Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 99, Issue 4, Pages 2293-2298Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.032523999
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- NIAID NIH HHS [AI33987] Funding Source: Medline
- NIGMS NIH HHS [T32 GM007104, T32GM07104] Funding Source: Medline
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Sortase (SrtA), an enzyme that anchors surface proteins to the cell wail 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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