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« Previous AbstractAnalysis of functional domains of the Enterococcus faecalis pheromone-induced surface protein aggregation substance    Next AbstractNucleotide excision repair in cellular chromatin: studies with yeast from nucleotide to gene to genome »

Infect Immun


Title:"The aggregation domain of aggregation substance, not the RGD motifs, is critical for efficient internalization by HT-29 enterocytes"
Author(s):Waters CM; Wells CL; Dunny GM;
Address:"Department of Microbiology, University of Minnesota Medical School, 1420 Delaware Street SE, Minneapolis, MN 55455, USA"
Journal Title:Infect Immun
Year:2003
Volume:71
Issue:10
Page Number:5682 - 5689
DOI: 10.1128/IAI.71.10.5682-5689.2003
ISSN/ISBN:0019-9567 (Print) 1098-5522 (Electronic) 0019-9567 (Linking)
Abstract:"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"
Keywords:"Bacterial Proteins/*chemistry/genetics/*physiology Base Sequence Cell Line DNA, Bacterial/genetics Enterococcus faecalis/genetics/*pathogenicity/physiology Enterocytes/microbiology Gram-Positive Bacterial Infections/etiology Humans Membrane Proteins/*chem;"
Notes:"MedlineWaters, Christopher M Wells, Carol L Dunny, Gary M eng HL 51987/HL/NHLBI NIH HHS/ 5T32 AI 07421-05/AI/NIAID NIH HHS/ R01 HL051987/HL/NHLBI NIH HHS/ GM 066751/GM/NIGMS NIH HHS/ T32 AI007421/AI/NIAID NIH HHS/ R01 GM066751/GM/NIGMS NIH HHS/ Research Support, U.S. Gov't, P.H.S. 2003/09/23 Infect Immun. 2003 Oct; 71(10):5682-9. doi: 10.1128/IAI.71.10.5682-5689.2003"

 
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