Staphylococcus aureus expresses a panel of cell wall-anchored adhesins, including proteins belonging to the microbial surface components recognizing adhesive matrix molecule (MSCRAMM) family, exemplified by the serine-aspartate repeat protein D (SdrD), which serve key roles in colonization and infection. Deletion of sdrD from S. aureus subsp. aureus strain NCTC8325-4 attenuated bacterial survival in human whole blood ex vivo, which was associated with increased killing by human neutrophils. Remarkably, SdrD was able to inhibit innate immune-mediated bacterial killing independently of other S. aureus proteins, since addition of recombinant SdrD protein and heterologous expression of SdrD in Lactococcus lactis promoted bacterial survival in human blood. SdrD contributes to bacterial virulence in vivo, since fewer S. aureus subsp. aureus NCTC8325-4 ΔsdrD bacteria than bacteria of the parent strain were recovered from blood and several organs using a murine intravenous infection model. Collectively, our findings reveal a new property of SdrD as an important key contributor to S. aureus survival and the ability to escape the innate immune system in blood.
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Article Synopsis
- Staphylococcus aureus uses a family of adhesive proteins with serine-aspartate repeat (SDR) domains, such as ClfA, to initiate infection and colonize host tissues, with O-linked glycosylation by SdgB and SdgA being crucial for their virulence and protection against the host's immune response.
- This study reveals the crystal structures of SdgB and SdgA, showing how SdgB changes from open to closed conformation upon binding with ligands and functions in various forms, providing insights into their roles in glycosylation.
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