Identification of a precursor processing protease from the spider Cupiennius salei essential for venom neurotoxin maturation.

ABSTRACT: Spider venom neurotoxins and cytolytic peptides are expressed as elongated precursor peptides, which are post-translationally processed by proteases to yield the active mature peptides. The recognition motifs for these processing proteases, first published more than 10 years ago, include the processing quadruplet motif (PQM) and the inverted processing quadruplet motif (iPQM). However, the identification of the relevant proteases was still pending. Here we describe the purification of a neurotoxin precursor processing protease from the venom of the spider Cupiennius salei The chymotrypsin-like serine protease is a 28-kDa heterodimer with optimum activity at venom's pH of 6.0. We designed multiple synthetic peptides mimicking the predicted cleavage sites of neurotoxin precursors. Usi

SUBMITTER: Langenegger N 

PROVIDER: S-EPMC5808768 | biostudies-literature | 2018 Feb

REPOSITORIES: biostudies-literature