also directly fight off plant pathogens to protect their plant hosts. For this, it uses two strategies: It either holds back essential nutrients from plant pathogens or kills the intruder.

Not sure which strategy is more evil though…

Pseudomonas putida keeps essential nutrients to inhibit plant pathogens

All living organisms need iron to live and grow. And one efficient strategy to prevent other microbes from growing is by stealing iron from them.

Our immune system does it as well: All iron in our body is bound to specific transporters. Like this, no free iron swims in our blood for microbes to use. This defence mechanism is one of the first strategies of our immune systems to keep harmful bacteria from growing inside our bodies.

Similarly, Pseudomonas putida produces many different iron transporters that bind iron very efficiently. Like this, no free iron is present in the soil that other microbes could use.

Yet, this is not all. Pseudomonas putida is quite a naughty one since it can also steal iron-loaded transporters from other bacteria. This not only prevents the other bacteria from using the iron, but it also helps Pseudomonas putida grow.

Pseudomonas putida kills intruding plant pathogens

Lastly, Pseudomonas putida is a real fighter when it comes to protecting its host plant. This bacterium uses a special nanoweapon to kill plant pathogens.

Our bacterial fighter carries a bow and arrow and is not afraid of using them to keep intruders off the plant. Pseudomonas putida actively shoots arrows together with lethal toxins into other bacteria to kill them. Many bacteria use this killer machine, called the type 6 secretion system. But interestingly, Pseudomonas putida seems to have a more efficient killing device than others.

Scientists proved that with a simple experiment. When different plant pathogens were growing inside plant leaves, the leaves got sick. However, when Pseudomonas putida was additionally living in the leaves, the plant leaves did not get sick.

Finally, the scientists let the plant pathogens grow together with a Pseudomonas putida bacterium that could not shoot its bow and arrow. Now, the plant leaves got sick again and the plants suffered from the plant pathogens.

These results show that Pseudomonas putida uses its bow and arrow to actively kill other harmful bacteria to protect plants. Even though the experiment was done in plant leaves, scientists are convinced that something similar happens in the root area of plants.

Bacteria as biocontrol agent to save our planet?

As soon as we better understand how exactly this plant warden protects its host from harmful bacteria, we could use Pseudomonas putida on a large scale. This would improve the health of plants so that they can grow more and better crops.

Hence, such a biocontrol agent would eventually help us have more food available for everyone.

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Bacterialworld - A blog about bacteria: from scientific studies to vivid stories about the fascinating bacterial world

But what do bacteria and fungi use antibiotics for? Why do they produce them? And what are the advantages of microbes having antibiotics as molecular weapons?

What are antibiotics?

The father of antibiotics, Selman Waksman, first used the word antibiotics for any small molecule made by a microbe that can inhibit the growth of other microbes.

So, microbes – especially bacteria and fungi – use antibiotics to kill other microbes. These other microbes can be bacteria, fungi or bigger organisms. Not viruses though!!!

Why not viruses?

Because antibiotics bind and inhibit cellular machines in living organisms. These molecules often bind to so-called targets. Antibiotic targets can be proteins or enzymes that make for example the cell wall, other proteins or components of the respiration complex.

These proteins are generally essential. So, when antibiotics inhibit the proteins, the cells are missing these essential functions. And without them, they cannot survive and die.

Hence, like other bacterial toxins, antibiotics are lethal.

Interestingly though, bacteria and fungi make antibiotics from simple building blocks. These are present in every cell and can be amino acids, lipids or even sugars.

But instead of using these building blocks for their normal functions, microbes link them together in different ways. With this, they create new – and fancier – molecules that barely resemble the original blocks.

Then, they transport these antibiotics to the outside or send them off in outer membrane vesicles. When the antibiotic hits another microbe, there are two possibilities: either the microbe is resistant to the activity of the antibiotic or it dies from it.

But what about the microbe that produces the antibiotic? Is it resistant to the antibiotic itself?

Why are microbes that produce antibiotics not get killed?

Since antibiotics are meant to KILL other microbes, then why do producing microbes not get killed by their own antibiotics? The answer is self-protection!

Whenever bacteria or fungi produce antibiotics, they always also produce some sort of self-protective means. Just as when bacteria produce other toxins, they always need to make sure they are not killed by their own weapons.

These self-protectors usually keep the antibiotic in an inactive state. For example, they completely surround the antibiotic molecule so that it cannot bind to its usual target within the cell. Another strategy is to add a small molecule to the antibiotic – again to keep it from binding to its target.

Then, when the microbe is ready to transport the antibiotic outside of the cell, it takes the self-protection off the antibiotic. This releases only the toxic part – the antibiotic itself – into the surrounding.

Note, however, that these self-protection mechanisms are not antibiotic resistance mechanisms. Self-protection mechanisms are meant to inactive antibiotics only temporarily. Hence, these mechanisms are reversible. The antibiotic can still become active and thus toxic.

Resistance mechanisms, on the other hand, are meant to inactive antibiotics permanently. Hence, these mechanisms are irreversible. Since this usually completely destroys the antibiotic, it cannot become active anymore.

But what triggers microbes and especially bacteria to produce antibiotics? How do antibiotics help the producing cell in their daily circumstances?

Why do bacteria produce antibiotics?

To answer this question, we need to look at where the bacteria live that make antibiotics. And two-thirds of the known antibiotics are made by bacteria from the Actinobacteria family. Within this family, Streptomyces is the best-known member that produces half of all known antibiotics.

Another example is bacteria from the Myxococcus family. So, where do Streptomyces and Myxococcus bacteria live? Interestingly, these bacteria call the soil their home.

And in the soil, they often confront lots of friends and foes. And they need to constantly fight for their own survival.

Myxococcus is known as a wolf-pack predator because it kills its prey in massive attacks. Colonies of Myxococcous roll over their prey, secrete antibiotics and thus kill them and feed on them.

Streptomyces, on the other hand, uses its antibiotics a bit more civil.

To move in the environment, Streptomyces bacteria grow as long filaments throughout the soil. They build long chains and branch out into the soil as multicellular organisms. These branches are filled with Streptomyces cells but also spores so that the bacteria can extend to new places.

When the bacteria hit a period of bad weather or don’t find much food, they release their spores as a survival strategy. Plus, they start releasing nutrients for the spores. But these nutrients also attract other organisms like bacteria.

Hence, at the same time, Streptomyces produces a huge amount of antibiotics to fend off these putative food-stealers. Like this, Streptomyces makes sure their spores are safe and can survive in their new homes for a while.

How do antibiotics produced by bacteria help others?

Like Streptomyces, lots of bacteria use antibiotics to fight off predators. This assures their own survival and that of their species.

Yet, more and more research finds that bacteria not only kill other species with antibiotics so they can survive. The killing also benefits their hosts.

For example, the bacterium Janthinobacterium lividum lives on frogs where it produces the antibiotic violacein. This antibiotic kills fungi so that the bacterium protects the frog from deadly fungal infections.

Also, a bacterium that lives in our noses is the harmless Staphylococcus lugdunensis. This bacterium produces the antibiotic lugdunin. That inhibits the harmful Staphylococcus aureus from settling down in our noses. Now, scientists look into how we could use the harmless Staphylococcus lugdunensis to protect us from infections.

Another example of microbes that produce antibiotics to help others is the three-member association of ants, Streptomyces and a fungus. Several species of ants grow fungi for food. They feed their fungi with fresh plants and let them grow in special underground gardens.

To not contaminate these fungal gardens, ants carry symbiotic Streptomyces that produce antibiotics. Like this, the antibiotics kill other microbes and keep the fungal gardens free of harmful intruders. As a thank you, the ants feed the Streptomyces and give them a place to live.

About antibiotic-producing microbes

So, just as we use antibiotics to kill harmful bacteria and fungi, antibiotic-producing microbes do the same. They want to fight off predators and assure their own survival.

When you think about it: we use their own killer weapons against them. Poor microbes!

The post Bacteria use antibiotics to kill their foes and protect others appeared first on Bacterialworld.
Bacterialworld - A blog about bacteria: from scientific studies to vivid stories about the fascinating bacterial world

Also, bacteria want to grow and flourish and reproduce. But they are only single cells so that their way of reproduction is unique. They reproduce asexually meaning you only need one parent bacterium to make two daughter bacteria.

When you think about it, bacterial cell division seems very easy: Start with one bacterium, divide it in the middle and you end up with two.

However, the mechanism of cell division is pretty complex and involves at least three tasks:

• the bacterium needs to decide WHERE to divide
• get all the needed machinery to the division site
• produce new cell envelope material to separate the two new daughter cells

How a bacterium starts cell division

As you can imagine, for most bacteria it makes the most sense to divide straight in the middle. Like this, they end up with two daughter cells of the same size.

This means a bacterium needs to find its middle and mark it. While it is not completely clear yet to researchers how bacteria find the exact middle, they know it involves a so-called Z-protein.

This Z-protein can bind two things: itself and the inside of the bacterial cell envelope. But it only binds the cell envelope where it is straight and not bent. And this is only the case in the middle of the bacterial cell envelope.

Hence, the Z-proteins bind themselves in a long chain linked to the straight cell envelope. Eventually, they form a ring on the inside of a bacterial cell. And this so-called Z-ring stays in the middle of the bacterium.

Also, the Z-ring is only stable when bacteria have enough nutrients and do not encounter any stress situations. This reassures that bacteria only divide when they have all the needed supplies.

How bacteria divide and produce two daughter cells

Once this Z-ring is stable, it recruits helper machineries to this now defined division site.

The Z-ring is a sign of an upcoming cell division. Now, the bacterium knows it needs to activate machineries to produce more cell envelope material and become longer. And to increase their cell envelopes, bacteria use ferries, tunnels and bridges to transport lipids into the cell envelope.

Like this, the bacterium becomes longer and can start the actual cell division. At the same time, the Z-ring becomes tighter and the cell envelope gets its natural bend again.

Now, two processes happen at the same time: Bacteria cut open their peptidoglycan envelope to separate the two daughter cells and also produce envelope material to close both cells.

After this happened, we have two daughter cells coming from the same parent. They both share the same cell envelope and genome. This is why we consider them identical twins.

But do all bacteria produce identical twins upon cell division?

Do bacteria always divide in the middle and produce identical daughter cells?

Yes, most bacteria are symmetrical. And when they divide right in the middle, they produce two identical daughter cells.

Researchers could even watch bacteria during this process thanks to amazing microscopy techniques. You can see the single stages of bacterial cell division and how bacteria produce the cell envelope in the image below.

Yet, the bacterium Caulobacter crescentus has two different cell ends. It can stick to a surface with its sticky stalk on one end and have flagella on the other.

This bacterium also starts cell division in the middle like what we discussed above. However, the new daughter cells are now different: one is still glued to the surface and the other one has flagella and can swim away.

Also, the bacterium Helicobacter pylori with its helical shape can never really find its perfect middle. Hence, the Z-ring forms somewhere inside the bacterium and its daughter cells always have different sizes.

And then there are funny bacteria that decided they don’t even need to divide in the middle. Bacteria like Gemmatimonas aurantiaca grow “budding” daughter cells out of their own parent cells. However, researchers don’t understand yet why this bacterium chooses to divide in this asymmetric way.

Another way of asymmetric cell division happens in the bacterium Bacillus subtilis when it produces spores. During the sporulation process, the spore daughter cell grows within the mother cell. In the end, the mother cell bursts to release the spore into the environment. In this case, only one daughter cell comes out of the division process.

Why and how we want to prevent bacteria from dividing

Since cell division is an essential mechanism for bacteria, nature also found ways to inhibit it. Many antibiotics or toxins inhibit the production of cell envelope material or of the Z-ring. Like this, bacteria cannot divide anymore; they cannot grow and die.

However, we also know that some bacteria can find ways around the toxicities of antibiotics or toxins and become resistant to them. Hence, by better understanding how the whole mechanism works, researchers can hopefully find new ways to interfere with bacterial growth and find new weapons in the fight against antimicrobial resistance.

The post Why bacteria divide into two and grow with the help of a strong ring appeared first on Bacterialworld.
Bacterialworld - A blog about bacteria: from scientific studies to vivid stories about the fascinating bacterial world

And looking at these bacterial siblings can help researchers understand the basic mechanisms of the bacterial world.

For example, some bacterial families contain both pathogenic and non-pathogenic bacteria. Pathogenic bacteria are those, that have weapons to infect us and make us sick.

On the contrary, non-pathogenic bacteria are harmless to us since they do not have these weapons.

But to fight off the dangerous bacteria, we still need to better understand what turns a harmless bacterium into a nasty one. Thus, researchers are trying to learn more about the differences between pathogenic and non-pathogenic bacteria.

So, what is better than looking at bacterial siblings that are both pathogenic and non-pathogenic. They often carry the same or similar genes. And yet, they have different weapons and some of these harm us while others don’t.

One interesting example of a bacterial family with diverse siblings is Vibrio cholerae.

Vibrio cholerae and its good and bad bacterial siblings

Bacteria from the Vibrio cholerae family live on zooplankton and shellfish in brackish waters. Every once in a while, we come into contact with such a bacterium when we eat seafood or drink contaminated water. And unfortunately, some siblings of the Vibrio cholerae family can cause very dangerous and even life-threatening diarrhoea. These are the pathogenic siblings.

But interestingly, not all bacterial siblings can infect our gastrointestinal tract. These non-pathogenic siblings do not have the right tools to infect and harm us.

Therefore, researchers have been curious about what distinguishes these pathogenic and non-pathogenic siblings.

All these siblings – pathogenic or non-pathogenic – have one killer machine in common. They use a bow to fire toxic arrows into prey cells. And these cells can be bacteria, amoebae or even human cells.

Yet, within the Vibrio cholera family, not every sibling has the same set of arrows and cannot fight the same target. Hence, researchers assumed that these different sets of arrows would give the siblings the skills to become a pathogen or not.

Vibrio cholerae siblings fight off amoebae with bow and arrow

Researchers looked at five siblings from the Vibrio cholerae family and their fighting behaviour. Let’s call these siblings Pan, Ariel, Bobby, Chris and Danny.

These five bacterial siblings all have the same bows. Yet, they have different arrows that give them different fighting powers.

So, the five siblings use these arrows to defend themselves against enemies in the environment, other bacteria or even their own siblings. Some of these enemies are even bigger microorganisms like amoebae.

These amoebae are like human immune cells. They hunt and eat bacteria in similar ways.

Hence, some Vibrio cholerae siblings use their bows and arrows to protect themselves from amoebae. For example, the siblings Chris and Danny have arrows that they fire into the amoebae. These arrows have toxic bullets attached to them so that they can kill the amoebae.

Ariel and Bobby have the same kind of arrows, but these do not carry the toxic bullets. Since Ariel and Bobby cannot kill amoebae, researchers suggested that only Chris and Danny use their toxic arrows to protect themselves from amoebae.

In comparison, Pan has the same arrow and the same toxic bullets. But Pan’s bow is not active. It only gets activated under certain circumstances. Hence, when Pan faces an amoeba, it gets eaten even though it has the weapon to defend itself. Poor Pan.

Vibrio cholerae siblings kill bacterial opponents with bow and arrow

Next, their different arrows also help our bacterial siblings when facing bacterial enemies. All siblings react and defend themselves in different ways.

Since Pan’s bow is inactive, it cannot fight off bacterial enemies. Even though it has many strong arrows. It just does not fire them.

The other siblings, however, know how to use their bows and arrows. And since their arrows deliver different toxic bullets, they kill with different efficiencies.

It becomes more interesting when these siblings fight each other. In these family fights, the toxic bullets make the difference.

For example, the four siblings Ariel, Bobby, Chris and Danny can all kill off Pan easily. This is because Pan does not have an active bow, so it would not fire any arrows. Pan does not stand a chance against its siblings.

Ariel has very toxic bullets. And it does not hesitate to fire them into its siblings to kill them.

Not Bobby. Bobby struggles with fighting off other bacteria as well as its siblings. Hence, researchers suggest that Bobby’s arrows and bullets are less toxic and thus less efficient to kill.

These types of experiments help researchers understand how bacterial siblings are immune to each other’s attacks. And it gives them some clues about what makes a toxic truly efficient.

Different powers give bacteria different advantages

Just as your special skills give you great opportunities or advantages in life, bacteria use their fighting powers to survive and thrive. They learned how to defend themselves against enemies of all kinds and families. And some of them seem to have more or less efficient ways to achieve this.

So, by learning about the defence mechanisms of bacteria, we might be able to find new and better ways to fight off the nasty bacteria ourselves. Let’s hope that one day we can fight them with their own weapons.

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Bacterialworld - A blog about bacteria: from scientific studies to vivid stories about the fascinating bacterial world

Some microbes come to make their hosts sick. Other microbes are there to help and protect them.

This is a story of both types of microbes and an unusual host: amphibians.

Yes, also frogs and salamanders and other amphibians carry microbes on their skins.

And some of these microbes mean to kill the animals. But, luckily, the animals are protected by helpful bacteria that produce colourful antibiotics.

Read on to find out how bacteria and fungi do not get along on the skin of amphibians. We will also explore how bacteria protect amphibians from extinction.

About fungi that infect the skins of their hosts

Many frogs, salamanders and other amphibians have gone extinct because of a deadly fungal infection. And it seems that many more animals are already infected and sick from that same pathogen.

The bad guys? The two fungal species Batrachochytrium dendrobatidis and Batrachochytrium salamandrivorans. They cause a deadly skin disease on frogs and other exotic amphibians.

Similarly, the fungus Trichophyton rubrum can infect our skin and hair. This pathogen causes a disease that you may know as ringworm or athlete’s foot. Typically, you can see such a fungal infection as a red, itchy and circular rash.

But luckily there is a new weapon around to keep these fungal intruders at bay: Bacteria that get rid of the fungus to protect their hosts.

Bacteria produce colourful antibiotics…

Few microbes can grow and thrive on the gloomy skin of frogs or salamanders. One such microbe is the bacterium Janthinobacterium lividum.

This bacterium has an interesting taste for food. It eats the released skin when the amphibians shed their skin. And it also really likes the mucus on the surface of the amphibians.

As a thank you for the good meal, the bacteria help the amphibians in the fight against the deadly fungus.

How?

Generally, bacteria produce antibiotics to get rid of annoying competitors. For example, Janthinobacterium produces the antibiotic violacein, which has a dark violet colour. This antibiotic also kills the fungi that make the frogs sick.

It is still unclear to researchers, how Janthinobacterium transports the antibiotic to the fungus. We already know that the bacterium Chromobacterium violaceum produces membrane bubbles filled with violacein. And that it throws these purple bubbles at its competitors. So, one idea is that Janthinobacterium uses a similar strategy and throws violacein bubbles at the fungus.

Also, when Janthinobacterium grows on the skin of frogs, it triggers the frog to produce more anti-fungal molecules. These molecules kill the fungus and other pathogenic bacteria that are dangerous to the frog.

… and protect them from deadly fungi

Janthinobacterium is not the only bacterium that produces colourful antibiotics to protect its host.

You might have seen red dots in your shower every once in a while. These come from the bacterium Serratia marcescens which makes a red antibiotic. Interestingly, this bacterium can also live on the skins of amphibians. And here, the red antibiotic also protects from deadly fungi.

Other bacteria, like allrounder Pseudomonas, also live on the skins of some amphibians. And these bacteria produce many different antifungals to protect their hosts.

Hence, it looks as if the right skin bacteria protect frogs and salamanders from deadly fungi. And these bacteria keep throwing around colourful bubbles filled with antibiotics – sounds like a bacterial festival to celebrate their hosts?

Colourful bacterial antibiotics to save amphibians?

Now, researchers are trying to save amphibians from the deadly fungus with a process called bioaugmentation. With this strategy, researchers introduce special bacterial communities to the environment. And they hope that the bacteria will jump over to different amphibians.

Bacteria like Janthinobacterium then hopefully establish stable communities on the skins of amphibians and protect them from fungal infections. And let’s hope that these bacterial parties will save more frog species from extinction!

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Bacterialworld - A blog about bacteria: from scientific studies to vivid stories about the fascinating bacterial world

What’s your New Year’s resolution?

Are you trying to eat healthier by eating microbially fermented foods full of nutrients?

Or do you want to be more friendly to the environment by using green bio-plastics?

Keeping this planet green and healthy is a great New Year’s resolution. And one that microbes can help us with.

For example, microbes can degrade and remove the toxic pollution that we have produced. They do that in a process called microbial bioremediation.

Just another way microbes help save the planet.

Our pollution problem

Oil spills, chemical leaks, industrial discharge. We hear about these types of toxic pollution all too often. Increased urbanization, industrialization, and utilization of natural resources pollute and contaminate the environment, which is unhealthy to humans and the planet.

Unfortunately, it is much easier to spill oil or leak a chemical than it is to clean it up. Especially, if the pollution compound is toxic. Cleaning up these types of pollution is costly and may be harmful to the environment.

Why microbial bioremediation?

How lucky are we that microbes can make cleaning up these messes easier? Our microbial friends can degrade and detoxify environmental pollution. This process is called microbial bioremediation.

Microbes absorb or eat toxic pollutants. They then break them down into harmless compounds. This process is a more cost-effective and environmentally friendly method to clean up toxic pollution.

Cleaning up after oil spills

We use petroleum oil in multiple ways, from powering our cars and homes to manufacturing plastics and medicines. Most petroleum oil is found deep in the ground and it takes much energy and expense to pump the oil to the surface.

Unfortunately, sometimes we spill some of that oil. The 2010 Deepwater Horizon oil spill in the Gulf of Mexico is the largest known oil spill and it released 4.9 million barrels of oil into the ocean! What an environmental disaster!

Petroleum oil is a type of fossil fuel full of different organic compounds called hydrocarbons. They contain hydrogen (“hydro”) and carbon molecules. For us humans, ingesting these compounds would be deadly.

So, when that oil disaster happened in 2010, microbiologists and their microbial friends came to the rescue. Luckily, some microbes have special enzymes that recognize and degrade hydrocarbons into smaller compounds. They then use these smaller compounds to grow and reproduce.

Microbes eating hydrocarbons

Many bacteria can degrade petroleum oil. For example, a special Pseudomonas aeruginosa strain can break down oil droplets and grow on petroleum oil with nothing else to eat.

Additional Pseudomonas strains as well as Bacillus subtilis strains are capable of eating hydrocarbons too.

Researchers have also found communities of bacteria working together to degrade and remove petroleum oil. And they are now developing ways to implement these bacterial communities for cleaning up oil spills from contaminated soil and water.

Fungi are also used for bioremediation, called mycoremediation (“myco” refers to fungus). Researchers discovered 16 different fungi species that degrade hydrocarbons in crude oil.

The superhero fungi Trichoderma viridae, Aspergillus flavus and Varicosporium elodeae have the highest rates of degradation. And the Exophiala xenobiotica fungus degrades a hydrocarbon compound found in car gasoline.

Scientists are working to use these microbes in larger bioremediation projects as greener and cheaper ways to clean up oil spills.

Detoxifying heavy metal contamination

Oil spills are not the only toxic pollution generated by us humans. Through many industrial processes, we release heavy metals such as copper, lead, and mercury. Once in the environment, heavy metals can enter the food supply and accumulate in our bodies. Unfortunately, these can lead to health issues and sometimes even cancer.

Removing heavy metals from contaminated water and soils is costly, time-consuming, and ineffective at low concentrations of the contaminate. Good thing microbes can make this process faster and more efficient.

They help remove heavy metals through a process called biosorption. Microbial cell walls are made up of proteins and sugars with a slightly negative charge. Metals have a positive charge.

Thus, microbes can attract and bind these toxic metals. This means microbes act like magnets and pull out the toxic metals from the environment.

Many microbes can absorb a variety of metals. But these microbes also need to protect themselves from toxic metals. For this, they have special enzymes that transform the metals into less toxic forms inside the cell.

However, even microbes cannot survive if the concentration of toxic metals is too high. So, it is important to find microbes that can tolerate high levels of metals and detoxify them. Scientists have discovered some Aspergillus species that can survive high concentrations of copper and nickel metals.

These microbes must also be superb at decontaminating. One rockstar strain of Aspergillus flavus removed over 97% of mercury contamination. And two Pseudomonas species strains removed over 75% of copper, lead, and zinc contamination. Microbes like these will be vital for removing future heavy metal contamination.

Microbes creating a cleaner future

There are a lot of toxic materials in our world. As human activity increases, so too does the amount of toxic pollution we create on our planet. The results of oil spills and heavy metal contamination hurt our human health as well as the health of our planet.

Luckily, microbes have evolved ways to survive and detoxify these types of pollution. Our microbial friends can help remove these toxins and clean up messes created by us. By harnessing the power of microbes, bioremediation projects address our pollution problem and work to make our planet a greener and healthier place. And that’s a great New Year’s resolution!

Along with microbes, we can save the planet!

Take away messages from this week’s article:

• Toxic pollution is a major problem for the health of humans and our planet
• Microbes can detoxify environmental pollution in a process called microbial bioremediation
• Microbial bioremediation is an environmentally friendly and relatively inexpensive way to clean up toxic pollution

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Bacterialworld - A blog about bacteria: from scientific studies to vivid stories about the fascinating bacterial world

They need food, more space and are just annoyed by intruding competitors.

So, when they decide to bring out the big (tiny) killer machines, they aim to hurt their opponents badly.

One of these killer weapons is the so-called type 6 secretion system. It looks like a crossbow that sits within a bacterial cell waiting to fire lethal arrows.

And these arrows are the real deal in this killer weapon. They punch holes into the membrane of the opposing microbes and carry lethal toxins into the cell.

Here, we will focus on these arrows and how they work.

Bacteria fire lethal spikes to kill

This type 6 secretion system crossbow is made up of two parts. One part – the base – stays within the firing bacterium. You can understand this as a stem inside the bacterium.

On top of this stem sits the second part – the arrow. This arrow is ready to be fired and will actually leave the bacterium. It consists of three parts, that you can also see in the picture below:

Such an arrow has a long thin spike (red) that is connected to the stem (black). Onto this spike, different toxins (purple) are glued and hang around the arrow. On the top of the spike, the arrow has a pointy tip (pink) that pokes the membrane of the prey bacterium.

So, when bacteria shoot these type 6 secretion system arrows into other bacteria, they shoot all these different parts: the tips, the spikes and the toxins. And the toxins are what ultimately kill the prey bacteria.

Now, bacteria actually have several different proteins for these parts of the arrow lying around in their cells. And for long, it was not clear how bacteria decide how to assemble such an arrow. So, different studies looked at these different parts and how they interact with each other to better understand how bacteria build their lethal arrows.

Let’s start at the top.

A master hat protein decides for the assembly of the arrow

The protein at the very end of the arrow is called the PAAR protein. It is very sharp and has the shape of a hat. The bacterium uses this pointy end to punch a hole into the prey bacterium’s membrane.

Our bacterium of interest, Pseudomonas aeruginosa, contains seven of these hat PAAR proteins and ten different spike proteins. Generally, one PAAR protein sits on the top of one arrow spike while the spike is actually made of three VgrG proteins. So, one study looked at which of these pointy PAAR proteins belongs to which arrow spike.

To do this, researchers made different versions of the same bacterium – so-called mutants. These did not have certain hat proteins anymore so they could not kill their opponents that efficiently anymore. Also, these bacteria were unable to fire their arrows in the first place.

With these experiments, the researchers could then identify the different hat-spike pairs in Pseudomonas aeruginosa. They also learned that the PAAR protein actually determines which arrow the bacterium will fire next.

Lethal toxins stick to the spike protein

Next, the spike proteins are incredibly important since they carry the different toxins into the prey cell. And for a toxin to stick to a spike, they both have specific patches. And these patches are unique for each spike-toxin pair.

Researchers showed this by swapping the patches for the toxins between different spike proteins. They looked at the spikes G4b and G5 in the bacterium Pseudomonas aeruginosa. Usually, the G4b spike has a patch for the toxin A and the G5 spike has a patch for the toxin B.

So, Pseudomonas aeruginosa uses spike G4b to kill with toxin A and if it feels like killing with toxin B, it shoots spike G5.

The researchers then interchanged those patches. Now the G4b spike had the patch for toxin B and the G5 spike the patch for toxin A. And they showed that G4b could not fire toxin A anymore and G5 could not fire toxin B anymore.

Instead, Pseudomonas aeruginosa now fired toxin B with the G4b spike and toxin A with the G5 spike.

This helped the scientists better understand how bacteria shoot their toxins out of the cell. Another study then looked at how this patch works and how exactly the toxin is glued to the type 6 secretion system spike.

Bacteria can (sometimes!) fire spikes with random stuff

Other studies then look at whether bacteria could use random toxins and glue them to the type 6 secretion system spikes. This idea might give us tools to shoot whatever we want with this killer machine. However, in practice, it is a bit tricky.

So, researchers tried different versions of this concept in the bacterium Pseudomonas aeruginosa.

First, they took a toxin from the same bacterium but from a different part to the arrow. Instead, they glued this toxin to the spike of the bacterium and looked at whether it would fire an arrow with this toxin. Indeed, the bacterium could now shoot this new arrow into other bacteria, even though it was not as efficiently.

In a second try, they tried to patch a toxin from a different bacterium to the spike in Pseudomonas aeruginosa. This new arrow was not able to shoot that toxin into other bacteria. So, there are some limitations about how the spikes and their patches work to make toxins stick.

Understanding bacteria and their spikes for new strategies

This bacterial nanoweapon is an incredibly handy tool for bacteria. They can deliver lethal proteins into almost any organism. If we managed to understand this weapon better, we might be able to modify it and deliver whatever we want with this.

We might be able to transport therapeutics, drugs or even anti-cancerous agents. But until we’re there, still quite a bit of research is needed.

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Bacterialworld - A blog about bacteria: from scientific studies to vivid stories about the fascinating bacterial world

Vaccines helped eradicate deadly diseases like smallpox.

And for over a century, researchers developed vaccines according to Pasteur’s principle. They isolated the microorganism and inactivated it. Then they injected the now harmless microorganism into people. 

Now these people were vaccinated.

Their immune systems would detect this foreign microorganism and develop antibodies against it. The next time this person gets infected with the real microorganism, the antibodies would be ready to fight the intruder.

New challenges for researchers

But unfortunately, developing vaccines is not always that easy.

Especially, when researchers have trouble growing an organism in the lab. As it is the case with the hepatitis C virus. And then there are nasty pathogens like Neisseria meningitidis. These know too well how to hide from the immune system and cause deadly meningitis. Or to fight a clever virus like HIV, we need help from extra skilled parts of our immune system. Let alone a virus as SARS-CoV-2 that emerged from nowhere and for which we need a vaccine real quick.

To develop vaccines against these microorganisms, researchers needed a new strategy. They try to find new vaccines that activate the immune system and trigger it to produce antibodies. These antibodies have to detect a specific piece of foreign microorganism. Often, this is a protein from the surface of the virus or the bacterium: the so-called antigen. 

But not every antigen is a good antigen that activates the immune system.

Hence, researchers need to produce and test different antigens. And for this, they rely on fancy technologies and super-efficient helpers: bacteria. Here, we will look at how researchers use bacteria in the hunt for vaccines. 

Bacterial pets in the lab

For some researchers, the bacterium Escherichia coli is a dear lab pet. They know exactly how to grow, change, regulate, mutate, shock and kill this bacterium. And they appreciate that their favourite lab bacterium can carry big chunks of DNA and produce almost any protein.

So, to produce and test antigens, researchers need to make DNA with a gene for an antigen.

Bacterial machines to produce DNA

To produce any piece of DNA, researchers use a special DNA production machine from the bacterium Thermus aquaticus. This bacterium lives in hot regions, so its enzymes only work at hot temperatures. 

Hence, researchers can control this DNA production machine by regulating the temperature. And like this, they can produce any gene they need.

Bacterial machines to cut and paste DNA

The problem is that the gene alone is not stable. This is why researchers need to put this gene (in blue in the picture below) into a plasmid. Plasmids are stable DNA circles (in yellow), that bacteria recognise and produce. 

To link these two pieces of DNA together, researchers use special scissors. These scissors cut the gene and the plasmid so that they now work like puzzle pieces. They can only fit together. 

These scissors also come from bacteria and, interestingly, every bacterium has its own type of scissors. This means researchers can produce many different puzzle pieces that always work in pairs.

Next, the plasmid and the gene need to be glued together. And for this, researchers use a glue stick from a virus. And yes, it works like the plaster in the picture.

Finally, we have a big chunk of DNA with a gene for an antigen.

Now, researchers need to produce this antigen.

Guess what, they use bacteria for that too!

Bacteria are protein production machines

First, the plasmid with the gene for the antigen needs to go inside the bacterial cell. For that, researchers electrocute the bacteria together with the plasmid. Yes, electrocute them! Poor bacteria!

But this brings the plasmids into the bacteria.

Next, researchers grow these bacteria with the plasmid. The bacteria now produce a lot of that plasmid and a lot of that antigen (blue).

Next, researchers need to kill the bacteria and clean the antigens from them.

With all the antigens produced now, the fun experiments can get started. 

Finding the best antigen for a vaccine

Generally, researchers produce many different antigens to find the best one as a vaccine. The best antigen is the one that binds to an antibody the tightest.

To test all the antigens, researchers do an experiment that is funnily called ELISA. And they can do this ELISA experiment only thanks to bacteria.

Some bacteria from the Streptomyces family produce the protein streptavidin. This protein binds very, very tightly to the vitamin biotin. Obviously, researchers make use of these two proteins in the lab.

In the simplest version of an ELISA experiment, researchers glue antigens to a surface (yellow, blue and green). Then, they add liquids with different antibodies (grey) to these antigens to test which one binds most tightly. 

These antibodies are linked to a biotin molecule (grey circle). Next, the researchers add streptavidin (green) that is linked to an enzyme. Now, only if the antibody bound the antigen, the streptavidin can bind the biotin. And if that happens, the enzyme can change the colour of the liquid. 

Like this, researchers can test many different antigens and “see” for which the colour changes. These are the ones that bound to an antibody.

Researchers need to repeat all these steps many times; each time changing the antigen a bit to make it more efficient.

But eventually, this antigen becomes a vaccine.

And just as bacteria produced the antigen in the lab, they might have to do that in large amounts to produce the masses of vaccines needed.

About vaccines produced by bacteria

Bacteria can produce different proteins and therefore different vaccines.

For example, the vaccine against the hepatitis E virus is completely made by bacteria. Bacteria produce the envelope proteins of the virus. These then assemble and build the virus structure. This vaccine now has the same structure as the virus, but it is inactive and harmless since no viral DNA is inside the envelope. 

Some vaccines also have components from different organisms. 

Our immune system can very well detect the sugars on the surface of bacteria. Hence, researchers attach some of these sugars to vaccines. Like this, they attract the big players of the immune system to the vaccine. This activates the immune system so that it develops antibodies against the vaccine.

Researchers also linked bacterial proteins to vaccines. Here, researchers found that bacterial toxins or proteins from the bacterial surface attract and activate the immune system. But not to worry, researchers worked out how to inactivate the toxin so that the vaccine is not harmful.

Not all vaccines are produced by bacteria

Lastly, researchers developed new strategies to produce vaccines without bacteria. And they even use this strategy for some vaccine candidates against SARS-CoV-2 that causes the COVID-19 disease.

These vaccines only contain a piece of RNA enveloped in a lipid membrane. And, yes, this concept looks a lot like bacterial outer membrane vesicles that transport DNA or drugs. 

In this case, our body produces the protein – the antigen – from the RNA. This again activates the immune system and triggers it to make antibodies against the antigen.

So while the delivery mode of the vaccine is pretty different, the way to activate the immune system is still the same.

Bacteria are important in the hunt for vaccines

Some microorganisms are real burdens to the world population. Hence, researchers had to come up with new strategies to tackle them. There is no vaccine against the nasty SARS-CoV-2 yet, and maybe the final vaccine will be produced completely independent of bacteria. But still, bacteria are massively helping researchers in the lab. 

They are amazing little machines to produce proteins or transport DNA or drugs. And they evolved helpful enzymes that every lab researcher uses daily. No biology-related research would work without the amazing mechanisms of bacteria.

Ever since the pandemic started, a lot of people ask me whether we can have bacteria kill the nasty SARS-CoV-2. I doubt it will be a direct fight between bacteria and viruses. But I am convinced that in the end bacteria and their superpowers will save this planet.

Researching and writing this post was possible due to the Journalism Research Grant from the Berlin Science Week.

it’s been a great first adventure as a proper science journalist at the #BerlinScienceWeek https://t.co/ZlJFOb9e18

— Sarah Wettstadt (@DrBommel) November 6, 2020

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Bacterialworld - A blog about bacteria: from scientific studies to vivid stories about the fascinating bacterial world