title: Human common salivary protein 1 (CSP-1) promotes binding of Streptococcus mutans to experimental salivary pellicle and glucans formed on hydroxyapatite surface.
abstract: The saliva proteome includes host defense factors and specific bacterial-binding proteins that modulate microbial growth and colonization of the tooth surface in the oral cavity. A multidimensional mass spectrometry approach identified the major host-derived salivary proteins that interacted with Streptococcus mutans (strain UA159), the primary microorganism associated with the pathogenesis of dental caries. Two abundant host proteins were found to tightly bind to S. mutans cells, common salivary protein-1 (CSP-1) and deleted in malignant brain tumor 1 (DMBT1, also known as salivary agglutinin or gp340). In contrast to gp340, limited functional information is available on CSP-1. The sequence of CSP-1 shares 38.1% similarity with rat CSP-1. Recombinant CSP-1 (rCSP-1) protein did not cause aggregation of S. mutans cells and was devoid of any significant biocidal activity (2.5 to 10 μg/mL). However, S. mutans cells exposed to rCSP-1 (10 μg/mL) in saliva displayed enhanced adherence to experimental salivary pellicle and to glucans in the pellicle formed on hydroxyapatite surfaces. Thus, our data demonstrate that the host salivary protein CSP-1 binds to S. mutans cells and may influence the initial colonization of this pathogenic bacterium onto the tooth surface.
authors.affiliation: Departments of Pharmacology and Physiology, Rochester Proteomics Center, University of Rochester Medical Center, Rochester, New York 14642, United States.
authors.forename: Kiran S
authors.initials: KS
authors.lastname: Ambatipudi
authors.forename: Fred K
authors.initials: FK
authors.lastname: Hagen
authors.forename: Claire M
authors.initials: CM
authors.lastname: Delahunty
authors.forename: Xuemei
authors.initials: X
authors.lastname: Han
authors.forename: Rubina
authors.initials: R
authors.lastname: Shafi
authors.forename: Jennifer
authors.initials: J
authors.lastname: Hryhorenko
authors.forename: Stacy
authors.initials: S
authors.lastname: Gregoire
authors.forename: Robert E
authors.initials: RE
authors.lastname: Marquis
authors.forename: James E
authors.initials: JE
authors.lastname: Melvin
authors.forename: Hyun
authors.initials: H
authors.lastname: Koo
authors.forename: John R
authors.initials: JR
authors.lastname: Yates
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001422:Bacterial Adhesion / Q000187:drug effects; D002135:Calcium-Binding Proteins; D002460:Cell Line; D004268:DNA-Binding Proteins; D044622:Dental Pellicle / Q000187:drug effects / Q000378:metabolism* / Q000382:microbiology; D017886:Durapatite / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D005936:Glucans / Q000378:metabolism*; D006801:Humans; D036341:Intercellular Signaling Peptides and Proteins; D008969:Molecular Sequence Data; D011485:Protein Binding; D011506:Proteins / Q000235:genetics / Q000378:metabolism / Q000494:pharmacology; D011956:Receptors, Cell Surface / Q000378:metabolism; D011994:Recombinant Proteins / Q000378:metabolism / Q000494:pharmacology; D012463:Saliva / Q000378:metabolism / Q000382:microbiology; D012471:Salivary Proteins and Peptides / Q000235:genetics / Q000378:metabolism* / Q000494:pharmacology; D017386:Sequence Homology, Amino Acid; D013295:Streptococcus mutans / Q000187:drug effects / Q000254:growth & development / Q000378:metabolism*; D025521:Tumor Suppressor Proteins
chemical_list: D002135:Calcium-Binding Proteins; C108174:DMBT1 protein, human; D004268:DNA-Binding Proteins; D005936:Glucans; D036341:Intercellular Signaling Peptides and Proteins; D011506:Proteins; D011956:Receptors, Cell Surface; D011994:Recombinant Proteins; D012471:Salivary Proteins and Peptides; D025521:Tumor Suppressor Proteins; C517340:ZG16B protein, human; D017886:Durapatite