Mazmanian, Sarkis K. and Ton-That, Hung and Su, Kenneth and Schneewind, Olaf (2002) An iron-regulated sortase anchors a class of surface protein during Staphylococcus aureus pathogenesis. Proceedings of the National Academy of Sciences of the United States of America, 99 (4). pp. 2293-2298. ISSN 0027-8424 http://resolver.caltech.edu/CaltechAUTHORS:MAZpnas02
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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.
|Additional Information:||Copyright © 2002 by the National Academy of Sciences Edited by Christopher T. Walsh, Harvard Medical School, Boston, MA, and approved December 13, 2001 (received for review October 3, 2001). Published online before print February 5, 2002, 10.1073/pnas.032523999 We thank Simon Foster (University of Sheffield) for materials. S.K.M. acknowledges support from the Predoctoral Training Program in Genetics (T32GM07104) at the University of California, Los Angeles. Work in the O.S. laboratory is supported by National Institutes of Health-National Institute of Allergy and Infectious Diseases, Infectious Disease Branch Grant AI33987. This paper was submitted directly (Track II) to the PNAS office.|
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|Deposited On:||10 Nov 2006|
|Last Modified:||26 Dec 2012 09:16|
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