Sialic acid-dependent binding and transcytosis of serotype D botulinum neurotoxin and toxin complex in rat intestinal epithelial cells.

A large toxin complex (L-TC) produced by Clostridium botulinum is composed of neurotoxin (BoNT), non-toxic non-hemagglutinin (NTNHA) and hemagglutinin subcomponents (HA-70, -33 and -17). In animal botulism, BoNT or L-TC is internalized by intestinal epithelial cells. Previous studies showed that L-TC binds to intestinal cells via sugar chains on the cell surface, but the role of toxin binding to sugar chains in the toxin absorption from intestine is unclear.

Expression and characterization of a recombinant unique acid phosphatase from kidney bean hypocotyl exhibiting chloroperoxidase activity in the yeast Pichia pastoris.

We previously purified and characterized a novel acid phosphatase (KhACP) from kidney bean hypocotyls that exhibited vanadate-dependent chloroperoxidase (V-CPO) activity. In the present study, a functional recombinant KhACP (rKhACP) was successfully produced at a high expression level by the methylotrophic yeast Pichia pastoris. The KhACP cDNA excising signal peptide sequence was subcloned into the pPICZalphaA vector and then integrated into the genome of P.