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Infection and Immunity, November 2006, p. 6163-6170, Vol. 74, No. 11
0019-9567/06/$08.00+0     doi:10.1128/IAI.00857-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Novel Surface Structures Are Associated with the Adhesion of Actinobacillus actinomycetemcomitans to Collagen

Teresa Ruiz,1 Christopher Lenox,2 Michael Radermacher,1 and Keith P. Mintz1*

Department of Molecular Physiology and Biophysics,1 Department of Microbiology and Molecular Genetics, University of Vermont, Burlington, Vermont2

Received 30 May 2006/ Returned for modification 23 July 2006/ Accepted 3 August 2006

Actinobacillus actinomycetemcomitans is a gram-negative, facultative, anaerobic bacterium that colonizes the human oral cavity and the upper respiratory tract. This bacterium is strongly associated with localized aggressive periodontitis and adult periodontitis and is the causative agent for other serious systemic infections. Recently, we have identified a protein, EmaA (extracellular matrix protein adhesin A), that mediates the adhesion of A. actinomycetemcomitans to collagen. The conserved sequence and predicted secondary structure suggest that EmaA is an orthologue of the Yersinia enterocolitica adhesin YadA. Electron microscopy examinations of A. actinomycetemcomitans have identified antenna-like protrusions associated with the surface of the bacterium. These structures are absent on emaA mutant strains and can be restored by transformation of the mutant strain with emaA in trans. The loss of these structures is associated with a decrease in the binding of this bacterium to collagen. The antenna-like structures are composed of a long rod that terminates in an ellipsoidal head region. The analysis of these structures using image processing techniques has provided an initial estimate of the overall dimensions, which suggests that the appendages are oligomeric structures formed by either three or four subunits. Together, the data suggest that emaA is required for the expression of novel appendages on the surface of A. actinomycetemcomitans that mediate the adhesion of the bacterium to collagen.


* Corresponding author. Mailing address: Department of Microbiology and Molecular Genetics, Room 118, Stafford Hall, University of Vermont, Burlington, VT 05405. Phone: (802) 656-0712. Fax: (802) 656-8749. E-mail: Keith.Mintz{at}uvm.edu.

Editor: J. B. Bliska


Infection and Immunity, November 2006, p. 6163-6170, Vol. 74, No. 11
0019-9567/06/$08.00+0     doi:10.1128/IAI.00857-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:

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