Document Detail

Impact of actin on adhesion and translocation of Enterococcus faecalis.
MedLine Citation:
PMID:  24362949     Owner:  NLM     Status:  Publisher    
This study focuses on the impact of actin on adhesion and translocation of Enterococcus (E.) faecalis OG1RF, E. faecalis Symbioflor(®), and E. faecalis V583. Insight into the role of actin aggregation in the mediation of bacterial adhesion and translocation was provided by a two-chamber translocation assay, which employed Ptk6 cells. Determination of translocation rates, cytochalasin D treatment, and laser scanning confocal microscopic observation revealed actin as a predominant brace for enterococci to pass through the epithelial cell layer. As the three enterococci had moderate adhesion ability to actin, actin-binding proteins were isolated and characterized by LC-MS/MS. The isolated proteins were identified as pyruvate formate lyase, enolase, glyceraldehyde-3-phosphate dehydrogenase, and GroEL. All these proteins belong to two major groups of moonlighting proteins, i.e., proteins, which display additional functions other than their described major biochemical catalysis. Both groups of moonlight proteins were determined to be associated with epithelial cell binding.
Zhen Peng; Viktoria Krey; Hua Wei; Qianglai Tan; Roger Vogelmann; Matthias A Ehrmann; Rudi F Vogel
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2013-12-21
Journal Detail:
Title:  Archives of microbiology     Volume:  -     ISSN:  1432-072X     ISO Abbreviation:  Arch. Microbiol.     Publication Date:  2013 Dec 
Date Detail:
Created Date:  2013-12-23     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0410427     Medline TA:  Arch Microbiol     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
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