Linked Life Data

18541473

Source:http://linkedlifedata.com/resource/pubmed/id/18541473

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2008-6-10
pubmed:abstractText
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 reported 11 partial or full-length venom gland transcripts, and venom proteome and transcriptome depart in their relative abundances of different toxin families. As expected from their close phylogenetic relationship, the venoms of L. muta and L. stenophrys share (or contain highly similar) proteins, in particular BPPs, serine proteinases, a galactose-specific C-type lectin, and LAO. However, they dramatically depart in their respective PLA(2) complement. Intraspecific quantitative and qualitative differences in the expression of PLA(2) molecules were found when the venoms of five L. muta specimens (3 from Bolivia and 2 from Peru) and the venom of the same species purchased from Sigma were compared. These observations indicate that these class of toxins represents a rapidly-evolving gene family, and suggests that functional differences due to structural changes in PLA(2)s molecules among these snakes may have been a hallmark during speciation and adaptation of diverging snake populations to new ecological niches, or competition for resources in existing ones. Our data may contribute to a deeper understanding of the biology and ecology of these snakes, and may also serve as a starting point for studying structure-function correlations of individual toxins.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1874-3919
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
71
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
46-60
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Snake venomics of the South and Central American Bushmasters. Comparison of the toxin composition of Lachesis muta gathered from proteomic versus transcriptomic analysis.
pubmed:affiliation
Instituto de Biomedicina de Valencia, C.S.I.C., Valencia, Spain.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't