Cited by 426Biochemical and Structural CharacterizationBacterial Genetics and BiotechnologyAntimicrobial Resistance in Staphylococcus

Cell wall sorting signals in surface proteins of gram‐positive bacteria.

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Schneewind, O., Mihaylova‐Petkov, D., Model, P.·1993·The EMBO Journal

Abstract

Staphylococcal protein A is anchored to the cell wall, a unique cellular compartment of Gram-positive bacteria. The sorting signal sufficient for cell wall anchoring consists of an LPXTG motif, a C-terminal hydrophobic domain and a charged tail. Homologous sequences are found in many surface proteins of Gram-positive bacteria and we explored the universality of these sequences to serve as cell wall sorting signals. We show that several signals are able to anchor fusion proteins to the staphylococcal cell wall. Some signals do not sort effectively, but acquire sorting activity once the spacing between the LPXTG motif and the charged tail has been increased to span the same length as in protein A. Thus, signals for cell wall anchoring in Gram-positive bacteria are as universal as signal (leader) sequences.

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Crossref · 10.1002/j.1460-2075.1993.tb06169.x

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  • The C-terminal cell wall sorting signal of staphylococcal protein A encompasses a 35-residue peptide with an LPXTG motif, followed by a hydrophobic domain and a positively charged tail.

    “The C-terminal cell wall sorting signal of staphylococcal protein A encompasses a 35-residue peptide with an LPXTG motif, followed by a hydrophobic domain and a positively charged tail [20].”
  • Lysozyme, an N-acetyl-muramidase that cuts the glycan strands, releases protein A molecules as a spectrum of fragments with different mass due to the presence of linked peptidoglycan fragments of different sizes.

    “Lysozyme, an N-acetyl-muramidase that cuts the glycan strands [19], releases protein A molecules as a spectrum of fragments with different mass due to the presence of linked peptidoglycan fragments of different sizes [16,20,21].”
  • When fused to the C-terminus of polypeptides, the cell wall sorting signal alone is sufficient to cause cell wall anchoring of hybrid proteins that are initiated into the secretory pathway of S. aureus via an N-terminal signal peptide.

    “When fused to the C-terminus of polypeptides, the cell wall sorting signal alone is sufficient to cause cell wall anchoring of hybrid proteins that are initiated into the secretory pathway of S. aureus via an N-terminal signal peptide [13,20,32 -34].”
  • Sorting signals from one bacterial species can be functional in another microbe.

    “Moreover, sorting signals from one bacterial species can be functional in another microbe [20].”

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References 57 · Cited by 426

Research works printed but not linked: 5

  1. [2]2. Blobel,G. (1980) Proc. Natl Acad. Sci. USA, 77, 1496-1500.
  2. [30]30. Kreiswirth,B.N., Lofdahl,S., Betley,M.J., O'Reilly,M., Schlievert,P.M., Bergdoll,M.S. and Novick,R.P. (1983) Nature, 305, 709-712.
  3. [41]41. Ranelli,D.M., Jones,C.L., Johns,M.B., Mussey,G.J. and Khan,S.A. (1985) Proc. Natl Acad. Sci. USA, 82, 5850-5854.
  4. [42]42. Schindler,C.A. and Schuhardt,V.T. (1964) Proc. NatlAcad. Sci. USA, 51, 414-421.
  5. [45]45. Signas,C., Raucci,G., Jonsson,K., Lindgren,P.-E., Anantharamaiah,G.M., Hook,M. and Lindberg, M. (1989) Proc. Natl Acad. Sci. USA, 86, 699-703.

Authors
Schneewind, O., Mihaylova‐Petkov, D., & Model, P.
Affiliations
University of California, Los Angeles (US)
Venue
The EMBO Journal
Published
1993-12-01
Volume
12
Issue
12
Pages
4803-4811
ISSN
  • 0261-4189 (ISSN-L)
  • 1460-2075
OpenAlex
W184263843
Cited by
426
References
57
Citations by year
2026: 2 · 2025: 1 · 2024: 6 · 2023: 5 · 2022: 6 · 2021: 7 · 2020: 10 · 2019: 17 · 2018: 10 · 2017: 9 · 2016: 16 · 2015: 12 · 2014: 23 · 2013: 9 · 2012: 10
FWCI
4.00
Type
journal article
Language
en
Open access
Locations
  • The EMBO Journal (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • National Science Foundation (8817641)
  • National Institutes of Health (5r29ai033985-04)
  • National Institute of Allergy and Infectious Diseases (AI33985)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
  • Health Sciences › Medicine › Infectious Diseases › Antimicrobial Resistance in Staphylococcus
Keywords
LPXTG motif, protein A, cell wall anchoring, Gram-positive bacteria, surface proteins, fusion protein
MeSH terms
Amino Acid Sequence, Base Sequence, Cell Wall, DNA, Bacterial, Enterotoxins, Biological Evolution, Gram-Positive Bacteria, Molecular Sequence Data, Staphylococcal Protein A, Signal Transduction, Conserved Sequence

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