文摘
The protein composition of the venoms of the West African Gaboon viper (Bitis gabonica rhinoceros),the rhinoceros viper (Bitis nasicornis), and the horned puff adder (Bitis caudalis) were analyzed byRP-HPLC, N-terminal sequencing, SDS-PAGE, MALDI-TOF peptide mass fingerprinting, and CID-MS/MS. In line with previous proteomic and transcriptomic analyses showing that snake venom proteinsbelong to only a few major protein families, the venom proteomes of Bitis gabonica rhinoceros, Bitisnasicornis, and Bitis caudalis comprise, respectively, toxins from 11, 9, and 8 toxin families. Dimericdisintegrins, PLA2 molecules, serine proteinases, a CRISP, C-type lectin-like proteins, L-amino acidoxidases, and snake venom metalloproteases are present in the three Bitis snake venoms, though theydepart from each other in the composition and the relative abundance of their toxins. The venomcomposition appears to keep information on the evolutionary history of congeneric taxa. Proteinsimilarity coefficients used to estimate the similarity of venom proteins of the Bitis taxa sampled hereand in previous studies (eg. Bitis arietans and Bitis gabonica gabonica) support the monophyly of thethree West African taxa (B.g. gabonica, B.g. rhinoceros, and B. nasicornis) based on genetic distancereconstructions, the lack of alliances between B. arietans and any other Bitis species, and are consistentwith the taxonomic association of Bitis caudalis within the differentiated group of small Bitis species.The low level of venom toxin composition similarity between the two conventionally recognizedsubspecies of Bitis gabonica, B. g. gabonica and B. g. rhinoceros, supports the consideration by someauthors of B. g. rhinoceros as a separate species, Bitis rhinoceros. Moreover, our proteomic data fitbetter to a weighted phylogram based on overall genetic distances than to an unweighted maximum-parsimony tree.