This Article Full Text 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 Loimaranta, V. Articles by Strömberg, N. Search for Related Content PubMed PubMed Citation Articles by Loimaranta, V. Articles by Strömberg, N.

 Previous Article  |  Next Article 

Infection and Immunity, April 2005, p. 2245-2252, Vol. 73, No. 4
0019-9567/05/$08.00+0     doi:10.1128/IAI.73.4.2245-2252.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Fluid- or Surface-Phase Human Salivary Scavenger Protein gp340 Exposes Different Bacterial Recognition Properties

Department of Cariology, Umeå University, Umeå, Sweden,¹ Department of Oral and Dental Science, University of Bristol, Bristol, United Kingdom,² Department of Medical Biochemistry and Molecular Biology, University of Turku, Turku, Finland³

Received 1 July 2004/ Returned for modification 28 September 2004/ Accepted 20 December 2004

Salivary scavenger receptor cysteine-rich protein gp340 aggregates streptococci and other bacteria as part of the host innate defense system at mucosal surfaces. In this article, we have investigated the properties of fluid-phase gp340 and hydroxylapatite surface-adsorbed gp340 in aggregation and adherence, respectively, of viridans group streptococci (e.g., Streptococcus gordonii and Streptococcus mutans), non-viridans group streptococci (e.g., Streptococcus pyogenes and Streptococcus suis), and oral Actinomyces. Fluid-phase gp340 and surface-phase gp340 bioforms were differentially recognized by streptococci, which formed three phenotypic groupings according to their modes of interaction with gp340. Group I streptococci were aggregated by and adhered to gp340, and group II streptococci preferentially adhered to surface-bound gp340, while group III streptococci were preferentially aggregated by gp340. Each species of Streptococcus tested was found to contain strains representative of at least two of these gp340 interaction groupings. The gp340 interaction modes I to III and sugar specificities of gp340 binding strains coincided for several species. Many gp340 interactions were sialidase sensitive, and each of the interaction modes (I to III) for S. gordonii was correlated with a variant of sialic acid specificity. Adherence of S. gordonii DL1 (Challis) to surface-bound gp340 was dependent upon expression of the sialic acid binding adhesin Hsa. However, aggregation of cells by fluid-phase gp340 was independent of Hsa and involved SspA and SspB (antigen I/II family) polypeptides. Conversely, both gp340-mediated aggregation and adherence of S. mutans NG8 involved antigen I/II polypeptide. Deletion of the mga virulence regulator gene in S. pyogenes resulted in increased cell aggregation by gp340. These results suggest that salivary gp340 recognizes different bacterial receptors according to whether gp340 is present in the fluid phase or surface bound. This phase-associated differential recognition by gp340 of streptococcal species of different levels of virulence and diverse origins may mediate alternative host responses to commensal or pathogenic bacterial phenotypes.

Editor: V. J. DiRita

This article has been cited by other articles:

• Ahn, S.-J., Ahn, S.-J., Wen, Z. T., Brady, L. J., Burne, R. A. (2008). Characteristics of Biofilm Formation by Streptococcus mutans in the Presence of Saliva. Infect. Immun. 76: 4259-4268 [Abstract] [Full Text]  
• van der Mei, H. C., Rustema-Abbing, M., de Vries, J., Busscher, H. J. (2008). Bond Strengthening in Oral Bacterial Adhesion to Salivary Conditioning Films. Appl. Environ. Microbiol. 74: 5511-5515 [Abstract] [Full Text]  
• Crowley, P. J., Seifert, T. B., Isoda, R., van Tilburg, M., Oli, M. W., Robinette, R. A., McArthur, W. P., Bleiweis, A. S., Brady, L. J. (2008). Requirements for Surface Expression and Function of Adhesin P1 from Streptococcus mutans. Infect. Immun. 76: 2456-2468 [Abstract] [Full Text]  
• Nobbs, A. H., Zhang, Y., Khammanivong, A., Herzberg, M. C. (2007). Streptococcus gordonii Hsa Environmentally Constrains Competitive Binding by Streptococcus sanguinis to Saliva-Coated Hydroxyapatite. J. Bacteriol. 189: 3106-3114 [Abstract] [Full Text]  
• Zhang, S., Green, N. M., Sitkiewicz, I., LeFebvre, R. B., Musser, J. M. (2006). Identification and Characterization of an Antigen I/II Family Protein Produced by Group A Streptococcus. Infect. Immun. 74: 4200-4213 [Abstract] [Full Text]  
• Takamatsu, D., Bensing, B. A., Prakobphol, A., Fisher, S. J., Sullam, P. M. (2006). Binding of the Streptococcal Surface Glycoproteins GspB and Hsa to Human Salivary Proteins. Infect. Immun. 74: 1933-1940 [Abstract] [Full Text]  
• Allaker, R.P., Dymock, D. (2005). Proceedings of the 8th European Oral Microbiology Workshop. Adv. Dent. Res. 18: 27-33 [Full Text]  
• Allaker, R.P., Dymock, D. (2005). Proceedings of the 8th European Oral Microbiology Workshop. fake Adv Dent Res 18: 27-33 [Full Text]  
• Jakubovics, N. S., Kerrigan, S. W., Nobbs, A. H., Stromberg, N., van Dolleweerd, C. J., Cox, D. M., Kelly, C. G., Jenkinson, H. F. (2005). Functions of Cell Surface-Anchored Antigen I/II Family and Hsa Polypeptides in Interactions of Streptococcus gordonii with Host Receptors. Infect. Immun. 73: 6629-6638 [Abstract] [Full Text]  
• Hakkarainen, J., Toivanen, M., Leinonen, A., Frangsmyr, L., Stromberg, N., Lapinjoki, S., Nassif, X., Tikkanen-Kaukanen, C. (2005). Human and Bovine Milk Oligosaccharides Inhibit Neisseria meningitidis Pili Attachment In Vitro. J. Nutr. 135: 2445-2448 [Abstract] [Full Text]