Document Detail

Differential interaction of Aggregatibacter (Actinobacillus) actinomycetemcomitans LsrB and RbsB proteins with autoinducer 2.
MedLine Citation:
PMID:  17526716     Owner:  NLM     Status:  MEDLINE    
Our previous studies showed that the Aggregatibacter actinomycetemcomitans RbsB protein interacts with cognate and heterologous autoinducer 2 (AI-2) signals and suggested that the rbsDABCK operon encodes a transporter that may internalize AI-2 (D. James et al., Infect. Immun. 74:4021-4029, 2006.). However, A. actinomycetemcomitans also possesses genes related to the lsr operon of Salmonella enterica serovar Typhimurium which function to import AI-2. Here, we show that A. actinomycetemcomitans LsrB protein competitively inhibits the interaction of the Vibrio harveyi AI-2 receptor (LuxP) with AI-2 from either A. actinomycetemcomitans or V. harveyi. Interestingly, LsrB was a more potent inhibitor of LuxP interaction with AI-2 from V. harveyi whereas RbsB competed more effectively with LuxP for A. actinomycetemcomitans AI-2. Inactivation of lsrB in wild-type A. actinomycetemcomitans or in an isogenic RbsB-deficient strain reduced the rate by which intact bacteria depleted A. actinomycetemcomitans AI-2 from solution. Consistent with the results from the LuxP competition experiments, the LsrB-deficient strain depleted AI-2 to a lesser extent than the RbsB-deficient organism. Inactivation of both lsrB and rbsB virtually eliminated the ability of the organism to remove AI-2 from the extracellular environment. These results suggest that A. actinomycetemcomitans possesses two proteins that differentially interact with AI-2 and may function to inactivate or facilitate internalization of AI-2.
Hanjuan Shao; Deanna James; Richard J Lamont; Donald R Demuth
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural     Date:  2007-05-25
Journal Detail:
Title:  Journal of bacteriology     Volume:  189     ISSN:  0021-9193     ISO Abbreviation:  J. Bacteriol.     Publication Date:  2007 Aug 
Date Detail:
Created Date:  2007-07-19     Completed Date:  2007-09-10     Revised Date:  2013-06-06    
Medline Journal Info:
Nlm Unique ID:  2985120R     Medline TA:  J Bacteriol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  5559-65     Citation Subset:  IM    
Department of Periodontics, Endodontics and Dental Hygiene, University of Louisville School of Dentistry, 501 South Preston Street, Room 209, Louisville, KY 40292, USA.
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MeSH Terms
Actinobacillus actinomycetemcomitans / metabolism*
Bacterial Proteins / antagonists & inhibitors,  metabolism*
Gene Deletion
Homoserine / analogs & derivatives*,  metabolism
Lactones / metabolism*
Periplasmic Binding Proteins / metabolism*
Protein Binding
Receptors, Cell Surface / metabolism*
Grant Support
Reg. No./Substance:
0/Bacterial Proteins; 0/Lactones; 0/LuxP protein, Vibrio; 0/N-octanoylhomoserine lactone; 0/Periplasmic Binding Proteins; 0/Receptors, Cell Surface; 498-19-1/Homoserine

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