Studies on the specificity of CNF, a phospholipase A(2) inhibitor isolatedfrom the blood plasma of the South American rattlesnake (Crotalus durissusterrificus). I. Interaction with PLA(2) from Lachesis muta muta snake venom
Cl. Fortes-dias et al., Studies on the specificity of CNF, a phospholipase A(2) inhibitor isolatedfrom the blood plasma of the South American rattlesnake (Crotalus durissusterrificus). I. Interaction with PLA(2) from Lachesis muta muta snake venom, TOXICON, 37(12), 1999, pp. 1747-1759
A phospholipase A(2) inhibitor has been previously purified and cloned from
the blood plasma of the South American rattlesnake, Crotalus durissus terr
ificus. This inhibitor, named CNF for Crotahus neutralizing factor, interac
ts with crotoxin, the main neurotoxin from C. d. terrificus venom, abolishi
ng its phospholipase A(2) activity. Crotoxin is a heterodimer of an acidic
subunit (CA) and a basic phospholipase A(2) (CB). CNF acts by forming a sta
ble non-toxic complex with CB, replacing CA in the toxic CA-CB of crotoxin.
In the present investigation, we have shown that CNF has a broader specific
ity. It is able to inhibit the PLA(2) activity of the whole venom from the
bushmaster snake (Lachesis muta muta), a species evolutionary related to Cr
otalus. Inhibition experiments have been carried out with four PLA(2) activ
e components isolated from L. m. muta venom, one basic and three acidic one
s. CNF inhibition is not restricted to the basic PLA(2), but extended to th
e three acidic forms as well. (C) 1999 Elsevier Science Ltd. All rights res
erved.