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

 Previous Article  |  Next Article 

Infection and Immunity, September 1998, p. 4403-4410, Vol. 66, No. 9
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

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

K. Hallberg, C. Holm, U. Öhman, and N. Strömberg*

Department of Cariology, Faculty of Odontology, University of Umeå, S-901 87 Umeå, Sweden

Received 27 February 1998/Returned for modification 21 April 1998/Accepted 24 June 1998

Actinomyces naeslundii genospecies 1 and 2 bind to acidic proline-rich proteins (APRPs) and statherin via type 1 fimbriae and to beta -linked galactosamine (GalNAcbeta ) structures via type 2 fimbriae. In addition, A. naeslundii displays two types of binding specificity for both APRPs-statherin and GalNAcbeta , while Actinomyces odontolyticus binds to unknown structures. To study the molecular basis for these binding specificities, DNA fragments spanning the entire or central portions of fimP (type 1) and fimA (type 2) fimbrial subunit genes were amplified by PCR from strains of genospecies 1 and 2 and hybridized with DNA from two independent collections of oral Actinomyces isolates. Isolates of genospecies 1 and 2 and A. odontolyticus, but no other Actinomyces species, were positive for hybridization with fimP and fimA full-length probes irrespective of binding to APRPs and statherin, GalNAcbeta , or unknown structures. Isolates of genospecies 1 and 2, with deviating patterns of GalNAcbeta 1-3Galalpha -O-ethyl-inhibitable coaggregation with Streptococcus oralis Ss34 and MPB1, were distinguished by a fimA central probe from genospecies 1 and 2, respectively. Furthermore, isolates of genospecies 1 and 2 displaying preferential binding to APRPs over statherin were positive with a fimP central probe, while a genospecies 2 strain with the opposite binding preference was not. The sequences of fimP and fimA central gene segments were highly conserved among isolates with the same, but diversified between those with a variant, binding specificity. In conclusion, A. naeslundii exhibits variant fimP and fimA genes corresponding to diverse APRP and GalNAcbeta specificities, respectively, while A. odontolyticus has a genetically related but distinct adhesin binding specificity.

* Corresponding author. Mailing address: Department of Cariology, Faculty of Odontology, Umeå University, S-901 87 Umeå, Sweden. Phone: 46 90 7856030. Fax: 46 90 770580. E-mail: Nicklas.Stromberg{at}oralbio.umu.se.

Infection and Immunity, September 1998, p. 4403-4410, Vol. 66, No. 9
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Loimaranta, V., Jakubovics, N. S., Hytonen, J., Finne, J., Jenkinson, H. F., Stromberg, N. (2005). Fluid- or Surface-Phase Human Salivary Scavenger Protein gp340 Exposes Different Bacterial Recognition Properties. Infect. Immun. 73: 2245-2252 [Abstract] [Full Text]  
  • Niemi, L. D., Johansson, I. (2004). Salivary Statherin Peptide-Binding Epitopes of Commensal and Potentially Infectious Actinomyces spp. Delineated by a Hybrid Peptide Construct. Infect. Immun. 72: 782-787 [Abstract] [Full Text]  
  • Li, T., Khah, M. K., Slavnic, S., Johansson, I., Stromberg, N. (2001). Different Type 1 Fimbrial Genes and Tropisms of Commensal and Potentially Pathogenic Actinomyces spp. with Different Salivary Acidic Proline-Rich Protein and Statherin Ligand Specificities. Infect. Immun. 69: 7224-7233 [Abstract] [Full Text]  
  • Stenudd, C., Nordlund, A., Ryberg, M., Johansson, I., KallestAl, C., Stromberg, N. (2001). The Association of Bacterial Adhesion with Dental Caries. JDR 80: 2005-2010 [Abstract]  
  • Li, T., Bratt, P., Jonsson, A. P., Ryberg, M., Johansson, I., Griffiths, W. J., Bergman, T., Stromberg, N. (2000). Possible Release of an ArgGlyArgProGln Pentapeptide with Innate Immunity Properties from Acidic Proline-Rich Proteins by Proteolytic Activity in Commensal Streptococcus and Actinomyces Species. Infect. Immun. 68: 5425-5429 [Abstract] [Full Text]  
  • Bratt, P., Boren, D., Boren, T., Stromberg, N. (1999). Secretory Immunoglobulin A Heavy Chain Presents Gal{beta}1-3GalNAc Binding Structures for Actinomyces naeslundii genospecies 1. JDR 78: 1238-1244 [Abstract]  
  • 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]  
  • Navarre, W. W., Schneewind, O. (1999). Surface Proteins of Gram-Positive Bacteria and Mechanisms of Their Targeting to the Cell Wall Envelope. Microbiol. Mol. Biol. Rev. 63: 174-229 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»