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Toxicon. 2005 Jul;46(1):31-8.

Identification of novel bradykinin-potentiating peptides and C-type natriuretic peptide from Lachesis muta venom.

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Rede Proteômica do Rio de Janeiro and Instituto de Bioquímica Médica/CCS, Universidade Federal do Rio de Janeiro, Cidade Universitária, Rio de Janeiro 21941-590, Brazil.


The generation of expressed sequence tags (ESTs) from the pit-viper snake Lachesis muta venom glands allowed us to identify two cDNA isoforms which encode the precursors for bradykinin-potentiating peptides (BPPs) and a C-type natriuretic peptide (CNP). The sequence data derived from these cDNAs combined with the venom peptides identification using MALDI-TOF mass spectrometry analysis predicted that these molecules are the precursor protein isoforms that are further processed to produce five novel BPPs and a CNP. They were identified directly in crude venom using MALDI-TOF. The BPPs sequences were further confirmed by MALDI-TOF/TOF de novo sequencing, and an unusual BPP with a residue of tryptophan at the N-terminus (usually it is pyroglutamate) was identified. The putative processing steps required to form the mature BPPs and CNP seem to be similar to those proposed for the ones found in the venom of Bothrops jararaca and Glodyus blomhoffi.

[Indexed for MEDLINE]

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