ArticleScientific reports2017
Characterization of a Propionibacterium acnes Surface Protein as a Fibrinogen-Binding Protein.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Unraveling the Enigmatic Behavior ofInternational journal of microbiology · 2026Article
- Optimization of Anthralin Microemulgel Targeted Delivery for Psoriasis and Acne.Molecules (Basel, Switzerland) · 2025Article
- Article
- Bacteria associated with acne use glycosaminoglycans as cell adhesion receptors and promote changes in the expression of the genes involved in their biosynthesis.BMC microbiology · 2022Article
- Review
- A Janus-Faced Bacterium: Host-Beneficial and -Detrimental Roles ofFrontiers in microbiology · 2021Review
- Epidermis as a Platform for Bacterial Transmission.Frontiers in immunology · 2021Review
- Article
- Platelet activation and aggregation by the opportunistic pathogen Cutibacterium (Propionibacterium) acnes.PloS one · 2018Article
- Over a Decade of recA and tly Gene Sequence Typing of the Skin Bacterium Propionibacterium acnes: What Have We Learnt?Microorganisms · 2017Review
- Prevalence of Flp Pili-Encoding Plasmids inFrontiers in microbiology · 2017Article
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Propionibacterium acnes (P. acnes) is a major skin-associated bacterium that was long considered commensal, until several studies revealed it to be an opportunistic pathogen. We investigated the ability of P. acnes surface proteins to recognize ECM proteins and showed that a 58 kDa P. acnes surface protein was specifically recognized by human fibrinogen (hFg). The 58 kDa protein was further characterized by two-dimensional (2-D) electrophoresis and MALDI-ToF as a P. acnes host cell-surface attachment protein, PA25957, recognizing dermatan sulfate (DsA1). This protein sequence contains 432 amino acids with the presence of three structurally different domains: an N-terminal signal peptide, a C-terminal LPXTG motif, and a PT repeat region. DsA1 is mostly produced during stationary phase. It appears to be highly glycosylated, containing GalNAc residues. Purified DsA1 strongly recognizes the Aα and Bβ subunits of hFg, and specific enzymatic deglycosylation of hFg demonstrated the involvement of the protein backbone in the recognition process. The Bβ subunit of hFg was cloned in four peptide fractions (Fg1-Fg4). The N-terminal Fg1 peptide of hFg was recognized by DsA1, and priming DsA1 with Fg1 inhibited DsA1/hFg recognition. We describe here for the first time, the characterization of a P. acnes surface glycoprotein recognizing human fibrinogen.
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