Abstract:
:Infection of host tissues by Staphylococcus aureus and S. epidermidis requires an unusual family of staphylococcal adhesive proteins that contain long stretches of serine-aspartate dipeptide-repeats (SDR). The prototype member of this family is clumping factor A (ClfA), a key virulence factor that mediates adhesion to host tissues by binding to extracellular matrix proteins such as fibrinogen. However, the biological siginificance of the SDR-domain and its implication for pathogenesis remain poorly understood. Here, we identified two novel bacterial glycosyltransferases, SdgA and SdgB, which modify all SDR-proteins in these two bacterial species. Genetic and biochemical data demonstrated that these two glycosyltransferases directly bind and covalently link N-acetylglucosamine (GlcNAc) moieties to the SDR-domain in a step-wise manner, with SdgB appending the sugar residues proximal to the target Ser-Asp repeats, followed by additional modification by SdgA. GlcNAc-modification of SDR-proteins by SdgB creates an immunodominant epitope for highly opsonic human antibodies, which represent up to 1% of total human IgG. Deletion of these glycosyltransferases renders SDR-proteins vulnerable to proteolysis by human neutrophil-derived cathepsin G. Thus, SdgA and SdgB glycosylate staphylococcal SDR-proteins, which protects them against host proteolytic activity, and yet generates major eptopes for the human anti-staphylococcal antibody response, which may represent an ongoing competition between host and pathogen.
journal_name
PLoS Pathogjournal_title
PLoS pathogensauthors
Hazenbos WL,Kajihara KK,Vandlen R,Morisaki JH,Lehar SM,Kwakkenbos MJ,Beaumont T,Bakker AQ,Phung Q,Swem LR,Ramakrishnan S,Kim J,Xu M,Shah IM,Diep BA,Sai T,Sebrell A,Khalfin Y,Oh A,Koth C,Lin SJ,Lee BC,Strandh Mdoi
10.1371/journal.ppat.1003653subject
Has Abstractpub_date
2013-01-01 00:00:00pages
e1003653issue
10eissn
1553-7366issn
1553-7374pii
PPATHOGENS-D-12-02552journal_volume
9pub_type
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