A Lego-Like Approach to Improve Nature’s Own Ability to Kill Dangerous Bacteria

A Lego-Like Approach to Improve Nature’s Own Ability to Kill Dangerous Bacteria A Lego-Like Approach to Improve Nature’s Own Ability to Kill Dangerous Bacteria

November 14, 20192 min read
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The Centers for Disease Control and Prevention considers antibiotic resistance one of the most urgent public health threats, one that affects communities worldwide. The ramifications of bacteria’s ability to become resistant to antibiotics can be seen in hospitals, public places, our food supply, and our water.



In their search for solutions, researchers at Rensselaer Polytechnic Institute have been looking to nature. In a paper recently published in Biomacromolecules, the team demonstrated how it could improve upon the ability of nature’s exquisitely selective collection of antimicrobial enzymes to attack bacteria in a way that’s much less likely to cause bacterial resistance.


“The idea is that we could take nature’s approach and just make it better,” said Jonathan Dordick, a chaired professor of chemical and biological engineering and a member of the Center for Biotechnology and Interdisciplinary Studies (CBIS).


In order for bacteria to grow and live, they naturally produce autolysin enzymes that can break down their own cell walls, allowing those cells to divide and multiply.

In attacking one another, bacteria take advantage of a similar process, using an antibacterial protein known as a bacteriocin to kill a bacterium.


Bacteria can also be attacked by bacteriophages, which are viruses that infect bacteria. They produce phage endolysin enzymes, which attack the bacterial cell from the inside. All three types of enzymes are broadly known as cell lytic enzymes, as they catalyze the breakdown of the bacterial cell wall.


“It’s very difficult for bacteria to become resistant to the action of these enzymes,” Dordick said. “For example, if they became resistant to an autolysin, they wouldn’t divide.”


Like building blocks, most cell lytic enzymes are modular. They’re made up of one binding domain which attaches to the cell wall, and a catalytic domain that breaks holes in the cell wall — effectively destroying the targeted bacteria.


 “The idea was: Could we use a Lego-like approach here? Could we take a binding domain from one enzyme and can we mix it with a binding domain or catalytic domain of another one?” Dordick said.


The issue of antibiotic resistant bacteria and disease is a serious one and of great concern to the medical community. If you’re a journalist covering this topic or are looking to know more about the ongoing research into this field – let our experts help.


Jonathan S. Dordick is the Howard P. Isermann Professor of Chemical and Biological Engineering at Rensselaer Polytechnic Institute where he is also the Senior Advisor to the President for Strategic Initiatives.  Dr. Dordick is available to speak with media regarding this topic - simply click on his icon to arrange an interview.




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  • Jonathan S. Dordick
    Jonathan S. Dordick Howard P. Isermann Professor, Chemical and Biological Engineering & Co-Director, Heparin Applied Research Center

    Applies biological principles to advance bioengineering and biomanufacturing, stem cell engineering, and drug discovery

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