ИСТИНА

Mycoplasma hominis is an opportunistic urogenital pathogen of vertebrates. It is a nonglycolytic species, producing energy through arginine degradation. Among the genital mycoplasmas, M. hominis is most commonly reported to play a role in systemic infections and can persist in the host for a long time. However, it is unclear how M. hominis proceeds under arginine-limitation. The recent metabolic reconstruction of M. hominis demonstrates the ability to catabolize deoxyribose-phosphate to produce ATP. In this study, we cultivate M. hominis on two different energy sources (arginine and thymidine) and demonstrate the difference in growth rate, antibiotic sensitivity, and biofilm formation. Using label-free quantitative proteomics, we compare the proteome of Mycoplasma hominis under these conditions. A total of 466 proteins are identified from M. hominis, representing approximately 85% of the predicted proteome. While the levels of 94 proteins change significantly. As expected, we found changes in the level of metabolic enzymes. The energy source strongly affects the synthesis of enzymes related to RNA modifications and ribosome assembly. The translocation of lipoproteins and other membrane-associated proteins is impaired. It is the first global characterization of the proteomic switching of Mycoplasma hominis in arginine-deficiency media illustrates energy source-dependent control of pathogenicity factors like lipoproteins. This study can help to find out mechanisms underlying of interaction between growth rate and fitness of genome-reduced bacteria. This work was supported by the Russian Science Foundation (project no.19-75-10124).