Streptococcal antigen I/II binds to extracellular proteins through intermolecular $beta;-sheets

KELEMEN, L

doi:10.1016/s0014-5793(04)00496-x

Cited by 4 publications

(5 citation statements)

References 18 publications

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“…The contribution of P1 to this process is becoming established and isogenic Antigen I/II-deficient mutants have been reported to form 65% less biofilm than the wild-type organism in the presence of saliva (Pecharki et al, 2005). In addition to human salivary agglutinin (gp340), Antigen I/II proteins interact with collagen, laminin, keratin, fibronectin, fibrinogen and other oral microorganisms (Sciotti et al, 1997;Heddle et al, 2003;Kelemen et al, 2004;Jakubovics et al, 2005a, b). The molecular basis for the specificity of these interactions is not fully understood, although many appear to be mediated by discontinuous but interacting domains of the proteins (Jakubovics et al, 2005b).…”

Section: Discussionmentioning

confidence: 99%

Characterization of epitopes recognized by anti-Streptococcus mutansP1 monoclonal antibodies

McArthur

Rhodin

Seifert

et al. 2007

FEMS Immunol Med Microbiol

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Sequences contributing to epitopes recognized by a panel of monoclonal antibodies (mAbs) against the Streptococcus mutans surface protein P1 were delineated by Western blot and enzyme-linked immunosorbent assay using a battery of deletion constructs and recombinant polypeptides. mAbs that recognize complex discontinuous epitopes reconstituted by combining the alanine-rich and proline-rich repeat domains and varying degrees of flanking sequence were identified as well as mAbs that bound epitopes contained within contiguous segments of P1. Cross-reactivity with SspA and SspB from Streptococcus gordonii is also reported. This information enables insight into the structure and function of a streptococcal adhesin and its correlates of protection and furthers our understanding of the immunomodulatory and bacterial-adherence inhibition activities of anti-P1 mAbs.

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Section: Discussionmentioning

confidence: 99%

Characterization of epitopes recognized by anti-Streptococcus mutansP1 monoclonal antibodies

McArthur

Rhodin

Seifert

et al. 2007

FEMS Immunol Med Microbiol

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“…Crowley and colleagues (2008) identified the A region as the salivary agglutinin binding domain within the P1 molecule. Moreover, P1 interacts with Fn and Fg forming a β‐structure upon interaction with both proteins (Kelemen et al. , 2004).…”

Section: Major Adhesin Familiesmentioning

confidence: 99%

Adhesion determinants of the Streptococcus species

Moschioni

Pansegrau

Barocchi³

2010

Microbial Biotechnology

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SummaryStreptococci are clinically important Gram‐positive bacteria that are capable to cause a wide variety of diseases in humans and animals. Phylogenetic analyses based on 16S rRNA sequences of the streptococcal species reveal a clustering pattern, reflecting, with a few exceptions, their pathogenic potential and ecological preferences. Microbial adhesion to host tissues is the initial critical event in the pathogenesis of most infections. Streptococci use multiple adhesins to attach to the epithelium, and their expression is regulated in response to environmental and growth conditions. Bacterial adhesins recognize and bind cell surface molecules and extracellular matrix components through specific domains that for certain adhesin families have been well defined and found conserved across the streptococcal species. In this review, we present the different streptococcal adhesin families categorized on the basis of their adhesive properties and structural characteristics, and, when available, we focus the attention on conserved functional domains.

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“…mutans has also been linked to cases of bacterial endocarditis and has been detected in atherosclerotic plaque. − Some strains of S. mutans have been reported to invade human coronary endothelial cells. , In the oral environment, P1 interacts primarily with the glycoprotein salivary agglutinin (SAG) complex predominantly composed of the scavenger receptor glycoprotein 340 (gp340/DMBT1), contained within the salivary pellicle on tooth surfaces. ,,,− P1 has also been shown to bind to extracellular matrix proteins such as collagen (Coll) − and fibronectin (Fn), ,, and is involved in cell–cell adhesion as well . The ability of P1 to promote bacterial adherence and to affect colonization, cariogenicity and biofilm formation has made it of interest as a therapeutic target. ,− …”

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confidence: 99%

Binding Forces of Streptococcus mutans P1 Adhesin

Sullan

Crowley

et al. 2015

ACS Nano

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Streptococcus mutans is a Gram-positive oral bacterium that is a primary etiological agent associated with human dental caries. In the oral cavity, S. mutans adheres to immobilized salivary agglutinin (SAG) contained within the salivary pellicle on the tooth surface. Binding to SAG is mediated by cell surface P1, a multifunctional adhesin that is also capable of interacting with extracellular matrix proteins. This may be of particular importance outside of the oral cavity as S. mutans has been associated with infective endocarditis and detected in atherosclerotic plaque. Despite the biomedical importance of P1, its binding mechanisms are not completely understood. In this work, we use atomic force microscopy-based single-molecule and single-cell force spectroscopy to quantify the nanoscale forces driving P1-mediated adhesion. Single-molecule experiments show that full-length P1, as well as fragments containing only the P1 globular head or C-terminal region, binds to SAG with relatively weak forces (~50 pN). In contrast, single-cell analyses reveal that adhesion of a single S. mutans cell to SAG is mediated by strong (~500 pN) and long-range (up to 6000 nm) forces. This is likely due to the binding of multiple P1 adhesins to self-associated gp340 glycoproteins. Such a cooperative, long-range character of the S. mutans–SAG interaction would therefore dramatically increase the strength and duration of cell adhesion. We also demonstrate, at single-molecule and single-cell levels, the interaction of P1 with fibronectin and collagen, as well as with hydrophobic, but not hydrophilic, substrates. The binding mechanism (strong forces, cooperativity, broad specificity) of P1 provides a molecular basis for its multifunctional adhesion properties. Our methodology represents a valuable approach to probe the binding forces of bacterial adhesins and offers a tractable methodology to assess anti-adhesion therapy.

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Streptococcal antigen I/II binds to extracellular proteins through intermolecular $beta;-sheets

Cited by 4 publications

References 18 publications

Characterization of epitopes recognized by anti-Streptococcus mutansP1 monoclonal antibodies

Characterization of epitopes recognized by anti-Streptococcus mutansP1 monoclonal antibodies

Adhesion determinants of the Streptococcus species

Binding Forces of Streptococcus mutans P1 Adhesin

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