Home LiteratureArticle Details
PMID: 1322372 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Salivary receptors for GalNAc beta-sensitive adherence of Actinomyces spp.: evidence for heterogeneous GalNAc beta and proline-rich protein receptor properties.

Infection and immunity ·Vol. 60 ·No. 8 ·1992-08-00 ·Pages 3278-86

Strömberg N, Borén T, Carlén A, Olsson J

Abstract

The receptors for GalNAc beta 1-3Gal alpha Oethyl (GalNAc beta)-sensitive adherence of Actinomyces strains to salivary pellicles were investigated. Parotid and submaxillary saliva from one individual was size fractionated and utilized in hydroxyapatite adherence assays with Actinomyces naeslundii 12104 and A. viscosus 19246 and LY7 with and without GalNAc beta. Three parotid salivary fractions, the high-molecular-weight, acidic proline-rich protein (PRP), and statherin fractions, promote GalNAc beta-sensitive adherence of strain 12104, whereas only the high-molecular-weight fraction of submaxillary saliva promotes such adherence. In contrast, strain LY7, possessing a variant GalNAc beta specificity, shows GalNAc beta-sensitive adherence to the leading and trailing regions of the submaxillary PRP fractions but less distinct adherence to the parotid and submaxillary high-molecular-weight fractions. In addition, the PRP and statherin fractions promote adherence of strains LY7 and 19246 that is not inhibited by GalNAc beta. However, whereas strain LY7 binds more strongly to the PRP fraction than to the statherin fraction, strain 19246 binds preferentially to the statherin fractions of parotid and submaxillary saliva. These salivary protein fractions were analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and immunostained to detect glycosylated proteins. The different salivary receptor properties are paralleled by different glycosylation patterns. The variable GalNAc beta specificities may have evolved to match different salivary glycosylation patterns, and PRP and statherin binding properties seem to be heterogeneous among the Actinomyces strains.

MeSH Terms
Acetylgalactosamine/metabolism Actinomyces/physiology Adult Bacterial Adhesion Electrophoresis, Polyacrylamide Gel Glycosylation Humans Peptides/metabolism Proline-Rich Protein Domains Receptors, Cell Surface/metabolism Saliva/chemistry,metabolism,microbiology
Chemicals
Peptides Receptors, Cell Surface Acetylgalactosamine
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Strömberg N
Department of Cardiology, Faculty of Odontology, University of Göteborg, Sweden.
Borén T
Carlén A
Olsson J
References (41)
41 references, click to expand
  1. Characterization of the binding of propionibacterium granulosum to glycosphingolipids adsorbed on surfaces. An apparent recognition of lactose which is dependent on the ceramide structure.
    J Biol Chem. 1990 Jul 5;265(19):11244-50 PMID: 2358460
  2. Secretory immunoglobulin A carries oligosaccharide receptors for Escherichia coli type 1 fimbrial lectin.
    Infect Immun. 1990 Sep;58(9):3073-7 PMID: 2201644
  3. A 160-kilodalton epithelial cell surface glycoprotein recognized by plant lectins that inhibit the adherence of Actinomyces naeslundii.
    Infect Immun. 1986 Jun;52(3):840-5 PMID: 2872166
  4. Human salivary acidic proline-rich proteins and statherin promote the attachment of Actinomyces viscosus LY7 to apatitic surfaces.
    Infect Immun. 1988 Feb;56(2):439-45 PMID: 2892794
  5. Adsorbed salivary proline-rich protein 1 and statherin: receptors for type 1 fimbriae of Actinomyces viscosus T14V-J1 on apatitic surfaces.
    Infect Immun. 1988 Nov;56(11):2990-3 PMID: 2902013
  6. Structural aspects of salivary glycoproteins.
    J Dent Res. 1987 Feb;66(2):436-41 PMID: 3305626
  7. Longitudinal microbiological investigation of a hospitalized population of older adults with a high root surface caries risk.
    J Dent Res. 1985 Dec;64(12):1377-81 PMID: 3865948
  8. Cleavage of structural proteins during the assembly of the head of bacteriophage T4.
    Nature. 1970 Aug 15;227(5259):680-5 PMID: 5432063
  9. Carbohydrate-binding sites of the mannose-specific fimbrial lectins of enterobacteria.
    Infect Immun. 1984 Mar;43(3):1088-90 PMID: 6142000
  10. Lectin-dependent attachment of Actinomyces naeslundii to receptors on epithelial cells.
    Infect Immun. 1984 Nov;46(2):459-64 PMID: 6150008
  11. Sialidase-enhanced lectin-like mechanism for Actinomyces viscosus and Actinomyces naeslundii hemagglutination.
    Infect Immun. 1980 Feb;27(2):335-43 PMID: 6769798
  12. Development of a selective medium for detection and enumeration of Actinomyces viscosus and Actinomyces naeslundii in dental plaque.
    J Clin Microbiol. 1982 Feb;15(2):253-9 PMID: 7068820
  13. Attachment of Bacteroides melaninogenicus subsp. asaccharolyticus to oral surfaces and its possible role in colonization of the mouth and of periodontal pockets.
    Infect Immun. 1978 Jan;19(1):254-64 PMID: 24002
  14. Subgingival microflora and periodontitis.
    J Periodontal Res. 1976 Feb;11(1):1-18 PMID: 130475
  15. Neuraminidase-dependent hamagglutination of human erythrocytes by human strains of Actinomyces viscosus and Actinomyces naeslundii.
    Infect Immun. 1979 Nov;26(2):563-72 PMID: 232691
  16. Relative proportions of Actinomyces viscosus and Actinomyces naeslundii in dental plaques collected from single sites.
    J Dent Res. 1978 Apr;57(4):550 PMID: 280567
  17. Specificity of coaggregation reactions between human oral streptococci and strains of Actinomyces viscosus or Actinomyces naeslundii.
    Infect Immun. 1979 Jun;24(3):742-52 PMID: 468376
  18. Actinomyces tissue specificity may depend on differences in receptor specificity for GalNAc beta-containing glycoconjugates.
    Infect Immun. 1992 Aug;60(8):3268-77 PMID: 1322371
  19. Host-specificity of uropathogenic Escherichia coli depends on differences in binding specificity to Gal alpha 1-4Gal-containing isoreceptors.
    EMBO J. 1990 Jun;9(6):2001-10 PMID: 1693334
  20. Structure and bacterial receptor activity of a human salivary proline-rich glycoprotein.
    J Biol Chem. 1991 Sep 15;266(26):17358-68 PMID: 1894623
  21. Microflora associated with experimental root surface caries in humans.
    Infect Immun. 1990 Jun;58(6):1628-33 PMID: 2341169
  22. Characterization of the binding of Actinomyces naeslundii (ATCC 12104) and Actinomyces viscosus (ATCC 19246) to glycosphingolipids, using a solid-phase overlay approach.
    J Biol Chem. 1990 Jul 5;265(19):11251-8 PMID: 2358461
  23. Relative adherence of Bacteroides species and strains to Actinomyces viscosus on saliva-coated hydroxyapatite.
    J Dent Res. 1989 Sep;68(9):1308-12 PMID: 2550532
  24. A human salivary protein which promotes adhesion of Streptococcus mutans serotype c strains to hydroxyapatite.
    Infect Immun. 1989 Dec;57(12):3702-7 PMID: 2807544
  25. Actinomyces adsorption mediated by type-1 fimbriae.
    J Dent Res. 1986 Sep;65(9):1166-8 PMID: 2874164
  26. Identification of carbohydrate structures that are possible receptors for Neisseria gonorrhoeae.
    Proc Natl Acad Sci U S A. 1988 Jul;85(13):4902-6 PMID: 2898784
  27. Mutants of Actinomyces viscosus T14V lacking type 1, type 2, or both types of fimbriae.
    Infect Immun. 1988 Nov;56(11):2984-9 PMID: 2902012
  28. The primary structures of six human salivary acidic proline-rich proteins (PRP-1, PRP-2, PRP-3, PRP-4, PIF-s and PIF-f).
    Biochem J. 1988 Oct 1;255(1):15-21 PMID: 3196309
  29. Microbiology of the early colonization of human enamel and root surfaces in vivo.
    Scand J Dent Res. 1987 Oct;95(5):369-80 PMID: 3477852
  30. Quantitation of glycoproteins on electroblots using the biotin-streptavidin complex.
    Anal Biochem. 1987 May 15;163(1):204-9 PMID: 3619021
  31. Interbacterial aggregation of plaque bacteria.
    Arch Oral Biol. 1970 Dec;15(12):1397-400 PMID: 5280139
  32. Specific inhibition of adsorption of Actinomyces viscosus T14V to saliva-treated hydroxyapatite by antibody against type 1 fimbriae.
    Infect Immun. 1984 Feb;43(2):497-501 PMID: 6141143
  33. The function and distribution of different fimbriae on strains of Actinomyces viscosus and Actinomyces naeslundii.
    J Dent Res. 1984 Mar;63(3):393-6 PMID: 6142065
  34. Exclusive presence of lactose-sensitive fimbriae on a typical strain (WVU45) of Actinomyces naeslundii.
    Infect Immun. 1984 Nov;46(2):453-8 PMID: 6150007
  35. Interference of Salivary immunoglobulin A antibodies and other salivary fractions with adherence of Streptococcus mutans to hydroxyapatite.
    Infect Immun. 1982 Aug;37(2):401-6 PMID: 6288559
  36. Structural preferences of beta-galactoside-reactive lectins on Actinomyces viscosus T14V and Actinomyces naeslundii WVU45.
    Infect Immun. 1983 Aug;41(2):848-50 PMID: 6874075
  37. Differences in the adsorptive behavior of human strains of Actinomyces viscosus and Actinomyces naeslundii to saliva-treated hydroxyapatite surfaces.
    Infect Immun. 1981 Jan;31(1):261-6 PMID: 7216448
  38. Lactose-reversible coaggregation between oral actinomycetes and Streptococcus sanguis.
    Infect Immun. 1981 Jul;33(1):95-102 PMID: 7263074
  39. Establishment and distribution of Actinomyces viscosus and Actinomyces naeslundii in the human oral cavity.
    Infect Immun. 1976 Nov;14(5):1119-24 PMID: 977124
  40. Saccharide orientation at the cell surface affects glycolipid receptor function.
    Proc Natl Acad Sci U S A. 1991 Oct 15;88(20):9340-4 PMID: 1681550
  41. Factors affecting binding of galacto ligands to Actinomyces viscosus lectin.
    Infect Immun. 1985 Jan;47(1):61-7 PMID: 2578122
Article Info
Journal
Infection and immunity
Abbr.
Infect Immun
ISSN
0019-9567
DOI
10.1128/iai.60.8.3278-3286.1992
Published
1992-08-00
Pages
3278-86
Language
English
Region
United States
NLM ID
0246127
PMCID
PMC257312
Subset
IM
External Links
PubMed source DOI: 10.1128/iai.60.8.3278-3286.1992 PMC Full Text View journal details
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: product@genelibs.com

Copyright © 2026.Genelibs Jinan Honghui Biotechnology Co., Ltd. 鲁ICP备20007159号-2