With that prediction in hand, researchers were able to make specific mutations within the relevant pieces of the complex and validate Cong’s hypothesis in live bacteria. While it was already known that T4SS is involved in pilus assembly, Cong predicted how it occurs. Her computational analysis supported the cryo-EM data and suggested a hypothesis about the function of T4SS. Qian Cong, a computational biologist at UT Southwestern, then used her background in statistics and machine learning to analyze T4SS protein sequences from several bacteria to generate structural predictions, which were compared with the cryo-EM data. This study, published in Nature, now provides a blueprint that could help researchers design drugs that slow the development of antibiotic resistance genes.įirst, molecular biologists at the University of London used cryo-EM to elucidate the structure of T4SS-no small feat since the T4SS complex is larger than 99.6% of all those included to date in the worldwide library of protein structures. Scientists have long been searching for ways to shut down T4SS. The findings provide a blueprint that could help researchers design drugs that slow the development of antibiotic resistance genes.Īn international team of researchers has taken a key step forward in the fight against antibiotic resistance by elucidating the structure of the Type IV secretion system (T4SS), a protein complex on the outer envelope of bacterial cells that helps them exchange DNA with neighboring bacteria and resist antibiotics.For the first time, scientists determined the 3D structure of the entire T4SS complex.
T4SS helps bacteria spread drug resistance genes through the formation of a pilus to exchange DNA.
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