The antibiotic binding site found in the ribosome
The mechanism of tetracenomycin X – obstructing the process of bacterial protein synthesis was examined by a team of researchers from the USA, Russia, and Germany led by Skoltech researchers Ilya Osterman, Daniel Wilson, Olga Dontsova, and Petr Sergiev from Hamburg University. The researchers discovered that tetracenomycin X acts differently from the antibiotic Tetracycline that offers good prospects for overcoming bacterial antibiotic resistance.
One of the main issues of modern medication and healthcare is the resistance of bacteria to antibiotics. The conflict between antibiotics manufacturers and bacteria is like an arms race in which individuals are hardly keeping pace with microscopic parasites. Several conventional antibiotics are already inadequate against new strains of bacteria, so researchers need to think of something unique. Generally, Blocking the most essential processes of bacterial activity including the synthesis of the cell wall, proteins, and nucleic acids is the main focus of the antibiotics. Bacteria discover weapons against the new antibiotics as they are normally similar to their predecessors.
One of the most known groups of antibiotics is aromatic polyketides, which include tetracyclines – found in the mid-20th century, penicillin – extensively used in medication.
Tetracenomycin was formerly
thought to enter into bacterial DNA and cause disturbances in the replication of the cell. But, scientists from the Skoltech Center for Life Sciences, along with coworkers from the University of Hamburg and Moscow State University discovered that tetracenomycin X (one of the representatives of this family), obstructs protein synthesis. Additionally, it attaches to the large subunit of the ribosome, unlike tetracycline which binds to the small subunit.Skoltech principal researcher Ilya Osterman said it was possible to identify the binding site of tetracycinomycin X to the ribosome utilizing cryo-electron microscopy, it is present in the tunnel where the synthesized peptide leaves the ribosome, opposite the site in which the well-known protein synthesis inhibitors – macrolides and streptogramins B bind.
The outcomes show that bacterial strains will not be resistant to tetracenomycin X as it does not have cross-resistance with currently known protein synthesis inhibitors.
The new antibiotic binding site on the ribosome and new structural motif of the protein synthesis inhibitor might serve beneficial for the development of new antibacterial medicines.
The outcomes of the study are released in the journal Nature Chemical Biology.
Author: Sruthi S
