ArticleInfection and immunity1998
Binding of salivary glycoprotein-secretory immunoglobulin A complex to the surface protein antigen of Streptococcus mutans.
Article in Infection and immunity, 1998. 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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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
32 citing papers in PubMed, 91 citations in OpenAlex.
- α2-3-Sialylated Glycoproteins AttenuateInternational journal of molecular sciences · 2026Article
- Mechanistic Insights into the Anti-Virulence Effects ofAntibiotics (Basel, Switzerland) · 2026Article
- Surface-expressed phosphoglycerate mutase of Candida albicans binds to salivary DMBT1.Archives of microbiology · 2023Article
- New carbohydrate binding domains identified by phage display based functional metagenomic screens of human gut microbiota.Communications biology · 2023Article
- Structures of SALSA/DMBT1 SRCR domains reveal the conserved ligand-binding mechanism of the ancient SRCR fold.Life science alliance · 2020Article
- Polymer Adhesin Domains in Gram-Positive Cell Surface Proteins.Frontiers in microbiology · 2020Review
- DMBT1 inhibition of Pseudomonas aeruginosa twitching motility involves its N-glycosylation and cannot be conferred by the Scavenger Receptor Cysteine-Rich bacteria-binding peptide domain.Scientific reports · 2019Article
- Glycan recognition at the saliva - oral microbiome interface.Cellular immunology · 2018Review
- Streptococcus mutans SpaP binds to RadD of Fusobacterium nucleatum ssp. polymorphum.Molecular oral microbiology · 2017Article
- Effect of salivary agglutination on oral streptococcal clearance by human polymorphonuclear neutrophil granulocytes.Molecular oral microbiology · 2017Article
- Mucosal fluid glycoprotein DMBT1 suppresses twitching motility and virulence of the opportunistic pathogen Pseudomonas aeruginosa.PLoS pathogens · 2017Article
- Identification of a supramolecular functional architecture of Streptococcus mutans adhesin P1 on the bacterial cell surface.The Journal of biological chemistry · 2015Article
- Binding forces of Streptococcus mutans P1 adhesin.ACS nano · 2015Article
- Oral lactic acid bacteria related to the occurrence and/or progression of dental caries in Japanese preschool children.Bioscience of microbiota, food and health · 2015Article
- Immunogenicity and in vitro and in vivo protective effects of antibodies targeting a recombinant form of the Streptococcus mutans P1 surface protein.Infection and immunity · 2014Article
- The calcium-induced conformation and glycosylation of scavenger-rich cysteine repeat (SRCR) domains of glycoprotein 340 influence the high affinity interaction with antigen I/II homologs.The Journal of biological chemistry · 2014Article
- Alterations in immunodominance of Streptococcus mutans AgI/II: lessons learned from immunomodulatory antibodies.Vaccine · 2014Article
- Staphylococcus aureus SasA is responsible for binding to the salivary agglutinin gp340, derived from human saliva.Infection and immunity · 2013Article
- An intramolecular interaction involving the N terminus of a streptococcal adhesin affects its conformation and adhesive function.The Journal of biological chemistry · 2013Article
- GlmS and NagB regulate amino sugar metabolism in opposing directions and affect Streptococcus mutans virulence.PloS one · 2012Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The interaction between a surface protein antigen (PAc) of Streptococcus mutans and human salivary agglutinin was analyzed with a surface plasmon resonance biosensor. The major component sugars of the salivary agglutinin were galactose, fucose, mannose, N-acetylglucosamine, N-acetylgalactosamine, and N-acetylneuraminic acid. Binding of salivary agglutinin to PAc was calcium dependent and heat labile and required a pH greater than 5. Binding was significantly inhibited by N-acetylneuraminic acid and alpha2,6-linked sialic acid-specific lectin derived from Sambucus sieboldiana in a dose-dependent manner. Pretreatment of the salivary agglutinin with sialidase reduced the binding activity of the agglutinin to the PAc molecule. The agglutinin was dissociated into high-molecular-mass glycoprotein and secretory immunoglobulin A (sIgA) components by electrophoretic fractionation in the presence of 1% sodium dodecyl sulfate and 1% 2-mercaptoethanol. Neither of the components separated by electrophoretic fractionation, high-molecular-mass glycoprotein or sIgA, bound to the PAc molecule. Furthermore, the high-molecular-mass glycoprotein strongly inhibited the binding of the native salivary complex to PAc. These results suggest that the complex formed by the high-molecular-mass salivary glycoprotein and sIgA is essential for the binding reaction and that the sialic acid residues of the complex play an important role in the interaction between the agglutinin and PAc of S. mutans.
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