ArticleInfection and immunity2013
Staphylococcus aureus SasA is responsible for binding to the salivary agglutinin gp340, derived from human saliva.
Article in Infection and immunity, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 45 citations in OpenAlex.
- The mutational landscape of Staphylococcus aureus during colonisation.Nature communications · 2025Article
- Bacterial single-cell RNA sequencing captures biofilm transcriptional heterogeneity and differential responses to immune pressure.Nature communications · 2024Article
- Article
- The long and the short of Periscope Proteins.Biochemical Society transactions · 2022Review
- Systems biology approach to functionally assess theProceedings of the National Academy of Sciences of the United States of America · 2022Article
- The Glycoprotein 340's Scavenger Receptor Cysteine-Rich Domain Promotes Adhesion of Staphylococcus aureus and Pseudomonas aeruginosa to Contact Lens Polymers.Infection and immunity · 2022Article
- Monoclonal Antibodies Targeting Surface-Exposed and Secreted Proteins from Staphylococci.Vaccines · 2021Review
- 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
- Surface Proteins ofMicrobiology spectrum · 2019Review
- Transcriptomic Adjustments ofFrontiers in microbiology · 2019Article
- Sortases, Surface Proteins, and Their Roles inMicrobiology spectrum · 2019Article
- Tunicamycin Mediated Inhibition of Wall Teichoic Acid AffectsFrontiers in microbiology · 2018Article
- Comparative Genomics of the Herbivore Gut SymbiontFrontiers in microbiology · 2018Article
- The scavenging capacity of DMBT1 is impaired by germline deletions.Immunogenetics · 2017Article
- Mucosal fluid glycoprotein DMBT1 suppresses twitching motility and virulence of the opportunistic pathogen Pseudomonas aeruginosa.PLoS pathogens · 2017Article
- Defining the enzymatic pathway for polymorphicThe Journal of biological chemistry · 2017Article
- Whole-Genome Sequencing Analysis of Methicillin-Resistant Staphylococcus simulans Causing Surgical Site Infection.Genome announcements · 2016Article
- The Staphylococcus aureus Global Regulator MgrA Modulates Clumping and Virulence by Controlling Surface Protein Expression.PLoS pathogens · 2016Article
- Mechanism of a cytosolic O-glycosyltransferase essential for the synthesis of a bacterial adhesion protein.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Highly sensitive detection of influenza virus in saliva by real-time PCR method using sugar chain-immobilized gold nanoparticles; application to clinical studies.Biotechnology reports (Amsterdam, Netherlands) · 2015Article
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Staphylococcus aureus is a major human pathogen that can colonize the nasal cavity, skin, intestine, and oral cavity as a commensal bacterium. gp340, also known as DMBT1 (deleted in malignant brain tumors 1), is associated with epithelial differentiation and innate immunity. In the oral cavity, gp340 induces salivary aggregation with several oral bacteria and promotes bacterial adhesion to tissues such as the teeth and mucosa. S. aureus is often isolated from the oral cavity, but the mechanism underlying its persistence in the oral cavity remains unclear. In this study, we investigated the interaction between S. aureus and gp340 and found that S. aureus interacts with saliva- and gp340-coated resin. We then identified the S. aureus factor(s) responsible for binding to gp340. The cell surface protein SasA, which is rich in basic amino acids (BR domain) at the N terminus, was responsible for binding to gp340. Inactivation of the sasA gene resulted in a significant decrease in S. aureus binding to gp340-coated resin. Also, recombinant SasA protein (rSasA) showed binding affinity to gp340, which was inhibited by the addition of N-acetylneuraminic acid. Surface plasmon resonance analysis showed that rSasA significantly bound to the NeuAcα(2-3)Galβ(1-4)GlcNAc structure. These results indicate that SasA is responsible for binding to gp340 via the N-acetylneuraminic acid moiety.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.