Role of de-n-acetylase pgab from aggregatibacter actinomycetemcomitans in exopolysaccharide export in biofilm mode of growth

Aggregatibacter actinomycetemcomitans, a Gram-negative bacterium, is the causative agent of localized aggressive periodontitis. Attachment to a biotic surface is a critical first step in the A. actinomycetemcomitans infection process for which exopolysaccha-rides have been shown to be essential. In addition, the pga operon, containing genes encoding for biosynthetic proteins for poly-N-acetyl glucosamine (PNAG), plays a key role in A. actinomycetemcomitans virulence, as a mutant strain lacking the pga operon induces significantly less bone resorption. Among the genes in the pga operon, pgaB codes for a de-N-acetylase that is responsible for the deacetylation of the PNAG exopolysaccharide. Here we report the role of PgaB in regulation of virulence genes using a markerless, scarless deletion mutant targeting the coding region of the N-terminal catalytic domain of PgaB. The results demonstrate that the N-terminal, catalytic domain of PgaB is crucial for exopolysaccharide export.