ApuA, a multifunctional [alpha]-glucan-degrading enzyme of Streptococcus suis, mediates adhesion to porcine epithelium and mucus

We have identified apuA in Streptococcus suis, which encodes a bifunctional amylopullulanase with conserved [alpha]-amylase and pullulanase substrate-binding domains and catalytic motifs. ApuA exhibited properties typical of a Gram-positive surface protein, with a putative signal sequence and LPKTGE cell-wall-anchoring motif. A recombinant protein containing the predicted N-terminal [alpha]-amylase domain of ApuA was shown to have [alpha]-(1,4) glycosidic activity. Additionally, an apuA mutant of S. suis lacked the pullulanase [alpha]-(1,6) glycosidic activity detected in a cell-surface protein extract of wild-type S. suis. ApuA was required for normal growth in complex medium containing pullulan as the major carbon source, suggesting that this enzyme plays a role in nutrient acquisition in vivo via the degradation of glycogen and food-derived starch in the nasopharyngeal and oral cavities. ApuA was shown to promote adhesion to porcine epithelium and mucus in vitro, highlighting a link between carbohydrate utilization and the ability of S. suis to colonize and infect the host. DOI 10.1099/mic.0.037960-0