ArticleJournal of bacteriology2002
Patterns of sequence conservation in the S-Layer proteins and related sequences in Clostridium difficile.
Article in Journal of bacteriology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 63 citations in OpenAlex.
- Article
- Review
- Surface Layer Protein A Expressed inMicroorganisms · 2020Article
- Cwp2 from Clostridium difficile exhibits an extended three domain fold and cell adhesion in vitro.The FEBS journal · 2017Article
- Role of Glycosyltransferases Modifying Type B Flagellin of Emerging Hypervirulent Clostridium difficile Lineages and Their Impact on Motility and Biofilm Formation.The Journal of biological chemistry · 2016Article
- Targeting surface-layer proteins with single-domain antibodies: a potential therapeutic approach against Clostridium difficile-associated disease.Applied microbiology and biotechnology · 2015Article
- Biogenesis and functions of bacterial S-layers.Nature reviews. Microbiology · 2014Review
- Clostridium difficile virulence factors: Insights into an anaerobic spore-forming pathogen.Gut microbes · 2014Review
- Recombinational switching of the Clostridium difficile S-layer and a novel glycosylation gene cluster revealed by large-scale whole-genome sequencing.The Journal of infectious diseases · 2013Article
- Surface-layer protein A (SlpA) is a major contributor to host-cell adherence of Clostridium difficile.PloS one · 2013Article
- The role of flagella in Clostridium difficile pathogenesis: comparison between a non-epidemic and an epidemic strain.PloS one · 2013Article
- Emergence of new PCR ribotypes from the hypervirulent Clostridium difficile 027 lineage.Journal of medical microbiology · 2012Article
- Roles of cysteine proteases Cwp84 and Cwp13 in biogenesis of the cell wall of Clostridium difficile.Journal of bacteriology · 2011Article
- The Clostridium difficile cell wall protein CwpV is antigenically variable between strains, but exhibits conserved aggregation-promoting function.PLoS pathogens · 2011Article
- Comparative proteomic analysis of extracellular proteins of Clostridium perfringens type A and type C strains.Infection and immunity · 2010Article
- Cwp84, a surface-associated cysteine protease, plays a role in the maturation of the surface layer of Clostridium difficile.The Journal of biological chemistry · 2009Article
- A novel genetic switch controls phase variable expression of CwpV, a Clostridium difficile cell wall protein.Molecular microbiology · 2009Article
- Differential proteomic analysis of Clostridium perfringens ATCC13124; identification of dominant, surface and structure associated proteins.BMC microbiology · 2009Article
- Clostridium difficile infection: new developments in epidemiology and pathogenesis.Nature reviews. Microbiology · 2009Review
- Cwp84, a surface-associated protein of Clostridium difficile, is a cysteine protease with degrading activity on extracellular matrix proteins.Journal of bacteriology · 2007Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Clostridium difficile is the etiological agent of antibiotic-associated diarrhea. Among the factors that may play a role in infection are S-layer proteins (SLPs). Previous work has shown these to consist mainly of two components, resulting from the cleavage of a precursor encoded by the slpA gene. The high-molecular-weight (MW) subunit is related both to amidases from B. subtilis and to at least another 28 gene products in C. difficile strain 630. To gain insight into the functions of the SLPs and related proteins, we have further investigated the pattern of variability both at the slpA locus and at six nearby paralogs. Sequencing of the slpA gene from an S-layer group II strain and a variant S-layer group strain confirms a high degree of divergence in the low-MW SLP, which may result from diversifying selection. A highly conserved motif, however, is found at the C terminus in all low-MW subunits and may be essential for SlpA precursor cleavage. In strain 167, a variant cleavage product is present, suggesting a secondary processing site. Southern blotting analysis shows slpA-like open reading frames (ORFs) 2 to 7 to be conserved in all nine strains tested, with one exception: ORF2, which encodes a 66-kDa polypeptide coextracted at low pH with the main SLPs in strain 630, may be partially deleted in strain 167. Polymorphism within the slpA-ORF7 cluster may be more pronounced in the region proximal to the slpA gene. Unexpectedly, a high-MW subunit probe cross hybridizes to sequences outside the slpA locus, which appear to vary in number in different strains.
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