Figure 5From: Quantitative high-throughput profiling of snake venom gland transcriptomes and proteomes (Ovophis okinavensis and Protobothrops flavoviridis)Alignment of VEGF sequences. Owing to the diversification of this toxin family, classification of venom VEGFs is difficult. Ovophis VEGF 1 [AB852007] possesses a 24-residue insert seen in no other sequence. Ovophis VEGF 5 [AB848274] and Protobothrops VEGF 1 [AB848141] are homologous to vammin, from the venom of Vipera ammodytes. All three of these display short C-terminal extensions of 16-17 residues that bind heparin [102]. Both vammin and VR-1, a VEGF from Daboia russellii venom, enhance vascular permeability with great potency. Another subclass of VEGF including Ovophis VEGF 3-4 [AB852009, AB852010] and Protobothrops VEGF 3 [AB851941] comprise a subclass with no C-terminal extension, or an extremely short extension corresponding to the C-terminus of Ovophis VEGF 1-2 [AB852007, AB852008] and Protobothrops VEGF 2 [AB851940]. These are significantly shorter than barietin, from the venom of Bitis arietans[98], and they do not align well with it or with vammin.Back to article page