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Cited by 700Antimicrobial Resistance in StaphylococcusBacterial biofilms and quorum sensingBiochemical and Structural Characterization

The DOI matches its Crossref record; 71 of the 71 references it cites were found in a registry or an index.

Evidence for autolysin‐mediated primary attachment of Staphylococcus epidermidis to a polystyrene surface

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Heilmann, Christine, Hussain, Muzaffar, Peters, Georg, Götz, Friedrich·1997·Molecular Microbiology
DOI 10.1046/j.1365-2958.1997.4101774.x
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Abstract

Biofilm formation on a polymer surface which involves initial attachment and accumulation in multilayered cell clusters (intercellular adhesion) is proposed to be the major pathogenicity factor in Staphylococcus epidermidis foreign‐body‐associated infections. We have characterized two distinct classes of biofilm‐negative Tn 917 mutants in S. epidermidis affected in initial attachment (class A) or intercellular adhesion (class B). mut1 (class A mutant) lacks five surface‐associated proteins with molecular masses of 120, 60, 52, 45 and 38 kDa and could be complemented by transformation with a 16.4 kb wild‐type DNA fragment. The complemented mutant was able to attach to a polystyrene surface, to form a biofilm, and produced all of the proteins missing from mut1. Subcloning experiments revealed that the 60 kDa protein is sufficient for initial attachment. Immunofluorescence microscopy using an antiserum raised against the 60 kDa protein showed that this protein is located at the cell surface. DNA‐sequence analysis of the complementing region revealed a single open reading frame which consists of 4005 nucleotides and encodes a deduced protein of 1335 amino acids with a predicted molecular mass of 148 kDa. The amino acid sequence exhibits a high similarity (61% identical amino acids) to the atl gene product of Staphylococcus aureus, which represents the major autolysin; therefore the open reading frame was designated atlE. By analogy with the S. aureus autolysin, AtlE is composed of two bacteriolytically active domains, a 60 kDa amidase and a 52 kDa glucosaminidase domain, generated by proteolytic processing. The 120 kDa protein missing from mut1 presumably represents the unprocessed amidase and glucosaminidase domain after proteolytic cleavage of the signal‐ and propeptide. The 45 and 38 kDa proteins are probably the degradation products of the 60 and 52 kDa proteins, respectively. Additionally, AtlE was found to exhibit vitronectin‐binding activity, indicating that AtlE plays a role in binding of the cells not only to a naked polystyrene surface during early stages of adherence, but also to plasma protein‐coated polymer surfaces during later stages of adherence. Our findings provide evidence for a new function of an autolysin (AtlE) in mediating the attachment of bacterial cells to a polymer surface, representing the prerequisite for biofilm formation.

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Research works printed but not linked: 3

  1. C. Heilmann, M. Hussain, G. Peters, and F. Go ¨tz 13652958, 1997, 5, Downloaded from https://onlinelibrary.wiley.com/doi/10.1046/j.1365-2958.1997.4101774.x, Wiley Online Library on [19/08/2023]. See the Terms and Conditions (https://onlinelibrary.wiley.com/terms-and-conditions) on Wiley Online Library for rules of use; OA articles are governed by the applicable Creative Commons License
  2. Hayashi, M. (1993) Vitronectins: from vertebrates to inverte- brates. In Biology of Vitronectins and Their Receptors. Pre- issner, K.T., Rosenblatt, S., Kost, C., Wegerhoff, J., and Mosher, D.F (eds). Excerpta Medica Amsterdam, pp. 3- 11.
  3. ᮊ 1997 Blackwell Science Ltd, Molecular Microbiology, 24, 1013-1024 Initial attachment of Staphylococcus epidermidis 1023 13652958, 1997, 5, Downloaded from https://onlinelibrary.wiley.com/doi/10.1046/j.1365-2958.1997.4101774.x, Wiley Online Library on [19/08/2023]. See the Terms and Conditions (https://onlinelibrary.wiley.com/terms-and-conditions) on Wiley Online Library for rules of use; OA articles are governed by the applicable Creative Commons License

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Metadata

Authors
Heilmann, C., Hussain, M., Peters, G., & Götz, F.
Affiliations
University of Tübingen (DE)
Corresponding author
Götz, Friedrich
ORCID
Venue
Molecular Microbiology
Publisher
Wiley
Published
1997-06
Volume
24
Issue
5
Pages
1013-1024
ISSN
  • 0950-382X (ISSN-L)
  • 1365-2958
DOI
10.1046/j.1365-2958.1997.4101774.x
OpenAlex
W2061514792
Cited by
700
References
70
Citations by year
2026: 15 · 2025: 6 · 2024: 20 · 2023: 24 · 2022: 21 · 2021: 16 · 2020: 23 · 2019: 18 · 2018: 17 · 2017: 21 · 2016: 30 · 2015: 25 · 2014: 41 · 2013: 24 · 2012: 45
FWCI
14.58
Type
journal article
Language
en
Open access
Licence
onlinelibrary.wiley.com/termsAndConditions#vor (vor, 2343 d)
Locations
  • Molecular Microbiology (publishedVersion)
  • PubMed (publishedVersion)
Funders
Bundesministerium für Bildung und Forschung
Topics
  • Health Sciences › Medicine › Infectious Diseases › Antimicrobial Resistance in Staphylococcus
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Bacterial biofilms and quorum sensing
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
Keywords
Staphylococcus epidermidis, biofilm formation, cell-cell adhesion, foreign body-associated infections, vitronectin binding, surface-associated proteins, proteolytic processing
MeSH terms
Amino Acid Sequence, Bacterial Adhesion, Bacterial Proteins, Carrier Proteins, DNA Transposable Elements, DNA-Binding Proteins, DNA, Bacterial, Genetic Complementation Test, Membrane Proteins, Molecular Sequence Data, N-Acetylmuramoyl-L-alanine Amidase, Polystyrenes, Staphylococcus epidermidis, Mutagenesis, Insertional, Gene Deletion, Sequence Analysis, Adhesins, Bacterial

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