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Journal of Bacteriology, August 2007, p. 5559-5565, Vol. 189, No. 15
0021-9193/07/$08.00+0     doi:10.1128/JB.00387-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Differential Interaction of Aggregatibacter (Actinobacillus) actinomycetemcomitans LsrB and RbsB Proteins with Autoinducer 2{triangledown}

Hanjuan Shao,1 Deanna James,1 Richard J. Lamont,2 and Donald R. Demuth1*

Department of Periodontics, Endodontics and Dental Hygiene, University of Louisville School of Dentistry, Louisville, Kentucky,1 Department of Oral Biology, University of Florida School of Dentistry, Gainesville, Florida2

Received 15 March 2007/ Accepted 11 May 2007

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.

* Corresponding author. Mailing address: Department of Periodontics, Endodontics and Dental Hygiene, University of Louisville School of Dentistry, 501 South Preston Street, Room 209, Louisville, KY 40292. Phone: (502) 852-3807. Fax: (502) 852-4052. E-mail: drdemu01{at}louisville.edu

{triangledown} Published ahead of print on 25 May 2007.

Journal of Bacteriology, August 2007, p. 5559-5565, Vol. 189, No. 15
0021-9193/07/$08.00+0     doi:10.1128/JB.00387-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

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