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The binding of bacteria to collagen is an established virulence determinant. Recently, emaA (extracellular matrix protein adhesin A) was identified as a collagen binding protein of Actinobacillus actinomycetemcomitans, a bacterium associated with localized aggressive periodontitis and other systemic human infections [1, 2, 3]. emaA encodes a 201 kDa outer membrane protein and, based on primary and secondary protein predictions, belongs to a family of oligomeric coiled-coil adhesins (Oca)[4]. EmaA contains all of the conserved structural elements of the members of this adhesin family: a) an N-terminal secretion signal, b) a head domain containing the interactive site, c) a highly conserved neck region, d) a stalk domain with high coiled-coil formation probability, and e) a conserved membrane anchor domain. The N-terminal head domain of EmaA contains twelve putative collagen binding motifs, which are …