ArticleFrontiers in microbiology2016
A Novel MSCRAMM Subfamily in Coagulase Negative Staphylococcal Species.
Article in Frontiers in microbiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
8 citing papers in PubMed, 23 citations in OpenAlex.
- Comparative genomic analysis of resistance and virulence genes in staphylococcus epidermidis and their impact on clinical outcome of musculoskeletal infections.Scientific reports · 2025Article
- Review
- Staphylococcal Vaccine Antigens related to biofilm formation.Human vaccines & immunotherapeutics · 2021Review
- Identification of Three Clf-Sdr Subfamily Proteins inFrontiers in microbiology · 2021Article
- Identification of surface proteins in a clinical Staphylococcus haemolyticus isolate by bacterial surface shaving.BMC microbiology · 2020Article
- Article
- Surface Proteins ofFrontiers in microbiology · 2020Review
- Overview of Staphylococcus epidermidis cell wall-anchored proteins: potential targets to inhibit biofilm formation.Molecular biology reports · 2020Review
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
Coagulase negative staphylococci (CoNS) are important opportunistic pathogens. Staphylococcus epidermidis, a coagulase negative staphylococcus, is the third leading cause of nosocomial infections in the US. Surface proteins like Microbial Surface Components Recognizing Adhesive Matrix Molecules (MSCRAMMs) are major virulence factors of pathogenic gram positive bacteria. Here, we identified a new chimeric protein in S. epidermidis, that we call SesJ. SesJ represents a prototype of a new subfamily of MSCRAMMs. Structural predictions show that SesJ has structural features characteristic of a MSCRAMM along with a N-terminal repeat region and an aspartic acid containing C-terminal repeat region, features that have not been previously observed in staphylococcal MSCRAMMs but have been found in other surface proteins from gram positive bacteria. We identified and analyzed structural homologs of SesJ in three other CoNS. These homologs of SesJ have an identical structural organization but varying sequence identities within the domains. Using flow cytometry, we also show that SesJ is expressed constitutively on the surface of a representative S. epidermidis strain, from early exponential to stationary growth phase. Thus, SesJ is positioned to interact with protein targets in the environment and plays a role in S. epidermidis virulence.
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Registered trials
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