Toxicity evolution of Vipera aspis aspis venom: identification and molecular modeling of a novel phospholipase A(2) heterodimer neurotoxin.
We report the simultaneous presence of two phospholipase A(2) (PLA(2)) neurotoxins in the venom of Vipera aspis aspis, the first such observation. One is monomeric and identical to ammodytoxin B of Vipera ammodytes ammodytes. Its presence may result from gene flux after interbreeding between V. aspis aspis and V. ammodytes ammodytes. The second, a novel heterodimer named vaspin, is very similar to vipoxin of Vipera ammodytes meridionalis and to PLA(2)-I of Vipera aspis zinnikeri. It may result from expression of preexisting genes, the acidic subunit evolving from an ancestor common to ammodytin I2 from V. ammodytes ammodytes, which we also found in V. aspis aspis.
Jan
Virginie
V
Unité des Venins, Institut Pasteur, 25 rue du Dr Roux, 75724 Cedex 15, Paris, France. vjan@pasteur.fr
Maroun
R C
RC
Robbe-Vincent
Annie
A
De Haro
Luc
L
Choumet
Valérie
V
D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D000818:Animals; D001483:Base Sequence; D005075:Biological Evolution; D019281:Dimerization; D054501:Group II Phospholipases A2; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009498:Neurotoxins / Q000737:chemistry* / Q000235:genetics; D010741:Phospholipases A / Q000737:chemistry* / Q000235:genetics; D054467:Phospholipases A2; D011487:Protein Conformation; D030162:Reptilian Proteins; D017386:Sequence Homology, Amino Acid; D012689:Sequence Homology, Nucleic Acid; D014757:Viper Venoms / Q000737:chemistry* / Q000235:genetics; D017819:Viperidae / Q000502:physiology*
D009498:Neurotoxins; D030162:Reptilian Proteins; D014757:Viper Venoms; C033134:vipoxin; D010741:Phospholipases A; D054501:Group II Phospholipases A2; D054467:Phospholipases A2; C051125:ammodytoxin B; C467057:vaspin protein, Vipera aspis aspis