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Infection and Immunity, September 2007, p. 4440-4448, Vol. 75, No. 9
0019-9567/07/$08.00+0     doi:10.1128/IAI.02020-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

A Second Aggregatibacter actinomycetemcomitans Autotransporter Adhesin Exhibits Specificity for Buccal Epithelial Cells in Humans and Old World Primates{triangledown}

Gang Yue,1 Jeffrey B. Kaplan,1 David Furgang,1 Keith G. Mansfield,2 and Daniel H. Fine1*

Department of Oral Biology, New Jersey Dental School, Newark, New Jersey 07103,1 New England Regional Primate Research Center, Harvard University, Southborough, Massachusetts 017722

Received 24 December 2006/ Returned for modification 4 February 2007/ Accepted 26 June 2007

Previous work showed that the Aggregatibacter actinomycetemcomitans adhesin Aae demonstrated species specificity and tissue tropism to buccal epithelial cells (BECs) derived from humans and Old World primates, but a second, lower-affinity adhesin was noted. This study was designed to determine if Omp100 (also known as ApiA), a surface-expressed A. actinomycetemcomitans adhesin, is that second adhesin and if so to investigate its tissue tropism and species specificity. A targeted mutagenesis protocol was used to construct an isogenic apiA mutant and an aae apiA double mutant with wild-type A. actinomycetemcomitans. In addition, Escherichia coli strain DH5{alpha} was used to express apiA to further assess binding parameters. Results indicated that the apiA mutant strain showed significantly less binding to BECs than its parent strain (P ≤ 0.05). Further, binding mediated by ApiA was specific to BECs from humans and Old World primates, as seen in both wild-type A. actinomycetemcomitans and E. coli expressing ApiA (P ≤ 0.05). Pretreatment of wild-type A. actinomycetemcomitans cells with anti-ApiA antiserum reduced binding in a dose-dependent manner. The aae apiA double mutant completely abrogated A. actinomycetemcomitans binding to both human and Old World primate BECs. Taken together, these studies indicate that ApiA and Aae, in concert, modulate binding of A. actinomycetemcomitans to human BECs. Since the BEC is a prominent reservoir for A. actinomycetemcomitans, identification of this second adhesin could lead to important therapeutic strategies.

* Corresponding author. Mailing address: Dept. of Oral Biology, Room C-636, Medical Science Building, New Jersey Dental School, 185 S. Orange Ave., Newark, NJ 07103. Phone: (973) 972-3728. Fax: (973) 972-0045. E-mail: finedh{at}umdnj.edu

{triangledown} Published ahead of print on 9 July 2007.

Editor: J. B. Bliska

Infection and Immunity, September 2007, p. 4440-4448, Vol. 75, No. 9
0019-9567/07/$08.00+0     doi:10.1128/IAI.02020-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



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