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 Yeung, M. K.
Right arrow Articles by Ragsdale, P. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Yeung, M. K.
Right arrow Articles by Ragsdale, P. A.

 Previous Article  |  Next Article 

Infect Immun, April 1998, p. 1482-1491, Vol. 66, No. 4
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Identification of a Gene Involved in Assembly of Actinomyces naeslundii T14V Type 2 Fimbriae

Maria K. Yeung,1,* Jacob A. Donkersloot,2 John O. Cisar,2 and Pamela A. Ragsdale1

Department of Pediatric Dentistry, The University of Texas Health Science Center at San Antonio, San Antonio, Texas 782841 and Oral Infection and Immunity Branch, National Institute of Dental Research, National Institutes of Health, Bethesda, Maryland 208922

Received 10 September 1997/Returned for modification 6 November 1997/Accepted 23 December 1997

The nucleotide sequence of the Actinomyces naeslundii T14V type 2 fimbrial structural subunit gene, fimA, and the 3' flanking DNA region was determined. The fimA gene encoded a 535-amino-acid precursor subunit protein (FimA) which included both N-terminal leader and C-terminal cell wall sorting sequences. A second gene, designated orf365, that encoded a 365-amino-acid protein which contained a putative transmembrane segment was identified immediately 3' to fimA. Mutants in which either fimA or orf365 was replaced with a kanamycin resistance gene did not participate in type 2 fimbriae-mediated coaggregation with Streptococcus oralis 34. Type 2 fimbrial antigen was not detected in cell extracts of the fimA mutant by Western blotting with anti-A. naeslundii type 2 fimbrial antibody, but the subunit protein was detected in extracts of the orf365 mutant. The subunit protein detected in this mutant also was immunostained by an antibody raised against a synthetic peptide representing the C-terminal 20 amino acid residues of the predicted FimA. The antipeptide antibody reacted with FimA isolated from the recombinant Escherichia coli clone containing fimA but did not react with purified type 2 fimbriae in extracts of the wild-type strain. These results indicate that synthesis of type 2 fimbriae in A. naeslundii T14V may involve posttranslational cleavage of both the N-terminal and C-terminal peptides of the precursor subunit and also the expression of orf365.


* Corresponding author. Mailing address: Department of Pediatric Dentistry, 7703 Floyd Curl Dr., San Antonio, TX 78284. Phone: (210) 567-3536. Fax: (210) 567-6603. E-mail: yeung{at}uthscsa.edu.




This article has been cited by other articles:

  • Hendrickx, A. P. A., Bonten, M. J. M., van Luit-Asbroek, M., Schapendonk, C. M. E., Kragten, A. H. M., Willems, R. J. L. (2008). Expression of two distinct types of pili by a hospital-acquired Enterococcus faecium isolate. Microbiology 154: 3212-3223 [Abstract] [Full Text]  
  • Chen, P., Cisar, J. O., Hess, S., Ho, J. T. C., Leung, K. P. (2007). Amended Description of the Genes for Synthesis of Actinomyces naeslundii T14V Type 1 Fimbriae and Associated Adhesin. Infect. Immun. 75: 4181-4185 [Abstract] [Full Text]  
  • Marraffini, L. A., DeDent, A. C., Schneewind, O. (2006). Sortases and the Art of Anchoring Proteins to the Envelopes of Gram-Positive Bacteria. Microbiol. Mol. Biol. Rev. 70: 192-221 [Abstract] [Full Text]  
  • Levesque, C., Vadeboncoeur, C., Frenette, M. (2004). The csp operon of Streptococcus salivarius encodes two predicted cell-surface proteins, one of which, CspB, is associated with the fimbriae. Microbiology 150: 189-198 [Abstract] [Full Text]  
  • Lee, S. G., Pancholi, V., Fischetti, V. A. (2002). Characterization of a Unique Glycosylated Anchor Endopeptidase That Cleaves the LPXTG Sequence Motif of Cell Surface Proteins of Gram-positive Bacteria. J. Biol. Chem. 277: 46912-46922 [Abstract] [Full Text]  
  • Schell, M. A., Karmirantzou, M., Snel, B., Vilanova, D., Berger, B., Pessi, G., Zwahlen, M.-C., Desiere, F., Bork, P., Delley, M., Pridmore, R. D., Arigoni, F. (2002). The genome sequence of Bifidobacterium longum reflects its adaptation to the human gastrointestinal tract. Proc. Natl. Acad. Sci. USA 99: 14422-14427 [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]  
  • Bergeron, L. J., Burne, R. A. (2001). Roles of Fructosyltransferase and Levanase-Sucrase of Actinomyces naeslundii in Fructan and Sucrose Metabolism. Infect. Immun. 69: 5395-5402 [Abstract] [Full Text]  
  • Hui Wu, , Fives-Taylor, P. M. (2001). Molecular Strategies for Fimbrial Expression and Assembly. CROBM 12: 101-115 [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]  
  • Yeung, M.K. (1999). Molecular and Genetic Analyses of Actinomyces SPP. CROBM 10: 120-138 [Abstract] [Full Text]