Role of cryptic receptors (cryptitopes) in bacterial adhesion to oral surfaces.
Progress in characterizing the receptors that promote bacterial attachment to teeth and oral epithelial cells has suggested that hidden molecular segments may frequently be involved. Such cryptic receptors, referred to as 'cryptitopes', may become exposed by several mechanisms. Hidden segments of salivary acidic proline-rich proteins evidently become exposed when the molecules undergo a conformational change as they adsorb to apatitic mineral. Adhesins of Actinomyces viscosus and certain other prominent dental plaque bacteria are able to bind to these cryptitopes, and this enables these organisms to bind to proline-rich proteins on apatitic surfaces while avoiding interactions with these proteins in solution. Cryptitopes may also become exposed as a result of enzymatic action. Thus, several bacteria, including Fusobacterium nucleatum, Eikenella corrodens, A. viscosus, A. naeslundii and Bacteroides intermedius, have adhesins that bind to galactosyl receptors which become exposed after treatment with neuraminidase. Similarly, the adhesion of some Gram-negative bacteria, such as Bact. gingivalis, is enhanced when tissue surfaces are treated with certain proteases, or lysosomal enzymes derived from human polymorphonuclear leucocytes. It seems likely that elevated levels of enzymes present in gingival fluid as sequelae of poor oral hygiene and gingivitis may generate cryptitopes for potentially periodontopathic bacteria, and thereby contribute to modulation of the gingival flora.
Gibbons
R J
RJ
Forsyth Dental Center, Boston, MA 02115.
Hay
D I
DI
Childs
W C
WC
Davis
G
G
D000190:Actinomyces / Q000502:physiology; D000293:Adolescent; D000327:Adsorption; D000328:Adult; D001031:Apatites / Q000737:chemistry; D001422:Bacterial Adhesion / Q000502:physiology*; D018407:Bacterial Physiological Phenomena; D001426:Bacterial Proteins / Q000737:chemistry*; D001439:Bacteroides / Q000502:physiology; D003741:Dental Deposits / Q000503:physiopathology; D010450:Endopeptidases / Q000494:pharmacology; D004847:Epithelial Cells; D004848:Epithelium / Q000737:chemistry / Q000502:physiology; D006801:Humans; D008247:Lysosomes / Q000201:enzymology; D008875:Middle Aged; D009061:Mouth Mucosa / Q000737:chemistry / Q000502:physiology*; D019158:N-Acetylneuraminic Acid; D009439:Neuraminidase / Q000494:pharmacology; D010455:Peptides / Q000737:chemistry; D011392:Proline / Q000737:chemistry; D055232:Proline-Rich Protein Domains; D011971:Receptors, Immunologic / Q000187:drug effects / Q000502:physiology*; D055273:Salivary Proline-Rich Proteins; D012471:Salivary Proteins and Peptides / Q000737:chemistry; D012794:Sialic Acids / Q000032:analysis
D001031:Apatites; D001426:Bacterial Proteins; C524536:PRH1 protein, human; D010455:Peptides; D011971:Receptors, Immunologic; D055273:Salivary Proline-Rich Proteins; D012471:Salivary Proteins and Peptides; D012794:Sialic Acids; C047105:bacterial adhesin receptor; D011392:Proline; D009439:Neuraminidase; D010450:Endopeptidases; D019158:N-Acetylneuraminic Acid