Jun 11, 2008

Snake venomics of the South and Central American Bushmasters. Comparison of the toxin composition of Lachesis muta gathered from proteomic versus transcriptomic analysis

Journal of Proteomics
Libia SanzJuan J Calvete

Abstract

We report the proteomic characterization of the venoms of two closely related pit vipers of the genus Lachesis, L. muta (South American Bushmaster) and L. stenophrys (Central American Bushmaster), and compare the toxin repertoire of the former revealed through a proteomic versus a transcriptomic approach. The protein composition of the venoms of Lachesis muta and L. stenophrys were analyzed by RP-HPLC, N-terminal sequencing, MALDI-TOF peptide mass fingerprinting and CID-MS/MS. Around 30-40 proteins of molecular masses in the range of 13-110 kDa and belonging, respectively, to only 8 and 7 toxin families were identified in L. muta and L. stenophrys venoms. In addition, both venoms contained a large number of bradykinin-potentiating peptides (BPP) and a C-type natriuretic peptide (C-NP). BPPs and C-NP comprised around 15% of the total venom proteins. In both species, the most abundant proteins were Zn(2+)-metalloproteinases (32-38%) and serine proteinases (25-31%), followed by PLA(2)s (9-12%), galactose-specific C-type lectin (4-8%), l-amino acid oxidase (LAO, 3-5%), CRISP (1.8%; found in L. muta but not in L. stenophrys), and NGF (0.6%). On the other hand, only six L. muta venom-secreted proteins matched any of the previously re...Continue Reading

Mentioned in this Paper

Echis ocellatus
Necrosis
Natriuretic Peptide, C-Type
Snake Venoms
Progest
Lachesis
Complement System Proteins
Galactose Measurement
Protein Family
Genome

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