Proposed cleavage mechanism of partially deacetylated PNAG by the glycoside hydrolase domain of Bordetella bronchiseptica PgaB.

Microbial biofilms grow on biotic and abiotic surfaces. The matrix of the biofilm that the pathogen produces protects them from the host immune response and antibiotics.  This proposes a major challenge for the treatment of chronic infections. In an article published in Plos Pathogens, Dustin J. Little and Roland Pfoh (Howell lab) and co-authors demonstrate that the C-terminal domain of PgaB is a glycoside hydrolase that can hydrolyze poly-β(1,6)-N-acetyl-D-glucosamine (PNAG) dependent biofilms. PgaB potentiates antibiotic killing when applied to biofilm-embedded bacteria, highlighting its potential therapeutic application. Little and Pfoh’s analysis of the chemical structure of the cleavage products suggests that partially deacetylation of the PNAG polymer is required for catalysis.