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J. Bacteriol. doi:10.1128/JB.01709-07
Copyright (c) 2008, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

Functional mapping of an oligomeric autotransporter adhesin of Aggregatibacter actinomycetemcomitans

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

^* To whom correspondence should be addressed. Email: Keith.Mintz{at}uvm.edu.

	Abstract

EmaA (extracellular matrix protein adhesin A) is a 202 kDa non-fimbrial adhesin, which mediates the adhesion of the oral pathogen Aggregatibacter actinomycetemcomitans to collagen. EmaA oligomers form surface antennae-like protrusions consisting of a long helical rod with an ellipsoidal ending. The functional analysis of in-frame deletion mutants of emaA has located the collagen binding activity to the amino-terminus of the protein corresponding to amino acids 70-386. The level of collagen binding of this deletion mutant was comparable to the emaA^- strain. Transmission electron microscopy studies indicate that the first 330 amino acids of the mature protein form the ellipsoidal ending of the EmaA protrusions, where the activity resides. Amino acid substitution analysis within this sequence has identified a critical amino acid, which is essential for the formation of the ellipsoidal ending and for collagen binding activity.

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