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Characterization of a Novel Gene, srpa, Conferring Resistance to Streptogramin A, Pleuromutilins, and Lincosamides in Streptococcus suis

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Engineering 2022年第2期8卷 85-94页

作者： Chaoyang Zhang Lu Liu Peng Zhang Jingpo Cui Xiaoxia Qin Lichao Ma Kun Han Zhanhui Wang Shaolin Wang Shuangyang Ding Zhangqi Shen College of Veterinary Medicine China Agricultural UniversityBeijing 100193China Beijing Key Laboratory of Detection Technology for Animal-Derived Food Safety and Beijing Laboratory for Food Quality and Safety China Agricultural UniversityBeijing 100193China

Antimicrobial resistance is undoubtedly one of the greatest global health threats. The emergence of multidrug-resistant(MDR) Gram-positive pathogens, such as methicillin-resistant Staphylococcus aureus(MRSA), vancomycin-resistant Enterococcus faecium(VRE), and β-lactamase-resistant Streptococcus pneumonia, has severely limited our antibiotic arsenal. Numerous ribosome-targeting antibiotics, especially pleuromutilins, oxazolidinones, and streptogramins, are viewed as promising alternatives against aggressive MDR pathogens. In this study, we identified a new adenosine triphosphate(ATP)-binding cassete(ABC)-F family determinant, srp A, in Streptococcus suis(S. suis) by means of a comparative analysis of the whole-genome sequences of tiamulin(TIA)-resistant and TIA-sensitive bacteria. Functional cloning confirmed that the deduced gene can mediate cross-resistance to pleuromutilins, lincosamides, and streptogramin A in S. suis and S. aureus. A sequence alignment revealed that Srp A shares the highest amino acid identity with Vga(E)(36%) and shows canonical characteristics of ABC-F family *** Srp A-ribosome docked compounds, the extended loop region of Srp A approaches the valnemulinbinding pocket in the ribosome peptidyl-transferase center and competes with bound valnemulin. A detailed mutational analysis of the loop residues confirmed that this domain is crucial for Srp A activity,as substitutions or truncations of this region affect the efficiency and specificity of antibiotic *** antibiotics accumulation indicated that Srp A does not act as an efflux pump, while a ribosome binding assay supported the protective effects of Srp A on the ribosome by preventing antibiotic binding as well as displacing bound drugs. These findings clarify the mechanisms underlying resistance to ribosomal antibiotics.

关键词： srpa Streptococcus suis Antibiotic resistance Ribosome ABC-F family proteins

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