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Detailed mutational analysis of Vga(A) interdomain linker: implication for antibiotic resistance specificity and mechanism.

ABSTRACT: Detailed mutational analysis examines the roles of individual residues of the Vga(A) linker in determining the antibiotic resistance phenotype. It defines a narrowed region of residues 212 to 220 whose composition determines the resistance specificity to lincosamides, pleuromutilins, and/or streptogramins A. From the analogy with the recently described function of the homologous ABC-F protein EttA as a translational factor, we infer that the Vga(A) linker interacts with the ribosome and directly or indirectly affects the binding of the respective antibiotic.

SUBMITTER: Lenart J

PROVIDER: S-EPMC4335903 | biostudies-literature | 2015 Feb

REPOSITORIES: biostudies-literature

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Detailed mutational analysis of Vga(A) interdomain linker: implication for antibiotic resistance specificity and mechanism.

Lenart Jakub J Vimberg Vladimir V Vesela Ludmila L Janata Jiri J Balikova Novotna Gabriela G

Antimicrobial agents and chemotherapy 20141215 2

Detailed mutational analysis examines the roles of individual residues of the Vga(A) linker in determining the antibiotic resistance phenotype. It defines a narrowed region of residues 212 to 220 whose composition determines the resistance specificity to lincosamides, pleuromutilins, and/or streptogramins A. From the analogy with the recently described function of the homologous ABC-F protein EttA as a translational factor, we infer that the Vga(A) linker interacts with the ribosome and directly ...[more]

PMID: 25512423

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