Nat Chem Biol: A new antibiotic binding site found in ribosomes

, July 4, 2020 /
bio-valley,,000-bio-valley/-- A team of scientists from Russia, Germany and the United States, led by Ilya Osterman, Petr Sergiev, Olga Dontova and Daniel Wilson of the University of Hamburg, led by scientists from the Skolkovo Institute for Science and TechnologyThey found that its effect sway was different from the well-known tetracycline, which offered good prospects for overcomingantibioticresistancebacteriabacteriaresistance toantibioticis one of the main problems in modern health careThe confrontation betweenbacterialandantibioticsdevelopers is like an arms race in which people can barely keep up with tiny parasitesMany traditional antibiotics no longer work on new strains, so scientists must come up with new methods The role of antibiotics is often designed to prevent the most important active processes of bacteria: the synthesis of nucleic acids, proteins and cell walls New antibiotics are usually similar to their previous products, so bacteria sooner or later they will find a weapon to fight them photo source: Aromatic polyenone antibiotics are the most famous class of antibiotics, including tetracycline antibiotics found in the mid-20th century, and penicillin antibiotics widely used in medicine Tetracenomycin is a relatively new aromatic polyketone compound Previously, they were thought to penetrate bacteria into DNA, disrupting the replication of bacteria (double dna when cells divide) However, researchers from the Center for Life Sciences at the Skolkovo Institute of Science and Technology and colleagues from Moscow State University and the University of Hamburg found that one of the family's representatives, Tetracenomycin X, can block the synthesis of proteins; " using cryogenic electron microscopes, it can be determined that the ribosome binding site of tetracycinomycin X is located in a tunnel structure of synthetic peptides leaving ribosomes, different from the well-known protein synthesis inhibitors, the Great Ring Esters and steptogramins B binding sites Lead researcher Ilya Osterman said results showed that Tetracenomycin X did not cross-resistant with known protein synthesis inhibitors, so the strains did not become resistant to them the new structural base sequence of the protein synthesis inhibitor and the new antibiotic binding sites on the ribosome may help develop new antimicrobial drugs The study was published in Nature Chemical Biology (biovalleybioon.com) References: A new antibiotic binding site for the a new antibiotic binding site for the the ribosome Tetracenomycin X inhibits translation by binding this ribosomal exit, Nature Chemical Biology, DOI: 10.1038/s41589-020-0578-x