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Proc Natl Acad Sci U S A. 2002 Feb 19;99(4):2293-8. Epub 2002 Feb 5.

An iron-regulated sortase anchors a class of surface protein during Staphylococcus aureus pathogenesis.

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  • 1Committee on Microbiology, Department of Molecular Genetics and Cell Biology, University of Chicago, 920 58th Street, Chicago, IL 60637, USA.


Sortase (SrtA), an enzyme that anchors surface proteins to the cell wall of Gram-positive bacteria, cleaves sorting signals at the LPXTG motif. We have identified a second sortase (SrtB) in the Gram-positive pathogen Staphylococcus aureus that is required for anchoring of a surface protein with a NPQTN motif. Purified SrtB cleaves NPQTN-bearing peptides in vitro, and a srtB mutant is defective in the persistence of animal infections. srtB is part of an iron-regulated locus called iron-responsive surface determinants (isd), which also contains a ferrichrome transporter and surface proteins with NPQTN and LPXTG motifs. Cell wall-anchored surface proteins and the isd locus seem involved in a novel mechanism of iron acquisition that is important for bacterial pathogenesis.

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