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Cited by 112Biochemical and Structural CharacterizationOral microbiology and periodontitis researchBacterial Genetics and Biotechnology

Cell Wall-Anchored CshA Polypeptide (259 Kilodaltons) in Streptococcus gordonii Forms Surface Fibrils That Confer Hydrophobic and Adhesive Properties

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McNab, Roderick, Forbes, Helen, Handley, Pauline S., Loach, Diane M., Tannock, Gerald W., Jenkinson, Howard F.·1999·Journal of Bacteriology
DOI 10.1128/jb.181.10.3087-3095.1999PMC PMC93763
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Abstract

It has been shown previously that inactivation of the cshA gene, encoding a major cell surface polypeptide (259 kDa) in the oral bacterium Streptococcus gordonii , generates mutants that are markedly reduced in hydrophobicity, deficient in binding to oral Actinomyces species and to human fibronectin, and unable to colonize the oral cavities of mice. We now show further that surface fibrils 60.7 ± 14.5 nm long, which are present on wild-type S. gordonii DL1 (Challis) cells, bind CshA-specific antibodies and are absent from the cell surfaces of cshA mutants. To more precisely determine the structural and functional properties of CshA, already inferred from insertional-mutagenesis experiments, we have cloned the entire cshA gene into the replicative plasmid pAM401 and expressed full-length CshA polypeptide on the cell surface of heterologous Enterococcus faecalis JH2-2. Enterococci expressing CshA exhibited a 30-fold increase in cell surface hydrophobicity over E. faecalis JH2-2 carrying the pAM401 vector alone and 2.4-fold-increased adhesion to human fibronectin. CshA expression in E. faecalis also promoted cell-cell aggregation and increased the ability of enterococci to bind Actinomyces naeslundii cells. Electron micrographs of negatively stained E. faecalis cells expressing CshA showed peritrichous surface fibrils 70.3 ± 9.1 nm long that were absent from control E. faecalis JH2-2(pAM401) cells. The fibrils bound CshA-specific antibodies, as detected by immunoelectron microscopy, and the antibodies inhibited the adhesion of E. faecalis cells to fibronectin. The results demonstrate that the CshA polypeptide is the structural and functional component of S. gordonii adhesive fibrils, and they provide a molecular basis for past correlations of surface fibril production, cell surface hydrophobicity, and adhesion in species of oral “ sanguis -like” streptococci.

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  • The hydrophobic character was reported as a feature of a number of Gram-positive bacteria which possess cell wall anchored proteins.

    “The hydrophobic character was reported as feature of a number of Gram-positive bacteria which possess cell wall anchored proteins [42,43].”

    From Positive role of cell wall anchored proteinase PrtP in adhesion of lactococci (2007) · cites this paper as [43]

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Authors
McNab, R., Forbes, H., Handley, P. S., Loach, D. M., Tannock, G. W., & Jenkinson, H. F.
Affiliations
  • Eastman Dental Hospital (GB)
  • University of Manchester (GB)
  • University of Otago (NZ)
  • University Of Bristol Dental Hospital (GB)
ORCID
Venue
Journal of Bacteriology
Publisher
American Society for Microbiology
Published
1999-05-15
Volume
181
Issue
10
Pages
3087-3095
ISSN
  • 0021-9193 (ISSN-L)
  • 1098-5530
DOI
10.1128/jb.181.10.3087-3095.1999
PMC
PMC93763
OpenAlex
W2099141841
Cited by
112
References
47
Citations by year
2024: 1 · 2023: 1 · 2021: 2 · 2020: 5 · 2019: 6 · 2018: 4 · 2017: 2 · 2016: 3 · 2015: 2 · 2014: 10 · 2013: 4 · 2012: 5
FWCI
2.07
Type
journal article
Language
en
Open access
Licence
journals.asm.org/non-commercial-tdm-license (tdm)
Locations
  • Journal of Bacteriology (publishedVersion)
  • Europe PMC (PubMed Central) (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
  • UCL Discovery (University College London) (submittedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
  • Health Sciences › Dentistry › Periodontics › Oral microbiology and periodontitis research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
Keywords
Streptococcus gordonii, cell surface hydrophobicity, bacterial adhesion, fibronectin binding, Actinomyces naeslundii, cell-cell aggregation, oral bacteria, oral colonization
MeSH terms
Actinomyces, Antibodies, Bacterial, Bacterial Adhesion, Bacterial Proteins, Cell Wall, Fibronectins, Humans, Membrane Proteins, Microscopy, Electron, Molecular Weight, Phenotype, Polymers, Protein Binding, Recombinant Proteins, Streptococcus, Enterococcus faecalis, Blotting, Western

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