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“Background Porphyromonas gingivalis has been Interleukin-3 receptor shown to be a major etiologic agent of destructive adult periodontitis, with a significant lifestyle component

harbored within the complex multi-species biofilm (dental plaque) that develops along the gingival margins [1]. The bacterium expresses a number of potential virulence factors, such as long (major) and short (minor) fimbriae, lipopolysaccharides (LPS), and proteases [2]. Among these factors, a unique class of cysteine proteinases, termed gingipains, composed of arginine-specific [Arg-gingipain A and B, (RgpA and RgpB, respectively)] and lysine-specific (Kgp) proteases, are implicated in a wide range of both pathological and physiological processes [3]. Proteases can be post-translationally processed for retention on the cell surface or secretion into the extracellular milieu. Rgp enzymes are glycosylated, with their carbohydrate domain containing phosphorylated branched mannans that can contribute to the anchoring of Rgp on bacterial outer membrane [4]. In addition, this phosphorylated branched mannan constitutes an exopolysaccharide that is distinguishable from both LPS and the serotypeable capsule polysaccharides of P. gingivalis [4].