It's a fascinating discovery made at Ohio State University, which is featured in the Aug. 14 issue of Nature Chemical Biology. This discovery shows how bacteria make tweaks in their genes, and their proteins to gain strength.
The team includes research scientist Herve Roy, who joined the University of Central Florida faculty at the College of Medicine this month. He co-authored the paper after conducting research in OSU Professor Michael Ibba's lab.
"Mother Nature tinkers a lot," Roy said from his new lab in Orlando. "Our recent findings illustrate that new proteins in living organisms often evolve from older pre-existing ones, and that evolution updates biochemical mechanisms of living cells by tweaking them a little by applying molecular patches."
The precise role of one protein in bacteria, EF-P, remains a mystery, but this team found that it plays an essential role in the virulence of Salmonella enterica typhimurium, a common foodborne pathogen causing diarrhea, fever, and abdominal cramps, and occasionally lifetime chronic arthritis. Salmonella also accounts for about 400 deaths each year in the United States.
EF-P is known to play a role in protein biosynthesis, which is a keystone mechanism present in all organisms. This process is the chain assembly line that decodes the blue prints stored in the genomes of living organisms, to make all the proteins necessary to sustain life.
The team's research identified a modification born by EF-P that acts as a molecular patch on protein synthesis. The patch seems to increase the bacteria's prowess. Interestingly, the modification on EF-P is made by a hijacked protein, normally involved in the protein synthesis machinery itself.
In the Aug. 14 issue of Nature Chemical Biology, Roy and co-authors identified the chemical nature of the modification that occurs on EF-P. This is critical because in the team's experiments, when the modified version of EF-P is absent, Salmonella doesn't spread.
Because the mechanism by which the modification occurs is unique to bacteria and this system is involved in virulence it could be a potential drug target, Ibba said.
Roy's experience and interest in this area is what drew him to UCF. His lab in the Burnett School of Biomedical Sciences at UCF will use National Institutes of Health funding to explore how some other components of the protein synthesis machinery have been hijacked to accomplish alternate cellular processes. For instance, one process utilizes parts of the protein synthesis machinery to modify components of the bacterial membrane. This mechanism increases bacterial resistance to a large spectrum of antibiotics and presents a good avenue for new drugs that could potentially alleviate or cure many infectious diseases.
"That's why I came to UCF," Roy said. "There is a good team of scientists here working in infectious diseases. There is a good opportunity to collaborate and make a difference."
Other authors on the Nature paper include S. Betty Zou and William W. Navarre from the University of Toronto and Ibba, Tammy J. Bullwinkle, Marla S. Gilreath Benjamin S. Wolfe and Craig J. Forsyth from Ohio State University.
Roy received a Ph.D. in Structural Biochemistry and Molecular Biology from Louis Pasteur University in Strasbourg, France. He spent the past eight years as a post -doctoral research associate and research scientist at The Ohio State University in the laboratory of Dr. Ibba.
UCF Stands For Opportunity --The University of Central Florida is a metropolitan research university that ranks as the second largest in the nation with more than 56,000 students. UCF's first classes were offered in 1968. The university offers impressive academic and research environments that power the region's economic development. UCF's culture of opportunity is driven by our diversity, Orlando environment, history of entrepreneurship and our youth, relevance and energy. For more information visit http://news.ucf.edu
Zenaida Gonzalez Kotala | EurekAlert!
Hunting pathogens at full force
22.03.2017 | Helmholtz-Zentrum für Infektionsforschung
A 155 carat diamond with 92 mm diameter
22.03.2017 | Universität Augsburg
Astronomers from Bonn and Tautenburg in Thuringia (Germany) used the 100-m radio telescope at Effelsberg to observe several galaxy clusters. At the edges of these large accumulations of dark matter, stellar systems (galaxies), hot gas, and charged particles, they found magnetic fields that are exceptionally ordered over distances of many million light years. This makes them the most extended magnetic fields in the universe known so far.
The results will be published on March 22 in the journal „Astronomy & Astrophysics“.
Galaxy clusters are the largest gravitationally bound structures in the universe. With a typical extent of about 10 million light years, i.e. 100 times the...
Researchers at the Goethe University Frankfurt, together with partners from the University of Tübingen in Germany and Queen Mary University as well as Francis Crick Institute from London (UK) have developed a novel technology to decipher the secret ubiquitin code.
Ubiquitin is a small protein that can be linked to other cellular proteins, thereby controlling and modulating their functions. The attachment occurs in many...
In the eternal search for next generation high-efficiency solar cells and LEDs, scientists at Los Alamos National Laboratory and their partners are creating...
Silicon nanosheets are thin, two-dimensional layers with exceptional optoelectronic properties very similar to those of graphene. Albeit, the nanosheets are less stable. Now researchers at the Technical University of Munich (TUM) have, for the first time ever, produced a composite material combining silicon nanosheets and a polymer that is both UV-resistant and easy to process. This brings the scientists a significant step closer to industrial applications like flexible displays and photosensors.
Silicon nanosheets are thin, two-dimensional layers with exceptional optoelectronic properties very similar to those of graphene. Albeit, the nanosheets are...
Enzymes behave differently in a test tube compared with the molecular scrum of a living cell. Chemists from the University of Basel have now been able to simulate these confined natural conditions in artificial vesicles for the first time. As reported in the academic journal Small, the results are offering better insight into the development of nanoreactors and artificial organelles.
Enzymes behave differently in a test tube compared with the molecular scrum of a living cell. Chemists from the University of Basel have now been able to...
20.03.2017 | Event News
14.03.2017 | Event News
07.03.2017 | Event News
22.03.2017 | Materials Sciences
22.03.2017 | Physics and Astronomy
22.03.2017 | Materials Sciences