A polysaccharide deacetylase enhances bacterial adhesion in high-ionic-strength environments.

Differences in ionic strength, pH, temperature, shear forces, and other environmental factors impact adhesion, and organisms have evolved various strategies to optimize their adhesins for their specific environmental conditions. Many species of Alphaproteobacteria, including members of the order Caulobacterales, use a polar adhesin, called holdfast, for surface attachment and subsequent biofilm formation in both freshwater and marine environments. Hirschia baltica, a marine member of Caulobacterales, produces a holdfast adhesin that tolerates a drastically higher ionic strength than the holdfast produced by its freshwater relative, Caulobacter crescentus. In this work, we show that the holdfast polysaccharide deacetylase HfsH plays an important role in adherence in high-ionic-strength environments. We show that increasing expression of HfsH improves holdfast binding in high-ionic-strength environments. We conclude that HfsH plays a role in modulating holdfast binding at high ionic strength and hypothesize that this modulation occurs through varied deacetylation of holdfast polysaccharides.