Ar. Deroodt et al., CROSS-REACTIVITY AND HETEROLOGOUS NEUTRALIZATION OF CROTALINE ANTIVENOMS USED IN ARGENTINA, Toxicon (Oxford), 36(7), 1998, pp. 1025-1038
The immunochemical cross-reactivity and neutralizing capacity of four
crotalinae antivenoms consisting in equine F(ab')(2) fragments and ava
ilable in Argentina (bothropic Bivalent, against Bothrops alternatus a
nd B. neuwiedii venoms; bothropic Tetravalent against B. alternatus, B
. neuwiedii, B. jararaca and B. jararacussu venoms; bothropic-crotalic
Trivalent, against B. alternatus, B, neuwiedii and Crotalus (C.) duri
ssus terrificus venoms and anticrotalic against C. d. terrificus venom
) were studied against B. alternatus, B, ammodytoides; B. jararaca, B,
jararacussu; B. moojeni; B, neuwiedii and C, d. terrificus venoms. SD
S-PAGE analysis of the Bothrops venoms showed protein bands of high (>
40 kDa) medium (20-40 kDa) and low (< 15 kDa) molecular weights, while
that of C. d. terrificus exhibited a large amount of material with mo
lecular weight of 15.0 kDa or lower. Immunoblotting showed a high cros
sreactivity of all the major protein bands with all the antivenoms (ev
en heterologous) tested. All the antivenoms were effective in neutrali
zing the lethal activity of the venoms tested, and in some cases (B, j
araraca and B. jararacussu) heterologous antivenoms exhibited similar
neutralizing capacity than the homologous ones. In spite of the differ
ences in biochemical composition and pharmacology, Bothropic antivenom
s displayed a significant neutralizing capacity on lethal activity of
C, d. terrificus venom. In addition, all the antivenoms (including the
anticrotalic) were highly effective in neutralizing the hemorragic, n
ecrotizing, procoagulant, and proteolytic activities. The antivenoms t
ested produced different degrees of inhibition of phospholipase A2 act
ivity, which exhibited a certain specificity but was also related to t
he enzyme content in the venom. (C) 1998 Elsevier Science Ltd. All rig
hts reserved.