Molecular cloning of disintegrins from Cerastes vipera and Macrovipera lebetina transmediterranea venom gland cDNA libraries: insight into the evolution of the snake venom integrin-inhibition system

We report the cloning and sequence analysis of Cerastes vipera and Macrovipera lebetina transmediterranea cDNAs coding for short non-RGD (Arg-Gly-Asp) disintegrins and for dimeric disintegrin subunits. The mRNAs belong to the short-coding class, suggesting that these disintegrin mRNAs may be more wi...

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Bibliographic Details
Published in:Biochemical journal 2006-04, Vol.395 (2), p.385-392
Main Authors: Sanz, Libia, Bazaa, Amine, Marrakchi, Naziha, Pérez, Alicia, Chenik, Mehdi, Bel Lasfer, Zakaria, El Ayeb, Mohamed, Calvete, Juan J
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Base Sequence
Cerastes vipera
Cloning, Molecular
Dimerization
Disintegrins - chemistry
Disintegrins - genetics
DNA, Complementary - genetics
Evolution, Molecular
Gene Library
Integrins - antagonists & inhibitors
Life Sciences
Molecular Sequence Data
Oligopeptides - analysis
Oligopeptides - chemistry
Sequence Alignment
Spectrum Analysis
Viper Venoms - genetics
Viperidae - genetics
Viperidae - metabolism
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Summary:We report the cloning and sequence analysis of Cerastes vipera and Macrovipera lebetina transmediterranea cDNAs coding for short non-RGD (Arg-Gly-Asp) disintegrins and for dimeric disintegrin subunits. The mRNAs belong to the short-coding class, suggesting that these disintegrin mRNAs may be more widely distributed than previously thought. Our data also argue for a common ancestry of the mRNAs of short disintegrins and those coding for precursors of dimeric disintegrin chains. The Macrovipera lebetina transmediterranea dimeric disintegrin reported to inhibit the laminin-binding integrins alpha3beta1, alpha6beta1 and alpha7beta1 was analysed using a proteomic approach and was shown to bear MLD (Met-Leu-Asp) and VGD (Val-Gly-Asp) motifs. The results highlight the fact that disintegrins have evolved a restricted panel of integrin-blocking sequences that segregate with defined branches of the phylogenetic tree of the integrin alpha-chains, providing novel insights into the evolutionary adaptation of the snake venom antagonists to the ligand-binding sites of their target integrin receptors.
ISSN:0264-6021
1470-8728
DOI:10.1042/BJ20051678