Immunological properties of notexin, a potent presynaptic and myotoxic component from venom of the Australian tiger snake Notechis scutatus scutatus

• Published in: FEBS letters Vol. 250; no. 2; pp. 479 - 482
• Main Authors: Mollier, Pascale, Chwetzoff, Serge, Frachon, Paule, Ménez, André
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 03-07-1989; Elsevier; Wiley
• Subjects: Analytical, structural and metabolic biochemistry; Animals; Antibodies - immunology; Antibody; Biological and medical sciences; Chemical Sciences; Elapid Venoms - immunology; Enzymes and enzyme inhibitors; Fundamental and applied biological sciences. Psychology; Hydrolases; LD50, median lethal dose; Mice; Mice, Inbred BALB C; Neurotoxins - immunology; Notexin; O2NPhSCl, 2-nitrophenylsulfenyl chloride; Organic chemistry; PEG, poly(ethylene) glycol; Phospholipase A 2; Phospholipase A2; Phospholipases A - metabolism; Phospholipases A2; PLA2, phospholipase A2; Radioimmunoassay; RIA; RP-HPLC, reverse-phase high-performance liquid chromatography; Snake venom; PLA 2, phospholipase A 2; Snake venom; Phospholipase A 2; Antibody; LD 50, median lethal dose; O 2NPhSCl, 2-nitrophenylsulfenyl chloride; Notexin; RP-HPLC, reverse-phase high-performance liquid chromatography; RIA; PEG, poly(ethylene) glycol; Toxin; Vertebrata; Enzymatic activity; Radiolabelling; Radioimmunoassay; Venom; Reptilia; Phospholipase A; Ophidia
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(89)80780-X

Neutralizing antibodies were raised in mice against notexin, the most toxic phospholipase A
2 (PLA
2) from
Notechis scutatus scutatus venom, without the necessity of detoxifying the toxin prior to immunization. Using a sensitive radioimmunoassay we demonstrated that anti-notexin antibodies recognized (i) the parent antigen, (ii) closely related isoforms of notexin and (iii) venoms from
Notechis genus snakes. In contrast, they failed to recognize other purified PLA
2 or PLA
2-containing venoms from other origins. Substitutions or chemical modifications occurring in the C-terminal part of the polypeptide chain of notexin altered the binding affinity for antibodies, implying that this region constitutes an antigenic domain of notexin.