The DOI matches its Crossref record; 227 of the 227 references it cites were found in a registry or an index.
Sortases and the Art of Anchoring Proteins to the Envelopes of Gram-Positive Bacteria
Open accessAbstract
SUMMARY: The cell wall envelopes of gram-positive bacteria represent a surface organelle that not only functions as a cytoskeletal element but also promotes interactions between bacteria and their environment. Cell wall peptidoglycan is covalently and noncovalently decorated with teichoic acids, polysaccharides, and proteins. The sum of these molecular decorations provides bacterial envelopes with species- and strain-specific properties that are ultimately responsible for bacterial virulence, interactions with host immune systems, and the development of disease symptoms or successful outcomes of infections. Surface proteins typically carry two topogenic sequences, i.e., N-terminal signal peptides and C-terminal sorting signals. Sortases catalyze a transpeptidation reaction by first cleaving a surface protein substrate at the cell wall sorting signal. The resulting acyl enzyme intermediates between sortases and their substrates are then resolved by the nucleophilic attack of amino groups, typically provided by the cell wall cross bridges of peptidoglycan precursors. The surface protein linked to peptidoglycan is then incorporated into the envelope and displayed on the microbial surface. This review focuses on the mechanisms of surface protein anchoring to the cell wall envelope by sortases and the role that these enzymes play in bacterial physiology and pathogenesis.
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Metadata
- Authors
- Marraffini, L. A., DeDent, A. C., & Schneewind, O.
- Venue
- Microbiology and Molecular Biology Reviews
- Publisher
- American Society for Microbiology
- Published
- 2006-03
- Volume
- 70
- Issue
- 1
- Pages
- 192-221
- ISSN
- 1092-2172 (ISSN-L)
- 1098-5557
- OpenAlex
- W2116103187
- Cited by
- 686
- References
- 227
- FWCI
- 2.50
- Type
- journal article
- Language
- en
- Open access
- green
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