GroEL (Hsp60) of Clostridium difficile is involved in cell adherence.
Abstract
Previous results have demonstrated that adherence of Clostridium difficile to tissue culture cells is augmented by various stresses; this study focussed on whether the GroEL heat shock protein is implicated in this process. The 1940 bp groESL operon of C. difficile was isolated by PCR. The 1623 bp groEL gene is highly conserved between various C. difficile isolates as determined by RFLP-PCR and DNA sequencing, and the operon is present in one copy on the bacterial chromosome. The 58 kDa GroEL protein was expressed in Escherichia coli in fusion with glutathione S:-transferase and the fusion protein was purified from IPTG-induced bacterial lysates by affinity chromatography on glutathione-Sepharose. A polyclonal, monospecific antiserum was obtained for GroEL which established by immunoelectron microscopy, indirect immunofluorescence and immunoblot analysis that GroEL is released extracellularly after heat shock and can be surface associated. Cell fractionation experiments suggest that GroEL is predominantly cytoplasmic and membrane bound. GroEL-specific antibodies as well as the purified protein partially inhibited C. difficile cell attachment and expression of the protein was induced by cell contact, suggesting a role for GroEL in cell adherence.
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Heat-shock GroEL proteins are cell-surface proteins also involved in clostridial cell adhesion and were predicted to be encoded by the P. sordellii strain FL-manatee gene ORF_03377.
“Heat-shock GroEL proteins are cell-surface proteins also involved in clostridial cell adhesion and were predicted to be encoded by the P. sordellii strain FL-manatee gene ORF_03377.”
From Novel Lethal Clostridial Infection in Florida Manatees (Trichechus manatus latirostris): Cause of the 2013 Unusual Mortality Event in the Indian River Lagoon (2022) · cites this paper as Hennequin et al., 2001
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Antibiotic-associated pseudomembranous colitis due to toxin-producing clostridia
Bartlett, J. G., Chang, T. W., Gurwith, M., Gorbach, S. L., & Onderdonk, A. B. (1978) · New England Journal of Medicine · doi:10.1056/nejm197803092981003 · Cited by 1,374 · see citing works
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Savariau-Lacomme, M.-P., Lebarbier, C., Karjalainen, T., Collignon, A., & Janoir, C. (2003) · Journal of Bacteriology · doi:10.1128/jb.185.15.4461-4470.2003 · Cited by 44 · see citing works
Self-citationLandsberg, J. H., Tabuchi, M., Rotstein, D. S., Subramaniam, K., Rodrigues, T. C. S., Waltzek, T. B., Stacy, N. I., Wilson, P. W., Kiryu, Y., Uzal, F. A., et al. (2022) · Frontiers in Marine Science · doi:10.3389/fmars.2022.841857 · Cited by 20 · see citing works
“GroEL has adhesive function in Clostridioides difficile (Hennequin et al., 2001).”
Background
- Authors
- Hennequin, C., Collignon, A., Bourlioux, P., Waligora-Dupriet, A.-J., Karjalainen, T., Barc, M.-C., & Porcheray, F.
- Affiliations
- Université Paris-Sud (FR)
- Corresponding author
- Karjalainen, Tuomo
- ORCID
- Bourlioux, Pierre
- Venue
- Microbiology
- Publisher
- Microbiology Society
- Published
- 2001-01-01
- Volume
- 147
- Issue
- 1
- Pages
- 87-96
- ISSN
- 1350-0872 (ISSN-L)
- 1465-2080
- OpenAlex
- W2130890924
- Cited by
- 226
- References
- 1
- Citations by year
- 2025: 4 · 2024: 6 · 2023: 6 · 2022: 7 · 2021: 14 · 2020: 5 · 2019: 8 · 2018: 15 · 2017: 7 · 2016: 11 · 2015: 12 · 2014: 17 · 2013: 15 · 2012: 11
- FWCI
- 3.03
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Microbiology (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- Funders
- European Commission
- Institut National de la Recherche Agronomique
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Health Sciences › Medicine › Infectious Diseases › Clostridium difficile and Clostridium perfringens research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Keywords
- Clostridium difficile, GroEL, HSP60, heat shock proteins, cell adhesion, groESL operon, extracellular protein release, heat shock, cell contact
- MeSH terms
- Amino Acid Sequence, Animals, Bacterial Adhesion, Base Sequence, Chlorocebus aethiops, Enterocolitis, Pseudomembranous, Humans, Molecular Sequence Data, Operon, Polymorphism, Restriction Fragment Length, Vero Cells, Polymerase Chain Reaction, Microscopy, Immunoelectron, Clostridioides difficile, Sequence Analysis, DNA, Gene Dosage, Chaperonin 60
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