Cloning and cDNA sequence analysis of Lys(49) and Asp(49) basic phospholipase A(2) myotoxin isoforms from Bothrops asper

Citation
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
ISSN journal
13572725 → ACNP
Volume
33
Issue
2
Year of publication
2001
Pages
127 - 132
Database
ISI
SICI code
1357-2725(200102)33:2<127:CACSAO>2.0.ZU;2-5
Abstract
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.