Collagen binding toEscherichia coli strain NG7C

Shen, Wei; Ljungh, Åsa

doi:10.1007/bf01568953

Cited by 10 publications

(5 citation statements)

References 22 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Collagen is one of the major proteins of the ECM and is susceptible to invasion of pathogenic Gram‐positive and ‐negative bacteria under injury 22. Adhesion of probiotic bacteria to collagen is predicted to interfere with colonization and invasion of pathogenic bacteria.…”

Section: Resultsmentioning

confidence: 99%

The extracellular proteome of Bifidobacterium animalis subsp. lactis BB‐12 reveals proteins with putative roles in probiotic effects

et al. 2011

View full text Add to dashboard Cite

Probiotics are live microorganisms that exert health-promoting effects on the human host, as demonstrated for numerous strains of the genus Bifidobacterium. To unravel the proteins involved in the interactions between the host and the extensively used and well-studied probiotic strain Bifidobacterium animalis subsp. lactis BB-12, proteins secreted by the bacterium, i.e. belonging to the extracellular proteome present in the culture medium, were identified by 2-DE coupled with MALDI-TOF MS. Among the 74 distinct proteins identified, 31 are predicted to carry out their physiological role either outside the cell or on its surface. These proteins include solute-binding proteins for oligosaccharides, amino acids and manganese, cell wall-metabolizing proteins, and 18 proteins that have been described to interact with human host epithelial cells or extracellular matrix proteins. The potential functions include binding of plasminogen, formation of fimbriae, adhesion to collagen, attachment to mucin and intestinal cells as well as induction of immunomodulative response. These findings suggest a role of the proteins in colonization of the gastrointestinal tract, adhesion to host tissues, or immunomodulation of the host immune system. The identification of proteins predicted to be involved in such interactions can pave the way towards well targeted studies of the protein-mediated contacts between bacteria and the host, with the goal to enhance the understanding of the mode of action of probiotic bacteria.

show abstract

Section: Resultsmentioning

confidence: 99%

The extracellular proteome of Bifidobacterium animalis subsp. lactis BB‐12 reveals proteins with putative roles in probiotic effects

et al. 2011

View full text Add to dashboard Cite

show abstract

“…Surface proteins were extracted by heating at 60 °C for 20 min in PBS alone or at 45 °C for 2 h in the presence of 1% LiCl 60 . Bacteria were removed by centrifugation at 16,000 × g for 20 min at 4 °C.…”

Section: Methodsmentioning

confidence: 99%

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

Grange

Raingeaud

Morelle

et al. 2017

Sci Rep

View full text Add to dashboard Cite

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.

show abstract

“…Cells of P. acnes strains T1, GS‐1 and L4422 were washed in PBS and extracted with 1% LiCl for 1 h at 45°C [11]. After centrifugation (13 750× g , 30 min) the supernatant was dialyzed against PBS at +4°C overnight, and stored at −20°C.…”

Section: Methodsmentioning

confidence: 99%

“…Fn, vitronectin (Vn), BSP II, and Vitrogen ® (containing 95% type‐I collagen and 5% type‐III collagen) were iodinated using Iodobeads ® [11]. Washed bacterial cells (1.2×10 8 cells/ml, 100 μl) were incubated with 100 μl iodinated protein (1–3×10 6 cpm/μg stock solution, 2.5×10 5 cpm/ml) at 20°C for 1 h. After centrifugation (1350× g , 30 min), the radioactivity associated with the pellet was measured as earlier described [11].…”

Section: Methodsmentioning

confidence: 99%

See 1 more Smart Citation

Fibronectin binding by Propionibacterium acnes

Månsson

Flock

et al. 2006

FEMS Immunology &Amp; Medical Microbiology

View full text Add to dashboard Cite

Strains of Propionibacterium acnes, isolated from different kinds of orthopaedic and biomaterial‐associated infections and from skin flora were shown to express binding of soluble as well as immobilized fibronectin. Among these 7 strains isolated from orthopaedic infections, 2 from breast prostheses, and 9 skin isolates, 2, 2, and 5 strains respectively bound immobilized fibronectin. The fibronectin binding was sensitive to protease and heat treatment, and was inhibited by a cell surface extract from one of the binding strains. In SDS‐PAGE and autoradiography of cell surface extracts, a band corresponding to a MW of about 80 kD reacted with fibronectin and the 150 kD fragment of fibronectin. Binding to fibronectin and the 150 kD fragment of fibronectin could be inhibited with heparin. We thus present a first Fn binding protein of P. acnes, a surface exposed protein of 80 kD. None of the strains bound soluble collagen, and only one strain expressed weak binding of vitronectin and bone sialoprotein II.

show abstract

Collagen binding toEscherichia coli strain NG7C

Cited by 10 publications

References 22 publications

The extracellular proteome of Bifidobacterium animalis subsp. lactis BB‐12 reveals proteins with putative roles in probiotic effects

The extracellular proteome of Bifidobacterium animalis subsp. lactis BB‐12 reveals proteins with putative roles in probiotic effects

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

Fibronectin binding by Propionibacterium acnes

Contact Info

Product

Resources

About