Linear B-cell epitopes in BthTX-I, BthTX-II and BthA-I, phospholipase A2's from Bothrops jararacussu snake venom, recognized by therapeutically neutralizing commercial horse antivenom
نویسندگان
چکیده
Background The benefits from treatment with antivenom sera are indubitable. However, the mechanism for toxin neutralization has not been completely elucidated. A mixture of anti-bothropic and anti-crotalic horse antivenom has been reported to be more effective in neutralizing the effects of B. jararacussu snake venom than anti-bothropic antivenom alone. This study determined which regions in the three PLA2s from B.jararacussu snake venom are bound by antibodies in tetravalent anti-bothropic and monovalent anti-crotalic commercial horse antivenom.
منابع مشابه
Linear B-cell epitopes in BthTX-1, BthTX-II and BthA-1, phospholipase A₂'s from Bothrops jararacussu snake venom, recognized by therapeutically neutralizing commercial horse antivenom.
The benefits from treatment with antivenom sera are indubitable. However, the mechanism for toxin neutralization has not been completely elucidated. A mixture of anti-bothropic and anti-crotalic horse antivenom has been reported to be more effective in neutralizing the effects of Bothrops jararacussu snake venom than anti-bothropic antivenom alone. This study determined which regions in the thr...
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Bothropstoxin I (BthTX-I), a non-catalytic and myotoxic Lys49-PLA2 from Bothrops jararacussu venom, has been crystallized alone and complexed with -tocopherol inhibitor. These crystals have been shown to diffract X-rays between 2.17 and 1.83 Å resolution. The BthTX-I/ -tocopherol complex crystals are not isomorphous with those of the native protein. This suggests the inhibitor binding has lead ...
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