Sortase‐catalysed anchoring of surface proteins to the cell wall of Staphylococcus aureus
Open accessAbstract
Many surface proteins of Gram‐positive bacteria are anchored to the cell wall envelope by a transpeptidation mechanism, requiring a C‐terminal sorting signal with a conserved LPXTG motif. Sortase, a membrane protein of Staphylococcus aureus , cleaves polypeptides between the threonine and the glycine of the LPXTG motif and catalyses the formation of an amide bond between the carboxyl‐group of threonine and the amino‐group of peptidoglycan cross‐bridges. S. aureus mutants lacking the srtA gene fail to anchor and display some surface proteins and are impaired in the ability to cause animal infections. Sortase acts on surface proteins that are initiated into the secretion (Sec) pathway and have their signal peptide removed by signal peptidase. The S. aureus genome encodes two sets of sortase and secretion genes. It is conceivable that S. aureus has evolved more than one pathway for the transport of 20 surface proteins to the cell wall envelope.
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Based on the presence or absence of topogenic sequences, sortases can be divided into two classes.
“Based on the presence or absence of topogenic sequences, sortases can be divided into two classes.”
From Protein sorting to the cell wall envelope of Gram-positive bacteria (2004) · cites this paper as [41]
The “A second sortase gene (srtB)” section says that S. aureus has two sortase genes, srtA and srtB, and suggests their enzymes may act on different substrates. It does not classify sortases generally into two classes based on the presence or absence of topogenic sequences; no page number is available in our copy. (LLM, conf=0.76)
Experimental — accuracy not yet measuredEnzymes of the second class are mainly found encoded in the genomes of corynebacteria, enterococci and streptococci.
“Enzymes of the second class are mainly found encoded in the genomes of corynebacteria, enterococci and streptococci.”
From Protein sorting to the cell wall envelope of Gram-positive bacteria (2004) · cites this paper as [41]
The Sortase (SrtA) section lists Corynebacterium diphtheriae, Enterococcus faecalis and several streptococci among organisms with genes homologous to S. aureus srtA. The section on a second sortase gene discusses srtB in S. aureus, but does not say that this second class is found mainly in the three named groups. (LLM, conf=0.84)
Experimental — accuracy not yet measuredAll sortase homologs contain an active site signature motif, LXTC with conserved leucine (L), threonine (T), and cysteine (C) residues.
“All sortase homologs contain an active site signature motif, LXTC with conserved leucine (L), threonine (T), and cysteine (C) residues [41,42].”
From Protein sorting to the cell wall envelope of Gram-positive bacteria (2004) · cites this paper as [41]
The section “Sortase-catalysed cleavage at the LPXTG motif” (page unavailable) says that the active-site cysteine C184 is conserved within sortase genes. It does not identify an LXTC active-site motif or establish that leucine and threonine are conserved in all sortase homologs; its LPXTG motif is a signal on surface proteins, not a sortase active-site motif. (LLM, conf=0.84)
Experimental — accuracy not yet measuredThe major class of sortases encompasses enzymes with an N-terminal signal peptide/membrane anchor (class I).
“The major class of sortases encompasses enzymes with an N-terminal signal peptide/ membrane anchor (class I).”
From Protein sorting to the cell wall envelope of Gram-positive bacteria (2004) · cites this paper as [41]
The Sortase (SrtA) section describes SrtA as having a putative N-terminal membrane-spanning domain. Our copy does not classify sortases as “class I” or say that this is the major class; its references to signal peptides concern the surface-protein substrates, not sortase enzymes. No page number is available in our copy. (LLM, conf=0.86)
Experimental — accuracy not yet measuredAfter protein translocation through the membrane, the sortase enzyme mediates cleavage of LPXTG such that the threonine carboxyl group is linked to the cross-bridges in the peptidoglycan layer.
“After protein translocation through the membrane, the sortase enzyme mediates cleavage of LPXTG such that the threonine carboxyl group is linked to the cross-bridges in the peptidoglycan layer [26].”
From Positive role of cell wall anchored proteinase PrtP in adhesion of lactococci (2007) · cites this paper as [26]
The second, minor class is formed by sortases with an N-terminal signal peptide and a C-terminal membrane anchor (class II).
“The second, minor class is formed by sortases with an N-terminal signal peptide and a C-terminal membrane anchor (class II) [41].”
From Protein sorting to the cell wall envelope of Gram-positive bacteria (2004) · cites this paper as [41]
The “A second sortase gene (srtB)” section identifies a second sortase gene in S. aureus, but does not classify sortases by membrane topology. Searches for “class II,” “minor class,” and a sortase with an N-terminal signal peptide and C-terminal membrane anchor found no passage stating the claimed classification; the paper instead describes an N-terminal membrane anchor for SrtA. (LLM, conf=0.76)
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References 79 · Cited by 387
- Authors
- Mazmanian, S. K., Ton‐That, H., & Schneewind, O.
- Affiliations
- University of California, Los Angeles (US)
- Corresponding author
- Schneewind, Olaf
- Venue
- Molecular Microbiology
- Publisher
- Wiley
- Published
- 2001-06
- Volume
- 40
- Issue
- 5
- Pages
- 1049-1057
- ISSN
- 0950-382X (ISSN-L)
- 1365-2958
- OpenAlex
- W2075952240
- Cited by
- 387
- References
- 79
- Citations by year
- 2026: 15 · 2025: 14 · 2024: 6 · 2023: 10 · 2022: 14 · 2021: 15 · 2020: 8 · 2019: 15 · 2018: 10 · 2017: 8 · 2016: 18 · 2015: 15 · 2014: 25 · 2013: 16 · 2012: 9
- FWCI
- 1.61
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Molecular Microbiology (publishedVersion)
- PubMed (publishedVersion)
- CaltechAUTHORS (California Institute of Technology) (submittedVersion)
- Funders
- National Institutes of Health
- National Institute of General Medical Sciences (T32GM007104, GM 07104)
- National Institute of Allergy and Infectious Diseases (AI33987, AI 07323)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
- Health Sciences › Medicine › Infectious Diseases › Antimicrobial Resistance in Staphylococcus
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Keywords
- sortase, Staphylococcus aureus, LPXTG motif, transpeptidation, signal peptidase, protein sorting, virulence
- MeSH terms
- Amino Acid Sequence, Bacterial Outer Membrane Proteins, Bacterial Proteins, Cell Wall, Cysteine Endopeptidases, Molecular Sequence Data, Peptidoglycan, Staphylococcal Protein A, Staphylococcus aureus, Gene Expression Regulation, Bacterial, Aminoacyltransferases, Amino Acid Motifs
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