Binding of streptococci of the “mutans” group to type 1 collagen associated with apatitic surfaces

Liu, Tianjia; Gibbons, R. J.

doi:10.1111/j.1399-302x.1990.tb00410.x

Cited by 37 publications

(32 citation statements)

References 22 publications

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“…Non-specific binding of P. intermedia to collagen must be ruled out because (i) no attachment of bacteria to BSAcoated wells was detected and (ii) complete inhibition of attachment occurred in the presence of free soluble collagen or its denatured form (gelatin). Collagen-binding capacity has been previously demonstrated for other oral bacterial species, including certain streptococci of the mutans group (Liu & Gibbons, 1990), Actinomyces viscos~s (Liu e t al., 1991) and Por. gingivalis (Naito & Gibbons, 1988).…”

Section: Discussionmentioning

confidence: 98%

Collagen-binding activity of Prevotella intermedia measured by a microtitre plate adherence assay

Grenier

1996

Microbiology

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The ability of Prevotella intermedia to bind type I collagen was investigated. A simple method in which bacterial cells were allowed to attach to collagen-coated microtitre plate wells was used to characterize the activity. All strains of P. intermedia tested, as well as those of the closely related species Prevotella nigrescens, showed a capacity to attach to the collagen film. Exponential-phase cultures of P. intermedia demonstrated a greater binding capacity than older cells. Attachment to the collagen film was inhibited by the presence of EDTA, type I and IV collagen, denatured collagen (gelatin), fibrinogen or fibronectin. Pretreatment of bacterial cells with heat (60 0C, 30 min) or proteinase K also inhibited the binding. The collagen-binding activity could be solubilized from the bacterial cell surface by incubation with Zwittergent 3-14, a zwitterionic detergent. The collagen-binding capacity of P. intermedia demonstrated in the present study represents a mechanism of colonization allowing these bacteria to attach to a tissue matrix.

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Section: Discussionmentioning

confidence: 98%

Collagen-binding activity of Prevotella intermedia measured by a microtitre plate adherence assay

Grenier

1996

Microbiology

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“…In the presence of an adherencepromoting component which may be provided from food, other organism, and so on, S. mutans can easily achieve initial adherence to the teeth. We previously reported that the supernatant of P. gingivalis ATCC Col-HA surface to mimic the matrices of dentin and cementum (17). Therefore, these findings suggest that the adherence of S. mutans to dentin and cementum of teeth in vivo may be increased by the vesicle.…”

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confidence: 80%

Effect of Porphyromonas gingivalis ATCC 33277 Vesicle on Adherence of Streptococcus mutans OMZ 70 to the Experimental Pellicle

Kamaguchi

Baba

Hoshi

et al. 1995

Microbiology and Immunology

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The vesicles of Porphyromonas gingivalis ATCC 33277 strongly aggregated Streptococcus cricetus, S. rattus, and S. mutans, but poorly aggregated S. sobrinus. The adherence of S. mutans OMZ 70 to hydroxyapatite (HA) coated with whole saliva was increased in parallel with the quantity of the vesicles. The significant increase of adherence of S. mutans OMZ 70 by the vesicles was also observed on the HA coated with parotid saliva, submandibular saliva, serum, and type I collagen. These findings suggest that the vesicles may act as a bridge between mutans streptococcus and the tooth surface.

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“…Adhesion to rat collagen type I and to human collagen types I and IV was not significant for either the wild type or the isogenic mutant IB08981 ( Table 1). As S. mutans OMZ 175 has been shown to bind to human collagen (28), this strain was included as a control. Compared with the wild type, adherence of the mutant to human fibronectin was reduced by 75% and to human laminin by 35% (Table 1).…”

Section: Resultsmentioning

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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Binding of streptococci of the “mutans” group to type 1 collagen associated with apatitic surfaces

Cited by 37 publications

References 22 publications

Collagen-binding activity of Prevotella intermedia measured by a microtitre plate adherence assay

Collagen-binding activity of Prevotella intermedia measured by a microtitre plate adherence assay

Effect of Porphyromonas gingivalis ATCC 33277 Vesicle on Adherence of Streptococcus mutans OMZ 70 to the Experimental Pellicle

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

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