Binding of<i>Streptococcus gordonii</i>to extracellular matrix proteins

Giomarelli, Barbara; Visai, Livia; Hijazi, Karolin; Rindi, Simonetta; Ponzio, Michela; Iannelli, Francesco; Speziale, Pietro; Pozzi, Gianni

doi:10.1111/j.1574-6968.2006.00479.x

Cited by 29 publications

(31 citation statements)

References 39 publications

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“…Polysaccharides produced by some strains of Sg and Ss, including Sg Challis and Ss SK36, are not involved in coaggregation. Disruption of the polysaccharide gene locus in Sg Challis abrogated adhesion to collagen type I or II, indicating that the Sg Challis polysaccharide may be more important for the recognition of host tissue rather than other bacteria 34 .…”

Section: Resultsmentioning

confidence: 99%

Distinct Biological Potential of Streptococcus gordonii and Streptococcus sanguinis Revealed by Comparative Genome Analysis

Zheng

Tan

Old

et al. 2017

Sci Rep

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Streptococcus gordonii and Streptococcus sanguinis are pioneer colonizers of dental plaque and important agents of bacterial infective endocarditis (IE). To gain a greater understanding of these two closely related species, we performed comparative analyses on 14 new S. gordonii and 5 S. sanguinis strains using various bioinformatics approaches. We revealed S. gordonii and S. sanguinis harbor open pan-genomes and share generally high sequence homology and number of core genes including virulence genes. However, we observed subtle differences in genomic islands and prophages between the species. Comparative pathogenomics analysis identified S. sanguinis strains have genes encoding IgA proteases, mitogenic factor deoxyribonucleases, nickel/cobalt uptake and cobalamin biosynthesis. On the contrary, genomic islands of S. gordonii strains contain additional copies of comCDE quorum-sensing system components involved in genetic competence. Two distinct polysaccharide locus architectures were identified, one of which was exclusively present in S. gordonii strains. The first evidence of genes encoding the CylA and CylB system by the α-haemolytic S. gordonii is presented. This study provides new insights into the genetic distinctions between S. gordonii and S. sanguinis, which yields understanding of tooth surfaces colonization and contributions to dental plaque formation, as well as their potential roles in the pathogenesis of IE.

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Section: Resultsmentioning

confidence: 99%

Distinct Biological Potential of Streptococcus gordonii and Streptococcus sanguinis Revealed by Comparative Genome Analysis

Zheng

Tan

Old

et al. 2017

Sci Rep

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“…S. gordonii, which binds to eukaryotic cells through extracellular matrix (ECM) components such as collagen, laminin and fibronectin, showed significant impairment in fibronectin binding in the absence of MsrA [28]. In contrast, the msrA mutant of S. sanguis failed to adhere with platelets or to induce platelet aggregation [29].…”

Section: Msr and Bacterial Adherencementioning

confidence: 95%

Methionine Sulfoxide Reductases and Virulence of Bacterial Pathogens

2007

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Oxidation of methionine (Met) residues in proteins by reactive oxygen species and reactive nitrogen intermediates results in altered protein structures, which subsequently affect their functions. Oxidized Met (Met-O) residues are reduced to Met by the methionine sulfoxide reductase (Msr) system, which includes mainly MsrA and MsrB. MsrA and MsrB show no sequence and structural identity with each other but both reduce methionine sulfoxides. MsrA is specific to the reduction of methionine-S-sulfoxide, whereas MsrB is specific to the reduction of methionine-R-sulfoxide. Genes encoding the enzymes MsrA and MsrB exist in most living organisms including bacteria. In recent times, absence of these enzymes has been implicated in the virulence of bacterial pathogens. In particular, pathogens deficient in Msr have been reported to have reduced ability to adhere with eukaryotic cells, to survive inside hosts and to resist in vitro oxidative stress. Bacterial proteins that are susceptible to Met oxidation, in the absence of Msr, have also been identified. This review discusses the current knowledge on the role of Msr in bacterial virulence.

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“…Antibodies specific to this portion of CshA block Fn binding, whereas those raised against the repeat domain region elicit no effect (15). The CshA-Fn interaction has been proposed to be of general significance in promoting S. gordonii colonization at a range of sites within the host (7,15,16). These include the cardiac endothelium, where adherence by S. gordonii is known to promote the onset of infective endocarditis, a severe, potentially fatal inflammation of the inner tissues of the heart (17).…”

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confidence: 99%

The Streptococcus gordonii Adhesin CshA Protein Binds Host Fibronectin via a Catch-Clamp Mechanism

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Sztukowska

Till

et al. 2017

Journal of Biological Chemistry

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Edited by Norma AllewellAdherence of bacteria to biotic or abiotic surfaces is a prerequisite for host colonization and represents an important step in microbial pathogenicity. This attachment is facilitated by bacterial adhesins at the cell surface. Because of their size and often elaborate multidomain architectures, these polypeptides represent challenging targets for detailed structural and functional characterization. The multifunctional fibrillar adhesin CshA, which mediates binding to both host molecules and other microorganisms, is an important determinant of colonization by Streptococcus gordonii, an oral commensal and opportunistic pathogen of animals and humans. CshA binds the high-molecular-weight glycoprotein fibronectin (Fn) via an N-terminal non-repetitive region, and this protein-protein interaction has been proposed to promote S. gordonii colonization at multiple sites within the host. However, the molecular details of how these two proteins interact have yet to be established. Here we present a structural description of the Fn binding N-terminal region of CshA, derived from a combination of X-ray crystallography, small angle X-ray scattering, and complementary biophysical methods. In vitro binding studies support a previously unreported two-state "catch-clamp" mechanism of Fn binding by CshA, in which the disordered N-terminal domain of CshA acts to "catch" Fn, via formation of a rapidly assembled but also readily dissociable pre-complex, enabling its neighboring ligand binding domain to tightly clamp the two polypeptides together. This study presents a new paradigm for target binding by a bacterial adhesin, the identification of which will inform future efforts toward the development of anti-adhesive agents that target S. gordonii and related streptococci.

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Binding ofStreptococcus gordoniito extracellular matrix proteins

Cited by 29 publications

References 39 publications

Distinct Biological Potential of Streptococcus gordonii and Streptococcus sanguinis Revealed by Comparative Genome Analysis

Distinct Biological Potential of Streptococcus gordonii and Streptococcus sanguinis Revealed by Comparative Genome Analysis

Methionine Sulfoxide Reductases and Virulence of Bacterial Pathogens

The Streptococcus gordonii Adhesin CshA Protein Binds Host Fibronectin via a Catch-Clamp Mechanism

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