Salivary Receptors for GalNAc Beta-sensitive Adherence of Actinomyces Spp.: Evidence for Heterogeneous GalNAc Beta and Proline-rich Protein Receptor Properties

Overview

Journal Infect Immun

Publisher American Society for Microbiology

Specialty Allergy & Immunology

Date 1992 Aug 1

PMID 1322372

Citations 9

Authors

N Stromberg

T Boren

A Carlen

J Olsson

Affiliations

Soon will be listed here.

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.

Citing Articles

Application of MLST and pilus gene sequence comparisons to investigate the population structures of Actinomyces naeslundii and Actinomyces oris.

Henssge U, Do T, Gilbert S, Cox S, Clark D, Wickstrom C PLoS One. 2011; 6(6):e21430.

PMID: 21738661 PMC: 3127948. DOI: 10.1371/journal.pone.0021430.

Sequence analyses of fimbriae subunit FimA proteins on Actinomyces naeslundii genospecies 1 and 2 and Actinomyces odontolyticus with variant carbohydrate binding specificities.

Drobni M, Hallberg K, Ohman U, Birve A, Persson K, Johansson I BMC Microbiol. 2006; 6:43.

PMID: 16686953 PMC: 1473193. DOI: 10.1186/1471-2180-6-43.

Strains of Actinomyces naeslundii and Actinomyces viscosus exhibit structurally variant fimbrial subunit proteins and bind to different peptide motifs in salivary proteins.

Li T, Johansson I, Hay D, Stromberg N Infect Immun. 1999; 67(5):2053-9.

PMID: 10225854 PMC: 115937. DOI: 10.1128/IAI.67.5.2053-2059.1999.

Actinomyces naeslundii displays variant fimP and fimA fimbrial subunit genes corresponding to different types of acidic proline-rich protein and beta-linked galactosamine binding specificity.

Hallberg K, Holm C, Ohman U, Stromberg N Infect Immun. 1998; 66(9):4403-10.

PMID: 9712794 PMC: 108532. DOI: 10.1128/IAI.66.9.4403-4410.1998.

Binding of Porphyromonas gingivalis fimbriae to proline-rich glycoproteins in parotid saliva via a domain shared by major salivary components.

Amano A, Shizukuishi S, Horie H, Kimura S, Morisaki I, Hamada S Infect Immun. 1998; 66(5):2072-7.

PMID: 9573091 PMC: 108165. DOI: 10.1128/IAI.66.5.2072-2077.1998.

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