ArticleInfection and immunity1994
Conservation of salivary glycoprotein-interacting and human immunoglobulin G-cross-reactive domains of antigen I/II in oral streptococci.
Article in Infection and immunity, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 66 citations in OpenAlex.
- Virulence factors ofFrontiers in microbiology · 2022Review
- Streptococcus pyogenes antigen I/II-family polypeptide AspA shows differential ligand-binding properties and mediates biofilm formation.Molecular microbiology · 2011Article
- Article
- The changing faces of Streptococcus antigen I/II polypeptide family adhesins.Molecular microbiology · 2010Review
- Requirements for surface expression and function of adhesin P1 from Streptococcus mutans.Infection and immunity · 2008Article
- Redirecting the humoral immune response against Streptococcus mutans antigen P1 with monoclonal antibodies.Infection and immunity · 2004Article
- Bactericidal effects of a fusion protein of llama heavy-chain antibodies coupled to glucose oxidase on oral bacteria.Antimicrobial agents and chemotherapy · 2004Article
- Contribution of the alanine-rich region of Streptococcus mutans P1 to antigenicity, surface expression, and interaction with the proline-rich repeat domain.Infection and immunity · 2004Article
- Further characterization of immunomodulation by a monoclonal antibody against Streptococcus mutans antigen P1.Infection and immunity · 2004Article
- Enhanced immunogenicity of a genetic chimeric protein consisting of two virulence antigens of Streptococcus mutans and protection against infection.Infection and immunity · 2002Article
- Structural and functional variation within the alanine-rich repetitive domain of streptococcal antigen I/II.Infection and immunity · 2002Article
- Functional variation of the antigen I/II surface protein in Streptococcus mutans and Streptococcus intermedius.Infection and immunity · 2002Article
- Expression and functional properties of the Streptococcus intermedius surface protein antigen I/II.Infection and immunity · 2001Article
- Identification of saliva-regulated genes of Streptococcus gordonii DL1 by differential display using random arbitrarily primed PCR.Infection and immunity · 2000Article
- Identification of Streptococcus mutans PAc peptide motif binding with human MHC class II molecules (DRB1*0802, *1101, *1401 and *1405).Immunology · 1998Article
- Binding properties of Streptococcus gordonii SspA and SspB (antigen I/II family) polypeptides expressed on the cell surface of Lactococcus lactis MG1363.Infection and immunity · 1998Article
- Deletion of the central proline-rich repeat domain results in altered antigenicity and lack of surface expression of the Streptococcus mutans P1 adhesin molecule.Infection and immunity · 1998Article
- Comparison of an adherence domain and a structural region of Streptococcus mutans antigen I/II in protective immunity against dental caries in rats after intranasal immunization.Infection and immunity · 1998Article
- Binding of salivary glycoprotein-secretory immunoglobulin A complex to the surface protein antigen of Streptococcus mutans.Infection and immunity · 1998Article
- Invasion of dentinal tubules by oral streptococci is associated with collagen recognition mediated by the antigen I/II family of polypeptides.Infection and immunity · 1997Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In this study we localized more precisely the salivary glycoprotein-interacting and the human immunoglobulin G (hIgG)-cross-reacting domains on the SR molecule, an antigen I/II-related protein from S. mutans serotype f. Mapping of the SR molecule with polypeptides expressed by subclones covering the entire molecule and with synthetic peptides demonstrates that the salivary glycoprotein-binding domain is located in the N-terminal alanine-rich repeats of the SR molecule. In order to investigate the degree of conservation of both regions in various oral streptococci, we tested the reactivity of 8 representative strains of the mutans group and 11 nonmutans oral Streptococcus strains (S. anginosus, S. milleri, S. constellatus, S. intermedius, S. mitis, S. sanguis, S. gordonii, S. salivarius, and S. mitis strains) with antipeptide antibodies in a whole-cell enzyme linked immunosorbent assay together with colony hybridization analysis using DNA probes designed to map these two regions. All the mutans group strains except S. rattus and the 11 nonmutans streptococcal strains showed a high conservation of the C-terminal part of the SR molecule, especially the hIgG-cross-reacting domain, and less homology for the N-terminal salivary glycoprotein-binding region. Almost all of the sera from patients with rheumatic disease reacted strongly with SR from S. mutans serotype f, P1 from S. mutans serotype c, and four peptides located in the hIgG-cross-reacting region and not with peptides located at the C and N termini and in the proline-rich repeats. These results confirm that epitopes located within this region are immunogenic in humans and could lead to the synthesis of natural anti-IgG antibodies.
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