Transport of the botulinum neurotoxin-associating protein, nontoxic nonhemagglutinin, across the rat small intestinal epithelial cell monolayer.

Botulinum neurotoxin (BoNT) associates with nontoxic nonhemagglutinin (NTNHA) yielding a complex in culture. BoNT and NTNHA have similar domain organizations, implying that they share common functions, although this remains unclear. Here, we examined cell monolayer transport of serotype D NTNHA in the rat intestinal epithelial cell line IEC-6. NTNHA and BoNT both bound to the cell and were transported across the cell layer. NTNHA contains a QXW motif and a β-trefoil fold, both common in sugar chain-recognizing proteins, whereas the QXW motif is absent in all BoNT serotypes. This could explain the distinct sugar chain-recognizing properties of NTNHA and BoNT.