Staphylococcus aureus sortase mutants defective in the display of surface proteins and in the pathogenesis of animal infections.
نویسندگان
چکیده
Many gram-positive bacteria covalently tether their surface adhesins to the cell wall peptidoglycan. We find that surface proteins of Staphylococcus aureus are linked to the cell wall by sortase, an enzyme that cleaves polypeptides at a conserved LPXTG motif. S. aureus mutants lacking sortase fail to process and display surface proteins and are defective in the establishment of infections. Thus, the cell wall envelope of gram-positive bacteria represents a surface organelle responsible for interactions with the host environment during the pathogenesis of bacterial infections.
منابع مشابه
An iron-regulated sortase anchors a class of surface protein during Staphylococcus aureus pathogenesis.
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 ...
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molecules with important functions, such as adherence, invasion, signaling, and interaction with the host immune system or the environment. In Gram-positive bacteria, many surface proteins are anchored to the cell wall envelope by an enzyme called sortase, which recognizes a conserved carboxylic sorting motif. Two sortase isoforms, sortase A (SrtA) and sortase B (SrtB), have been identified in ...
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ورودعنوان ژورنال:
- Proceedings of the National Academy of Sciences of the United States of America
دوره 97 10 شماره
صفحات -
تاریخ انتشار 2000