FEBS Letters | |
Neutralization of lethal potency and inhibition of enzymatic activity of a phospholipase A2 neurotoxin, crotxin, by non‐precipitating antibodies (Fab) | |
Ownby, Charlotte1  Choumet, Valérie1  Jiang, Ming-Shi1  Radvanyi, François1  Bon, Cassian1  | |
[1] Laboratoire des Venins, Unité associée Pasteur/INSERM 285, Institut Pasteur, 25 rue du Dr Roux, 75724 Paris, France | |
关键词: Phospholipase A2; Snake venom neurotoxin; Lethal potency neutralization; Enzymatic inhibition; Neutralizing antibody; Neutralizing Fab; | |
DOI : 10.1016/0014-5793(89)81185-8 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Rabbit antibodies were prepared against both purified catalytic (component-B) and purified non-catalytic (component-A) subunits of crotoxin, the major phospholipase A2 neurotoxin from the South American rattlesnake. They cross-react with crotoxin-like toxins from the venom of several Crotalus species as well as with single-chain phospholipase A2 neurotoxins from Crotalid and Viperid venoms (agkistrodontoxin and ammodytoxin A) but not from Elapid venoms (notexin). Immunological cross-reactions of anti-component-A and anti-component-B sera with crotoxin and with its isolated components A and B showed that component-A exposes determinants of low immunogenicity which are present on component-B, whereas the major antigenic determinants of component-B are not present on component-A. Anti-component-B anti-bodies, but not anti-component-A antibodies, neutralize the lethal potency of crotoxin and inhibit its enzymatic activity. Furthermore, non-precipitating anti-component-B Fab fragments were as potent as antibodies, indicating that crotoxin neutralization results from the binding of the antibodies to the catalytic subunit, rather than the formation of an immuno-precipitate.
【 授权许可】
Unknown
【 预 览 】
Files | Size | Format | View |
---|---|---|---|
RO201912020291636ZK.pdf | 620KB | download |