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 Waters, C. M. Articles by Dunny, G. M. Search for Related Content PubMed PubMed Citation Articles by Waters, C. M. Articles by Dunny, G. M.

 Previous Article  |  Next Article 

Infection and Immunity, October 2003, p. 5682-5689, Vol. 71, No. 10
0019-9567/03/$08.00+0     DOI: 10.1128/IAI.71.10.5682-5689.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

The Aggregation Domain of Aggregation Substance, Not the RGD Motifs, Is Critical for Efficient Internalization by HT-29 Enterocytes

Departments of Microbiology,¹ Laboratory Medicine & Pathology, University of Minnesota Medical School, Minneapolis, Minnesota 55455²

Received 4 April 2003/ Returned for modification 9 June 2003/ Accepted 15 July 2003

Aggregation substance (AS), a surface protein encoded on the pheromone-inducible plasmids of Enterococcus faecalis, has been shown to increase adherence and internalization into a number of different cell types, presumably through integrin binding mediated by the N-terminal RGD motif of AS. Here, defined mutations constructed in Asc10, the AS encoded by the plasmid pCF10, are analyzed for their ability to promote increased internalization levels into HT-29 enterocytes. The results clearly show that the previously identified Asc10 functional domain, not the RGD motifs, is critical for Asc10-directed internalization of E. faecalis into HT-29 enterocytes. Also, expression of Asc10 in the nonaggregating E. faecalis strain INY3000 is unable to mediate HT-29 internalization. However, Asc10-expressing E. faecalis cells are not internalized as bacterial aggregates, suggesting bacterial aggregation is not a prerequisite for HT-29 internalization. These data show that Asc10 directs internalization of E. faecalis into HT-29 enterocytes through a non-RGD-dependent mechanism.

Editor: J. D. Clements

This article has been cited by other articles:

• Chen, Y., Zhang, X., Manias, D., Yeo, H.-J., Dunny, G. M., Christie, P. J. (2008). Enterococcus faecalis PcfC, a Spatially Localized Substrate Receptor for Type IV Secretion of the pCF10 Transfer Intermediate. J. Bacteriol. 190: 3632-3645 [Abstract] [Full Text]  
• Chandler, J. R., Hirt, H., Dunny, G. M. (2005). A paracrine peptide sex pheromone also acts as an autocrine signal to induce plasmid transfer and virulence factor expression in vivo. Proc. Natl. Acad. Sci. USA 102: 15617-15622 [Abstract] [Full Text]  
• Zeng, J., Teng, F., Murray, B. E. (2005). Gelatinase Is Important for Translocation of Enterococcus faecalis across Polarized Human Enterocyte-Like T84 Cells. Infect. Immun. 73: 1606-1612 [Abstract] [Full Text]  
• Kayaoglu, G., Orstavik, D. (2004). VIRULENCE FACTORS OF ENTEROCOCCUS FAECALIS: RELATIONSHIP TO ENDODONTIC DISEASE. Crit. Rev. Oral Biol. Med. 15: 308-320 [Abstract] [Full Text]