Protein controls the proliferation of bacteria: the future of new antibiotics

A team of scientists from Johns Hopkins University has solved the important problem of how certain proteins direct the process of bacterial proliferation. This finding may lead to a new antibiotic.

In the Current Biology publication, scientists have reported how a belt-shaped structure called a Z ring, which binds rod-shaped bacteria to separate into two individual animals, can suffer from a protein called MinC disabled. By exploiting this vulnerability, scientists say pharmaceutical companies can find ways to combat infectious diseases that old therapies are no longer effective.

According to Alex Dajkovic, the lead author of the study 'Potential medical applications from our findings are very important. Because the molecules involved in cell division are almost the same in most bacteria, the process we discovered brought new goals for those who produce antibiotics. This is extremely important because antibiotic resistance is increasing, and many deaths can be prevented, especially in developing countries, all caused by bacterial infectious diseases. '

Dajkovic participated in the discovery as a postdoctoral researcher in the laboratory of Denis Wirtz, a professor of molecular and chemical biology engineering at Johns Hopkins University's Whiting School of Engineering. Dajkovic is currently a researcher at the Curie Institute in Paris.

Wirtz, currently deputy director of the Johns Hopkins Nanotechnology Biotechnology Research Institute, notes that 'most antibiotics target the ability of bacteria to build cell membranes or produce proteins or DNA. In this work, Alex and colleagues identified new molecular targets that could disrupt cell division. If bacteria cannot reproduce, infectious diseases will be extinguished. '

Will there be a new antibiotic in the future?(Photo: wordpress.com)

The researchers focused on rodent E. coli bacteria, commonly found in the human gastrointestinal tract, which serve as a model organism for basic bacterial research processes. When these single-celled organisms want to multiply, a structure called the Z ring forms, then binds like a rubber band around the middle of the bacteria. The Z ring helps divide this rod-shaped body into two bacteria sections that will then split and form two new cells.

For about 20 years, scientists have known about the Z ring but still do not understand exactly how it works and why it is always formed in the middle of rod cells. The main component of Z rings is the protein molecule called FtsZ.

In the new paper, scientists from Johns Hopkins may for the first time report that the change of FtsZ fibers from liquid to more solid inside the cell is important for Z ring formation. They discovered that FtsZ fibers were woven into a frame or scaffold that could retain all other molecules involved in cell division. Ftsz fibers can weave this carpet because they tend to attract each molecule and interact along the length of the yarn.

The team also found MinC, another protein inside the cell, destroyed this structure by liquefying the structure used to form the ring Z. 'MinC blocks the attraction between FtsZ fibers along the fiber length. and it also makes the fiber more fragile. This has the effect of tearing the weave in the carpet of the Z ring, causing the whole structure to collapse. '

MinC has the most at the end outside rod-shaped bacterial cells, and this explains why the Z ring always forms and separates cells in the middle, where it is less likely to encounter protein enemies of me Team members also said the finding offers a promising opportunity: a new drug that mimics the effects of MinC may interfere with bacterial reproduction and thus end infectious disease.

This work is funded by the National Institutes of Health.