Cited by 53Bacterial biofilms and quorum sensingEscherichia coli research studiesBiochemical and Structural Characterization

Pleiotrophic Effects of 2 Enterococcus faecalis sagA–Like Genes,salA and salB,Which Encode Proteins That Are Antigenic during Human Infection, on Biofilm Formation and Binding to Collagen Type I and Fibronectin

Mohamed, Jamal A., Teng, Fang, Nallapareddy, Sreedhar R., Murray, Barbara E.·2006·The Journal of Infectious Diseases

Abstract

BACKGROUND: We have shown previously that Enterococcus faecium SagA has broad-spectrum binding to extracellular matrix (ECM) proteins. In the present study, 2 sagA-like genes, salA and salB, were identified in Enterococcus faecalis. METHODS: We compared the salA and salB mutants; their parental strain, OG1RF; and the salB-complemented strain for binding to ECM proteins and biofilm formation. RESULTS: The salB mutant (TX5123) grew more slowly but showed greater binding (approximately 10%-20% of cells bound) to fibronectin (FN) and collagen type I (CI) than did OG1RF (approximately 1% of cells bound) (P<.001). Although TX5123 showed decreased biofilm formation in tryptic soy broth plus 0.25% glucose (TSBG) (P<.001 vs. OG1RF), a marked increase in biofilm formation was shown by TX5123 but not by OG1RF when they were grown in TSBG plus horse serum (HS) or TSBG plus FN, and the increase was coincident with increased attachment and hydrophobicity of TX5123. Complementation of the salB mutant restored the wild-type phenotypes. CONCLUSIONS: Whether SalB expression is ever sufficiently low in vivo to enhance adherence to ECM proteins or the serum-elicited increase in biofilm formation seen with the salB mutant in vitro is not currently known, but it is a potential way in which this organism could increase its adherence and biofilm formation during infection.

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Crossref · 10.1086/498871

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  • No direct orthologs of SagA are found in E. faecalis, and the two most similar conserved enzymes SalA and SalB possess distinct C-terminal domains.

    “No direct orthologs were found in E. faecalis, and the two most similar conserved enzymes, sagA-like proteins A and B (SalA and SalB) (23), possessed distinct C-terminal domains.”

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Authors
Mohamed, J. A., Teng, F., Nallapareddy, S. R., & Murray, B. E.
Venue
The Journal of Infectious Diseases
Published
2006-01-15
Volume
193
Issue
2
Pages
231-240
ISSN
  • 0022-1899 (ISSN-L)
  • 1537-6613
OpenAlex
W2108167397
Cited by
53
References
24
Citations by year
2025: 1 · 2024: 3 · 2022: 1 · 2021: 2 · 2020: 2 · 2019: 7 · 2018: 1 · 2017: 2 · 2016: 3 · 2015: 6 · 2014: 3 · 2013: 3 · 2012: 1
FWCI
1.12
Type
journal article
Language
en
Open access
closed
Locations
  • The Journal of Infectious Diseases (publishedVersion)
  • PubMed (publishedVersion)
Funders
National Institute of Allergy and Infectious Diseases (R37AI047923)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Bacterial biofilms and quorum sensing
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Endocrinology › Escherichia coli research studies
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
Keywords
Enterococcus faecalis, Sala, biofilm formation, fibronectin binding, extracellular matrix proteins, bacterial adhesion, antigenic proteins, gene complementation
MeSH terms
Bacterial Adhesion, Bacterial Proteins, Fibronectins, Genetic Complementation Test, Microscopy, Phase-Contrast, Mutation, Photomicrography, Enterococcus faecalis, Extracellular Matrix Proteins, Gene Deletion, Biofilms, Collagen Type I

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