S. Lizano et al., Cloning and cDNA sequence analysis of Lys(49) and Asp(49) basic phospholipase A(2) myotoxin isoforms from Bothrops asper, INT J BIO C, 33(2), 2001, pp. 127-132
Citations number
29
Categorie Soggetti
Biochemistry & Biophysics
Journal title
INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY
Snake venom myotoxic phospholipases A(2) contribute to much of the tissue d
amage observed during envenomation by Bothrops asper, the major cause of sn
ake bites in Central America. Several myotoxic PLA(2)s have been identified
, but their mechanism of myotoxicity is still unclear. To aid in the molecu
lar characterization of these venom toxins, the complete open reading frame
s encoding two Lys(49) and one Asp(49) basic PLA(2) myotoxins From the Cent
ral American snake B, asper (terciopelo) were obtained by cDNA cloning from
venom gland poly-adenylated RNA. The amino acid sequence deduced from the
myotoxins II and III open reading frames corresponded in each case to one o
f the reported amino acid sequence isoforms. The sequence of a new myotoxin
IV-like sequence (MT-IVa) contains conservative Val --> Leu(18) and Ala --
> Val(23) substitutions when compared with the reported N-terminus of the n
ative myotoxin IV, suggesting minor isoform variations among specimens of a
single species. Sequence alignment studies indicated significant (>75% seq
uence identity) identities with other crotalid venom Lys(49) PLA(2)s, parti
cularly bothropstoxin I/Ia isoforms of B. jararacussu and myotoxin II of B.
asper. (C) 2001 Elsevier Science Ltd. All rights reserved.