Resistance to antibiotics is a severe problem in contemporary medicine. Many antibiotics inhibit protein biosynthesis by hampering the ribosome function. Structures of bacterial ribosomes in complex with these antibiotics illuminated common pathways of antibiotics inhibitory action, but not the species-specific diversity in infectious-diseases susceptibility.

Recent structural studies on ribosome from a multi-resistant pathogenic bacterium and careful comparisons to ribosomes from non-pathogenic bacteria revealed novel structural motifs, essential to protein biosynthesis but not located in the primary ribosomal active sites, hence no mechanism for modification leading to resistance of these sites is currently known. These led to the design of antibiotics with desired properties that can be optimized in terms of their chemical properties, toxicity and penetration, alongside species-specificity, thus preserving the microbiome, as well as in terms of bio degradability, thus reducing the ecological hazards caused by the spread of the current antibiotics’ metabolites.

Prof. Dr. Ada Yonath

Nobel laureate Ada Yonath is Martin S. and Helen Kimmel Professor of Structural Biology and Director of the Helen and Milton A. Kimmelman Center for Biomolecular Structure and Assembly at the Weizmann Institute of Science in Rechovot, Israel. She has been awarded numerous prizes and honorary doctorates and is member of many national academies of science, including the German National Academy of Sciences Leopoldina. In the year 2009, Yonath won the Nobel Prize for Chemistry, sharing it with Venkatraman Ramakrishnan and Thomas A. Steitz. The Nobel committee honoured their “studies of the structure and function of the ribosome”. Ada Yonath pioneered the use of X-ray crystallography in her field in Israel, and after decades of work she discovered the atomic structure of the ribosome, as well as the action of several antibiotics targeting the ribosome.