Structural basis for SdgB- and SdgA-mediated glycosylation of staphylococcal adhesive proteins.

ABSTRACT: The initiation of infection of host tissues by Staphylococcus aureus requires a family of staphylococcal adhesive proteins containing serine-aspartate repeat (SDR) domains, such as ClfA. The O-linked glycosylation of the long-chain SDR domain mediated by SdgB and SdgA is a key virulence factor that protects the adhesive SDR proteins against host proteolytic attack in order to promote successful tissue colonization, and has also been implicated in staphylococcal agglutination, which leads to sepsis and an immunodominant epitope for a strong antibody response. Despite the biological significance of these two glycosyltransferases involved in pathogenicity and avoidance of the host innate immune response, their structures and the molecular basis of their activity have not been investigated. Th

SUBMITTER: Kim DG 

PROVIDER: S-EPMC8561734 | biostudies-literature | 2021 Nov

REPOSITORIES: biostudies-literature