Characterization of a Propionibacterium acnes Surface Protein as a Fibrinogen-Binding Protein

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...

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Autores principales:	Philippe A. Grange, Joël Raingeaud, Willy Morelle, Anne-Geneviève Marcelin, Vincent Calvez, Nicolas Dupin
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/2189ef298cce4d45be1d65b8f3f15520
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spelling	oai:doaj.org-article:2189ef298cce4d45be1d65b8f3f155202021-12-02T15:05:47ZCharacterization of a Propionibacterium acnes Surface Protein as a Fibrinogen-Binding Protein10.1038/s41598-017-06940-32045-2322https://doaj.org/article/2189ef298cce4d45be1d65b8f3f155202017-07-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-06940-3https://doaj.org/toc/2045-2322Abstract 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.Philippe A. GrangeJoël RaingeaudWilly MorelleAnne-Geneviève MarcelinVincent CalvezNicolas DupinNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-14 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Philippe A. Grange Joël Raingeaud Willy Morelle Anne-Geneviève Marcelin Vincent Calvez Nicolas Dupin Characterization of a Propionibacterium acnes Surface Protein as a Fibrinogen-Binding Protein
description	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.
format	article
author	Philippe A. Grange Joël Raingeaud Willy Morelle Anne-Geneviève Marcelin Vincent Calvez Nicolas Dupin
author_facet	Philippe A. Grange Joël Raingeaud Willy Morelle Anne-Geneviève Marcelin Vincent Calvez Nicolas Dupin
author_sort	Philippe A. Grange
title	Characterization of a Propionibacterium acnes Surface Protein as a Fibrinogen-Binding Protein
title_short	Characterization of a Propionibacterium acnes Surface Protein as a Fibrinogen-Binding Protein
title_full	Characterization of a Propionibacterium acnes Surface Protein as a Fibrinogen-Binding Protein
title_fullStr	Characterization of a Propionibacterium acnes Surface Protein as a Fibrinogen-Binding Protein
title_full_unstemmed	Characterization of a Propionibacterium acnes Surface Protein as a Fibrinogen-Binding Protein
title_sort	characterization of a propionibacterium acnes surface protein as a fibrinogen-binding protein
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/2189ef298cce4d45be1d65b8f3f15520
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Characterization of a Propionibacterium acnes Surface Protein as a Fibrinogen-Binding Protein

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