Adsorbed salivary proline-rich protein 1 and statherin: receptors for type 1 fimbriae of Actinomyces viscosus T14V-J1 on apatitic surfaces. 1988

R J Gibbons, and D I Hay, and J O Cisar, and W B Clark
Forsyth Dental Center, Boston, Massachusetts 02115.

Use of specific fimbria-defective mutants derived from Actinomyces viscosus T14 has shown that salivary acidic proline-rich protein 1 and statherin serve as receptors for type 1 fimbriae which mediate attachment of the organism to experimental pellicles on apatitic surfaces.

UI MeSH Term Description Entries
D010455 Peptides Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are considered to be larger versions of peptides that can form into complex structures such as ENZYMES and RECEPTORS. Peptide,Polypeptide,Polypeptides
D010861 Fimbriae, Bacterial Thin, hairlike appendages, 1 to 20 microns in length and often occurring in large numbers, present on the cells of gram-negative bacteria, particularly Enterobacteriaceae and Neisseria. Unlike flagella, they do not possess motility, but being protein (pilin) in nature, they possess antigenic and hemagglutinating properties. They are of medical importance because some fimbriae mediate the attachment of bacteria to cells via adhesins (ADHESINS, BACTERIAL). Bacterial fimbriae refer to common pili, to be distinguished from the preferred use of "pili", which is confined to sex pili (PILI, SEX). Bacterial Fimbriae,Bacterial Pili,Common Fimbriae,Common Pili,Pili, Bacterial,Pili, Common,Bacterial Fimbria,Bacterial Pilus,Common Fimbria,Common Pilus,Fimbria, Bacterial,Pilus, Bacterial,Fimbria, Common,Fimbriae, Common,Pilus, Common
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D006882 Hydroxyapatites A group of compounds with the general formula M10(PO4)6(OH)2, where M is barium, strontium, or calcium. The compounds are the principal mineral in phosphorite deposits, biological tissue, human bones, and teeth. They are also used as an anticaking agent and polymer catalysts. (Grant & Hackh's Chemical Dictionary, 5th ed) Hydroxyapatite Derivatives,Derivatives, Hydroxyapatite
D000190 Actinomyces A genus of gram-positive, rod-shaped bacteria whose organisms are nonmotile. Filaments that may be present in certain species are either straight or wavy and may have swollen or clubbed heads.
D001422 Bacterial Adhesion Physicochemical property of fimbriated (FIMBRIAE, BACTERIAL) and non-fimbriated bacteria of attaching to cells, tissue, and nonbiological surfaces. It is a factor in bacterial colonization and pathogenicity. Adhesion, Bacterial,Adhesions, Bacterial,Bacterial Adhesions
D012463 Saliva The clear, viscous fluid secreted by the SALIVARY GLANDS and mucous glands of the mouth. It contains MUCINS, water, organic salts, and ptylin. Salivas
D012471 Salivary Proteins and Peptides Proteins and peptides found in SALIVA and the SALIVARY GLANDS. Some salivary proteins such as ALPHA-AMYLASES are enzymes, but their composition varies in different individuals. Salivary Gland Protein,Salivary Gland Proteins,Salivary Peptide,Salivary Protein,Salivary Proteins,Salivary Peptides,Gland Protein, Salivary,Peptide, Salivary,Protein, Salivary,Protein, Salivary Gland
D055232 Proline-Rich Protein Domains Protein domains that are enriched in PROLINE. The cyclical nature of proline causes the peptide bonds it forms to have a limited degree of conformational mobility. Therefore the presence of multiple prolines in close proximity to each other can convey a distinct conformational arrangement to a peptide chain. Proline-Rich Peptide Domains,Domain, Proline-Rich Peptide,Domain, Proline-Rich Protein,Domains, Proline-Rich Peptide,Domains, Proline-Rich Protein,Peptide Domain, Proline-Rich,Peptide Domains, Proline-Rich,Proline Rich Peptide Domains,Proline Rich Protein Domains,Proline-Rich Peptide Domain,Proline-Rich Protein Domain,Protein Domain, Proline-Rich,Protein Domains, Proline-Rich
D055273 Salivary Proline-Rich Proteins A family of proline-rich proteins that constitute the majority of the protein component of SALIVA. Salivary proline-rich proteins occur as acidic, basic and glycosylated basic proteins. They perform a variety of functions such as adhering to the acquired ENAMEL PELLICLE, acting as lubricants and precipitating TANNINS. Salivary Acidic Proline-Rich Proteins,Salivary Basic Proline-Rich Proteins,Salivary Glycosylated-Basic Proline-Rich Proteins,Proline-Rich Proteins, Salivary,Salivary Acidic Proline Rich Proteins,Salivary Basic Proline Rich Proteins,Salivary Glycosylated Basic Proline Rich Proteins,Salivary Proline Rich Proteins

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