Expression pattern of three-finger toxin and phospholipase A2 genes in the venom glands of two sea snakes, Lapemis curtus and Acalyptophis peronii: comparison of evolution of these toxins in land snakes, sea kraits and sea snakes.
BACKGROUND
Snake venom composition varies widely both among closely related species and within the same species, based on ecological variables. In terrestrial snakes, such variation has been proposed to be due to snakes' diet. Land snakes target various prey species including insects (arthropods), lizards (reptiles), frogs and toads (amphibians), birds (aves), and rodents (mammals), whereas sea snakes target a single vertebrate class (fishes) and often specialize on specific types of fish. It is therefore interesting to examine the evolution of toxins in sea snake venoms compared to that of land snakes.


RESULTS
Here we describe the expression of toxin genes in the venom glands of two sea snakes, Lapemis curtus (Spine-bellied Sea Snake) and Acalyptophis peronii (Horned Sea Snake), two members of a large adaptive radiation which occupy very different ecological niches. We constructed cDNA libraries from their venom glands and sequenced 214 and 192 clones, respectively. Our data show that despite their explosive evolutionary radiation, there is very little variability in the three-finger toxin (3FTx) as well as the phospholipase A2 (PLA2) enzymes, the two main constituents of Lapemis curtus and Acalyptophis peronii venom. To understand the evolutionary trends among land snakes, sea snakes and sea kraits, pairwise genetic distances (intraspecific and interspecific) of 3FTx and PLA2 sequences were calculated. Results show that these proteins appear to be highly conserved in sea snakes in contrast to land snakes or sea kraits, despite their extremely divergent and adaptive ecological radiation.


CONCLUSIONS
Based on these results, we suggest that streamlining in habitat and diet in sea snakes has possibly kept their toxin genes conserved, suggesting the idea that prey composition and diet breadth may contribute to the diversity and evolution of venom components.
Pahari
Susanta
S
Protein Science and Conservation Ecology Laboratories, Department of Biological Sciences, National University of Singapore, 117543, Singapore. susanta2001@yahoo.com
Bickford
David
D
Fry
Bryan G
BG
Kini
R Manjunatha
RM
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D017838:Bungarus / Q000235:genetics*; D018076:DNA, Complementary; D004546:Elapid Venoms / Q000201:enzymology / Q000235:genetics*; D017815:Elapidae / Q000235:genetics*; D019143:Evolution, Molecular; D015870:Gene Expression; D015723:Gene Library; D008969:Molecular Sequence Data; D054467:Phospholipases A2 / Q000235:genetics*; D020033:Protein Isoforms / Q000235:genetics; D030162:Reptilian Proteins / Q000235:genetics*; D013045:Species Specificity
C054654:Acalyptophis neurotoxin; D018076:DNA, Complementary; D004546:Elapid Venoms; D020033:Protein Isoforms; D030162:Reptilian Proteins; D054467:Phospholipases A2