Document Detail


Snake venomics of the Armenian mountain vipers Macrovipera lebetina obtusa and Vipera raddei.
MedLine Citation:
PMID:  18590992     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Venoms from the Armenian mountain vipers Macrovipera lebetina obtusa and Vipera raddei were analyzed by RP-HPLC, N-terminal sequencing, MALDI-TOF mass fingerprinting and CID-MS/MS. The venom proteins of M.l. obtusa and V. raddei belong to 9 and 11 families, respectively. The two mountain viper venoms share bradykinin-potentiating/C-natriuretic peptides, and proteins from the dimeric distegrin, DC-fragment, CRISP, PLA(2), serine proteinase, C-type lectin-like, L-amino acid oxidase, and Zn(2+)-dependent metalloproteinase families, albeit each species exhibits distinct relative abundances. M.l. obtusa and V. raddei venoms contain unique components, e.g. the short disintegrin obtustatin in M.l. obtusa, and Kunitz-type serine proteinase inhibitor and VEGF-like molecules in V. raddei. The toxin formulation of M.l. obtusa and V. raddei venoms may be related to their adaptation to rocky mountain ecosystems. On the other hand, the possibility that the VEGF-like proteins from V. raddei underlie the reported potential therapeutic value of V. raddei venom for regenerating damaged peripheral nerves deserves further investigations. Using a similarity coefficient, we estimate that the similarity of venom proteins between M. l. obtusa and M. l. transmediterranea is less than 4%. Although this result would support the classification of M.l. obtusa and M.l. transmediterranea as different species, additional detailed genomic analyses are also required.
Authors:
Libia Sanz; Naira Ayvazyan; Juan J Calvete
Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't     Date:  2008-06-03
Journal Detail:
Title:  Journal of proteomics     Volume:  71     ISSN:  1874-3919     ISO Abbreviation:  -     Publication Date:  2008 Jul 
Date Detail:
Created Date:  2008-07-11     Completed Date:  2008-11-18     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101475056     Medline TA:  J Proteomics     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  198-209     Citation Subset:  IM    
Affiliation:
Instituto de Biomedicina de Valencia, C.S.I.C., Valencia, Spain.
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MeSH Terms
Descriptor/Qualifier:
Animals
Chromatography, High Pressure Liquid
Proteome*
Proteomics
Sequence Analysis, Protein
Sequence Homology, Amino Acid
Species Specificity
Viper Venoms / chemistry*,  metabolism
Viperidae / classification,  metabolism*
Chemical
Reg. No./Substance:
0/Proteome; 0/Viper Venoms

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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