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Characterization of a Propionibacterium acnes Surface Protein as a Fibrinogen-Binding Protein
by
Calvez, Vincent
, Raingeaud, Joël
, Grange, Philippe A.
, Dupin, Nicolas
, Morelle, Willy
, Marcelin, Anne-Geneviève
in
38/44
/ 42/44
/ 631/326/41/1969/1317
/ 631/45/612/1237
/ 82/16
/ 82/29
/ 82/83
/ 96/109
/ Amino acid sequence
/ Amino acids
/ Bacterial Proteins - genetics
/ Bacterial Proteins - isolation & purification
/ Bacterial Proteins - metabolism
/ Blotting, Western
/ Cell surface
/ Deglycosylation
/ Dermatan Sulfate - metabolism
/ Electrophoresis, Polyacrylamide Gel
/ Extracellular matrix
/ Extracellular Matrix Proteins - metabolism
/ Fibrinogen
/ Fibrinogen - metabolism
/ Fibrinogen-binding protein
/ Glycosylation
/ Humanities and Social Sciences
/ Humans
/ Life Sciences
/ multidisciplinary
/ Opportunist infection
/ Peptide Fragments - metabolism
/ Peptides
/ Propionibacterium
/ Propionibacterium acnes - chemistry
/ Propionibacterium acnes - growth & development
/ Propionibacterium acnes - metabolism
/ Proteins
/ Science
/ Science (multidisciplinary)
/ Skin
/ Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
/ Stationary phase
/ Sulfates
2017
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Characterization of a Propionibacterium acnes Surface Protein as a Fibrinogen-Binding Protein
by
Calvez, Vincent
, Raingeaud, Joël
, Grange, Philippe A.
, Dupin, Nicolas
, Morelle, Willy
, Marcelin, Anne-Geneviève
in
38/44
/ 42/44
/ 631/326/41/1969/1317
/ 631/45/612/1237
/ 82/16
/ 82/29
/ 82/83
/ 96/109
/ Amino acid sequence
/ Amino acids
/ Bacterial Proteins - genetics
/ Bacterial Proteins - isolation & purification
/ Bacterial Proteins - metabolism
/ Blotting, Western
/ Cell surface
/ Deglycosylation
/ Dermatan Sulfate - metabolism
/ Electrophoresis, Polyacrylamide Gel
/ Extracellular matrix
/ Extracellular Matrix Proteins - metabolism
/ Fibrinogen
/ Fibrinogen - metabolism
/ Fibrinogen-binding protein
/ Glycosylation
/ Humanities and Social Sciences
/ Humans
/ Life Sciences
/ multidisciplinary
/ Opportunist infection
/ Peptide Fragments - metabolism
/ Peptides
/ Propionibacterium
/ Propionibacterium acnes - chemistry
/ Propionibacterium acnes - growth & development
/ Propionibacterium acnes - metabolism
/ Proteins
/ Science
/ Science (multidisciplinary)
/ Skin
/ Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
/ Stationary phase
/ Sulfates
2017
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Characterization of a Propionibacterium acnes Surface Protein as a Fibrinogen-Binding Protein
by
Calvez, Vincent
, Raingeaud, Joël
, Grange, Philippe A.
, Dupin, Nicolas
, Morelle, Willy
, Marcelin, Anne-Geneviève
in
38/44
/ 42/44
/ 631/326/41/1969/1317
/ 631/45/612/1237
/ 82/16
/ 82/29
/ 82/83
/ 96/109
/ Amino acid sequence
/ Amino acids
/ Bacterial Proteins - genetics
/ Bacterial Proteins - isolation & purification
/ Bacterial Proteins - metabolism
/ Blotting, Western
/ Cell surface
/ Deglycosylation
/ Dermatan Sulfate - metabolism
/ Electrophoresis, Polyacrylamide Gel
/ Extracellular matrix
/ Extracellular Matrix Proteins - metabolism
/ Fibrinogen
/ Fibrinogen - metabolism
/ Fibrinogen-binding protein
/ Glycosylation
/ Humanities and Social Sciences
/ Humans
/ Life Sciences
/ multidisciplinary
/ Opportunist infection
/ Peptide Fragments - metabolism
/ Peptides
/ Propionibacterium
/ Propionibacterium acnes - chemistry
/ Propionibacterium acnes - growth & development
/ Propionibacterium acnes - metabolism
/ Proteins
/ Science
/ Science (multidisciplinary)
/ Skin
/ Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
/ Stationary phase
/ Sulfates
2017
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Characterization of a Propionibacterium acnes Surface Protein as a Fibrinogen-Binding Protein
Journal Article
Characterization of a Propionibacterium acnes Surface Protein as a Fibrinogen-Binding Protein
2017
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Overview
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.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 42/44
/ 82/16
/ 82/29
/ 82/83
/ 96/109
/ Bacterial Proteins - genetics
/ Bacterial Proteins - isolation & purification
/ Bacterial Proteins - metabolism
/ Dermatan Sulfate - metabolism
/ Electrophoresis, Polyacrylamide Gel
/ Extracellular Matrix Proteins - metabolism
/ Humanities and Social Sciences
/ Humans
/ Peptide Fragments - metabolism
/ Peptides
/ Propionibacterium acnes - chemistry
/ Propionibacterium acnes - growth & development
/ Propionibacterium acnes - metabolism
/ Proteins
/ Science
/ Skin
/ Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
/ Sulfates
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