Binding of laminin to oral and endocarditis strains of viridans streptococci

Switalski, Lech M.; Murchison, H; Timpl, Rupert; Curtiss, rd R; Höök, Magnus

doi:10.1128/jb.169.3.1095-1101.1987

Cited by 72 publications

(48 citation statements)

References 25 publications

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“…Several strains of oral streptococci, particularly those isolated from the heart valves of patients with endocarditis, express receptors that interact specifically with laminin (43). Such interaction may be critical for the bacterial colonization of damaged tissue.…”

Section: Discussionmentioning

confidence: 99%

Expression and Functional Properties of the Streptococcus intermedius Surface Protein Antigen I/II

et al. 2001

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Streptococcus intermedius is associated with deep-seated purulent infections. In this study, we investigated expression and functional activities of antigen I/II in S. intermedius. The S. intermedius antigen I/II appeared to be cell surface associated, with a molecular mass of approximately 160 kDa. Northern blotting indicated that the S. intermedius NCTC 11324 antigen I/II gene was transcribed as a monocistronic message. Maximum expression was seen during the early exponential phase. Insertional inactivation of the antigen I/II gene resulted in reduced hydrophobicity during early exponential phase, whereas no effect was detected during midand late exponential phases. Binding to human fibronectin and laminin was reduced in the isogenic mutant, whereas binding to human collagen types I and IV and to rat collagen type I was not significant for either the wild type or the mutant. Compared to the wild type, the capacity of the isogenic mutant to induce interleukin 8 (IL-8) release by THP-1 monocytic cells was significantly reduced. The results indicate that the S. intermedius antigen I/II is involved in adhesion to human receptors and in IL-8 induction.Streptococcus intermedius belongs to the anginosus group of streptococci. Members of this group are residents of the oral cavity and gastrointestinal and urogenital tracts but are also associated with suppurative infections at various clinical sites (17,39,49). S. intermedius shows tropism for infections of the brain and liver (49). Like other oral streptococci, S. intermedius may be implicated as a causative agent of infective endocarditis (11,39,49). For both abscesses and infective endocarditis, molecular interactions with host components represent presumptive virulence factors (2, 51).Bacterial interactions with host components are most often associated with surface proteins. The oral streptococci express a family of structurally and antigenically related surface proteins termed antigen I/II. These proteins have received a variety of names according to the strains or species in which they were identified, such as antigen B (40), Sr (35), I/II (20), and PAc (37) from Streptococcus mutans; SpaA from Streptococcus sobrinus (25, 45); and SspA and SspB from two tandemly arranged genes in Streptococcus gordonii (7). Multifunctional activities are attributed to the antigen I/II family, i.e., binding to soluble extracellular matrix glycoproteins (41) and to host cell receptors (42, 47), coaggregation with other microorganisms (4, 15, 24), interactions with salivary glycoproteins (3,9,12,19,21,27,36), and activation of monocytic cells (1,5,6). Members of the antigen I/II family may, however, exhibit functional species specificity. Differences in antigen I/II binding properties, mechanisms, and affinities have, for instance, been described for S. gordonii and S. mutans (18). Enzyme-linked immunosorbent assays (32), DNA hybridization studies (30), and homologous PCR-amplified sequences (6, 30) indicate that the anginosus group of streptococci also expresses an antigen I/II-l...

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Section: Discussionmentioning

confidence: 99%

Expression and Functional Properties of the Streptococcus intermedius Surface Protein Antigen I/II

et al. 2001

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“…Laminin is a highly glycosylated protein containing high-mannose-type glycans which is ubiquitous in the gastrointestinal tract (7). It is also a constituent of the basement membrane underlying the vascular epithelia and may be exposed in damaged tissues (26). The presence of exposed laminin and other glycoproteins containing high levels of mannose could act as a potential source of nutrients for enterococcal growth and facilitate the persistence of this organism on the endocardium.…”

Section: Discussionmentioning

confidence: 99%

Production of an Endo-β-N-Acetylglucosaminidase Activity Mediates Growth ofEnterococcus faecalison a High-Mannose-Type Glycoprotein

et al. 2000

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Enterococcus faecalis is associated with a high proportion of nosocomial infections; however, little is known of the ability of this organism to proliferate in vivo. The ability of RNase B, a model glycoprotein with a single N-glycosylation site occupied by a family of high-mannose-type glycans (Man 5 -to Man 9 -GlcNAc 2 ), to support growth of E. faecalis was investigated. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of RNase B demonstrated a reduction in the molecular mass of this glycoprotein during bacterial growth. Further analysis by matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) mass spectrometry revealed that this mass shift was due to the degradation of all high-mannose-type glycoforms to a single N-linked Nacetylglucosamine residue. High-pH anion-exchange chromatography analysis during exponential growth demonstrated the presence of RNase B-derived glycans in the culture supernatant, indicating the presence of an endoglycosidase activity. The free glycans were eluted with the same retention times as those generated by the action of Streptomyces plicatus endo-␤-N-acetylglucosaminidase H on RNase B. The cleavage specificity was confirmed by MALDI-TOF analysis of the free glycans, which showed glycan species containing only one N-acetylglucosamine residue. No free glycans were detectable after 5 h of bacterial growth, and we have subsequently demonstrated the presence of mannosidase activity in E. faecalis, which releases free mannose from RNase B-derived glycans. We propose that this deglycosylation of glycoproteins containing high-mannose-type glycans and the subsequent degradation of the released glycans by E. faecalis may play a role in the survival and persistence of this nosocomial pathogen in vivo.

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“…Interestingly, coated surfaces showed some structural differences, with more cell clusters, whereas uncoated polystyrene showed a uniform distribution of biofilm bacteria. The use of surfaces coated with matrix proteins can facilitate the isolation of mutants that are defective in binding to proteins on damaged heart valves and subsequent identification of bacteriumhost interactions that are important in biofilm formation and the pathogenesis of endocarditis (59,60).…”

Section: S Gordonii Biofilm Formation Is Nutrient Dependentmentioning

confidence: 99%

Streptococcus gordonii Biofilm Formation: Identification of Genes that Code for Biofilm Phenotypes

Loo¹,

Corliss²,

Ganeshkumar³

2000

J Bacteriol

453

426

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Viridans streptococci, which include Streptococcus gordonii, are pioneer oral bacteria that initiate dental plaque formation. Sessile bacteria in a biofilm exhibit a mode of growth that is distinct from that of planktonic bacteria. Biofilm formation of S. gordonii Challis was characterized using an in vitro biofilm formation assay on polystyrene surfaces. The same assay was used as a nonbiased method to screen isogenic mutants generated by Tn916 transposon mutagenesis for defective biofilm formation. Biofilms formed optimally when bacteria were grown in a minimal medium under anaerobic conditions. Biofilm formation was affected by changes in pH, osmolarity, and carbohydrate content of the growth media. Eighteen biofilm-defective mutants of S. gordonii Challis were identified based on Southern hybridization with a Tn916-based probe and DNA sequences of the Tn916-flanking regions. Molecular analyses of these mutants showed that some of the genes required for biofilm formation are involved in signal transduction, peptidoglycan biosynthesis, and adhesion. These characteristics are associated with quorum sensing, osmoadaptation, and adhesion functions in oral streptococci. Only nine of the biofilm-defective mutants had defects in genes of known function, suggesting that novel aspects of bacterial physiology may play a part in biofilm formation. Further identification and characterization of biofilmassociated genes will provide insight into the molecular mechanisms of biofilm formation of oral streptococci.

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Binding of laminin to oral and endocarditis strains of viridans streptococci

Abstract: Attachment of bacteria to the host tissue is regarded as a crucial step in the development of many types of infections. Recent

Cited by 72 publications

References 25 publications

Expression and Functional Properties of the Streptococcus intermedius Surface Protein Antigen I/II

Expression and Functional Properties of the Streptococcus intermedius Surface Protein Antigen I/II

Production of an Endo-β-N-Acetylglucosaminidase Activity Mediates Growth ofEnterococcus faecalison a High-Mannose-Type Glycoprotein

Streptococcus gordonii Biofilm Formation: Identification of Genes that Code for Biofilm Phenotypes

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