This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Strömberg, N Articles by Olsson, J Search for Related Content PubMed PubMed Citation Articles by Strömberg, N Articles by Olsson, J

 Previous Article  |  Next Article 

Infect Immun. 1992 August; 60(8): 3278-3286

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

Department of Cardiology, Faculty of Odontology, University of Göteborg, Sweden.

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.

This article has been cited by other articles:

• Sekine, S., Kataoka, K., Tanaka, M., Nagata, H., Kawakami, T., Akaji, K., Aimoto, S., Shizukuishi, S. (2004). Active domains of salivary statherin on apatitic surfaces for binding to Fusobacterium nucleatum cells. Microbiology 150: 2373-2379 [Abstract] [Full Text]  
• Li, T., Johansson, I., Hay, D. I., Stromberg, N. (1999). Strains of Actinomyces naeslundii and Actinomyces viscosus Exhibit Structurally Variant Fimbrial Subunit Proteins and Bind to Different Peptide Motifs in Salivary Proteins. Infect. Immun. 67: 2053-2059 [Abstract] [Full Text]  
• Hallberg, K., Holm, C., Ohman, U., Stromberg, N. (1998). 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. Infect. Immun. 66: 4403-4410 [Abstract] [Full Text]  
• Amano, A., Shizukuishi, S., Horie, H., Kimura, S., Morisaki, I., Hamada, S. (1998). Binding of Porphyromonas gingivalis Fimbriae to Proline-Rich Glycoproteins in Parotid Saliva via a Domain Shared by Major Salivary Components. Infect. Immun. 66: 2072-2077 [Abstract] [Full Text]