Molecular characterization and expression of a gene encoding a Staphylococcus aureus collagen adhesin.

Patti, Joseph M.; Jonsson, Hans; Guss, Bengt; Switalski, Lech M.; Wiberg, Kristina; Lindberg, Martin; Höök, Magnus

doi:10.1016/s0021-9258(18)42898-0

Cited by 238 publications

(20 citation statements)

References 31 publications

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“…The Cnm protein exhibited high homology with collagenbinding adhesins from S. aureus, E. faecium, and S. equi (Patti et al, 1992;Lannergard et al, 2003;Nallapareddy et al, 2003). Specifically, the 165-amino-acid sequence from residues 152 to 316 was highly homologous to the CBDs of these collagen-binding adhesins.…”

Section: Discussionmentioning

confidence: 99%

“…Previously identified collagen-binding adhesin molecules (Patti et al, 1992;Rich et al, 1999;Lannergard et al, 2003;Nallapareddy et al, 2003) contained the B repeat regions following the A domain containing the CBD. However, the number of repeats and the length of the repeating units were dependent on species variation.…”

Section: Discussionmentioning

confidence: 99%

“…#AB102689) involved in the cold-agglutination phenotype of S. mutans strain Z1 following in vitro random mutagenesis mediated by the Himar1 minitransposon introduced into the chromosomal DNA of the strain (Sato et al, 2004). This gene encoded a new member of wall-anchored proteins, which was highly homologous to a group of collagen-adhesin proteins from Staphylococcus aureus (Patti et al, 1992) as well as other bacteria (Rich et al, 1999;Lannergard et al, 2003;Nallapareddy et al, 2003). Some strains of S. mutans were reported to recognize and bind collagen (Liu et al, 1990;Switalski et al, 1993).…”

Section: Introductionmentioning

confidence: 99%

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Streptococcus mutans Strains Harboring Collagen-binding Adhesin

Satō

Okamoto²,

Kagami³

et al. 2004

J Dent Res

105

101

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A previously unidentified 120-kDa protein was detected in Streptococcus mutans strain Z1 and was involved in the cold-agglutination of the strain. We have identified the gene, designated cnm, as being involved in the agglutination of strain Z1 following random mutagenesis. The amino acid sequence of the deduced Cnm protein exhibited high similarity to those of collagen-binding adhesins from staphylococci and other organisms. To confirm whether the protein is involved in collagen-binding, we cloned a cnm gene fragment, overexpressed it in E.coli, and prepared crude extracts. The extracts containing recombinant protein exhibited binding to immobilized collagen and laminin but not to fibronectin. Compared with the parental strain Z1, the cold-agglutination-negative mutant 05A02 exhibited reduced binding to collagen and laminin but retained that to fibronectin. This gene was detected in some strains of S. mutans. Therefore, the cnm gene encoded a new strain-specific member of the collagen-binding adhesin family.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Streptococcus mutans Strains Harboring Collagen-binding Adhesin

Satō

Okamoto²,

Kagami³

et al. 2004

J Dent Res

105

101

View full text Add to dashboard Cite

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“…The value of ~314 nm that we obtained from WLC modeling is in the range of several important S. aureus surface-anchored adhesins that have been extensively described in literature (O'Neill et al 2008). By considering the length of a single amino acid to be ~0.36 nm (Herman et al 2014), we can determine the contour length for previously described S. aureus adhesins such as protein A (~183 nm; Uhlen et al 1984), clumping factor ClfA (~336 nm; Hartford et al 1997), fibrinogen-binding proteins FnBPA and FnBPB (~366 nm; Keane et al 2007), and cna (~426 nm;Patti et al 1992). Interestingly, FnBPA has been shown to express strongly in S. aureus 8325-4, the strain of choice in the present study.…”

Section: Deciphering the S Aureus-ti Nanoadhesive Interactionmentioning

confidence: 99%

Nanoadhesion ofStaphylococcus aureusonto Titanium Implant Surfaces

et al. 2015

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Adhesion of bacteria to dental implant surfaces is the critical initial step in the process of biofilm colonization; however, the specific nanoadhesive interactions occurring during the first contact between bacterial cells and biomaterial substrates remain poorly understood. In this report, we utilize single-cell force spectroscopy to characterize the dynamics of the initial interaction between living Staphylococcus aureus cells and machined titanium surfaces at the nanoscale. Values for maximum adhesion force were found to increase from 0-s (-0.27 ± 0.30 nN) to 60-s (-9.15 ± 0.78 nN) surface delays, with similar results observed for total adhesion work (7.39 ± 2.38 and 988.06 ± 117.08 aJ, respectively). Single unbinding events observed at higher surface delays were modeled according to the wormlike chain model, obtaining molecular contour-length predictions of 314.06 ± 9.27 nm. Average single-bond rupture forces of -0.95 ± 0.04 nN were observed at increased contact times. Short- and long-range force components of bacterial adhesion were obtained by Poisson analysis of single unbinding event peaks, yielding values of -0.75 ± 0.04 and -0.58 ± 0.15 nN, respectively. Addition of 2-mg/mL chlorhexidine to the buffer solution resulted in the inhibition of specific adhesive events but an increased overall adhesion force and work. These results suggest that initial attachment of S. aureus to smooth titanium is mostly mediated by short-range attractive forces observed at higher surface delays.

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“…An exception is the collagen adhesin Ace, which was identified based on its sequence similarity to the collagen-binding MSCRAMM Cna from Staphylococcus aureus (Nallapareddy et al, 2000;Rich et al, 1999). Staphylococci express a family of structurally related, cell wall-anchored proteins that act as MSCRAMMs and bind to fibrinogen (Fg), collagen, fibronectin, laminin, cytokeratin 10 and elastin (Davis et al, 2001;Jönsson et al, 1991;McDevitt et al, 1994;Nallapareddy et al, 2000Nallapareddy et al, , 2003Ni Eidhin et al, 1998;O'Brien et al, 2002;Patti et al, 1992;Rich et al, 1999;Roche et al, 2004;Signäs et al, 1989;Wann et al, 2000). The recognized staphylococcal MSCRAMMs contain an N-terminal A-region composed of three domains, of which at least two adopt a characteristic IgG-like fold.…”

Section: Introductionmentioning

confidence: 99%

A family of fibrinogen-binding MSCRAMMs from Enterococcus faecalis

et al. 2009

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We report that three (EF0089, EF2505 and EF1896, renamed here Fss1, Fss2 and Fss3, respectively, for Enterococcus faecalis surface protein) of the recently predicted MSCRAMMs (microbial surface components recognizing adhesive matrix molecules) in E. faecalis strain V583 bind fibrinogen (Fg). Despite an absence of extensive primary sequence homology, the three proteins appear to be related structurally. Within the N-terminal regions of the three enterococcal proteins, we identified pairs of putative IgG-like modules with a high degree of predicted structural similarity to the Fg-binding N2 and N3 domains of the staphylococcal MSCRAMMs ClfA and SdrG. A second N2N3-like segment was predicted in Fss1. Far-UV circular dichroism spectroscopy revealed that all four predicted N2N3-like regions are composed mainly of b-sheets with only a minor proportion of a-helices, which is characteristic of Ig-like folded domains. Three of the four identified enterococcal N2N3-like regions showed potent dose-dependent binding to Fg. However, the specificity of the Fg-binding MSCRAMMs differs, as indicated by far-Western blots, which showed that recombinant segments of the MSCRAMMs bound different Fg polypeptide chains. Enterococci grown in serum-supplemented broth adhere to Fg-coated surfaces, and inactivation in strain OG1RF of the gene encoding Fss2 resulted in reduced adherence, whilst complementation of the mutant restored full Fg adherence. Thus, E. faecalis contains a family of MSCRAMMs that structurally and functionally resemble the Fg-binding MSCRAMMs of staphylococci.

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Molecular characterization and expression of a gene encoding a Staphylococcus aureus collagen adhesin.

Cited by 238 publications

References 31 publications

Streptococcus mutans Strains Harboring Collagen-binding Adhesin

Streptococcus mutans Strains Harboring Collagen-binding Adhesin

Nanoadhesion ofStaphylococcus aureusonto Titanium Implant Surfaces

A family of fibrinogen-binding MSCRAMMs from Enterococcus faecalis

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