Studies of the mechanistic details of the pH-dependent association of botulinum neurotoxin with membranes.

ABSTRACT: Botulinum neurotoxin (BoNT) belongs to a large class of toxic proteins that act by enzymatically modifying cytosolic substrates within eukaryotic cells. The process by which a catalytic moiety is transferred across a membrane to enter the cytosol is not understood for any such toxin. BoNT is known to form pH-dependent pores important for the translocation of the catalytic domain into the cytosol. As a first step toward understanding this process, we investigated the mechanism by which the translocation domain of BoNT associates with a model liposome membrane. We report conditions that allow pH-dependent proteoliposome formation and identify a sequence at the translocation domain C terminus that is protected from proteolytic degradation in the context of the proteoliposome. Fluorescence que

SUBMITTER: Mushrush DJ 

PROVIDER: S-EPMC3143659 | biostudies-literature | 2011 Jul

REPOSITORIES: biostudies-literature