Functional Mapping of an Oligomeric Autotransporter Adhesin of Aggregatibacter actinomycetemcomitans

• DOI: 10.1128/jb.01709-07
• Publication Date: 2008-03-01T02:36:47Z
• Authors: Chunxiao Yu; Teresa Ruiz; Christopher Lenox; Keith P. Mintz
• Keywords: 0301 basic medicine; Binding Sites; DNA Mutational Analysis; Molecular Sequence Data; Bacterial Adhesion; Protein Structure, Tertiary; 03 medical and health sciences; Amino Acid Substitution; Microscopy, Electron, Transmission; Consensus Sequence; Amino Acid Sequence; Pasteurellaceae; Adhesins, Bacterial; Collagen Type V; Sequence Deletion

ABSTRACT

Extracellular matrix protein adhesin A (EmaA) is a 202-kDa nonfimbrial adhesin, which mediates the adhesion of the oral pathogen Aggregatibacter actinomycetemcomitans to collagen. EmaA oligomers form surface antenna-like protrusions consisting of a long helical rod with an ellipsoidal ending. The functional analysis of in-frame emaA deletion mutants has located the collagen binding activity to the amino terminus of the protein corresponding to amino acids 70 to 386. The level of collagen binding of this deletion mutant was comparable to the emaA mutant 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.