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A monoclonal antibody which recognized the functional site of snake neurotoxins and which neutralizes all short‐chain variants
Author(s) -
Trémeau Odile,
Boulain Jean-Claude,
Couderc Jacques,
Fromageot Pierre,
Ménez André
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)81024-9
Subject(s) - monoclonal antibody , monoclonal , antibody , chemistry , virology , computational biology , biology , immunology
We isolated a neurotoxin‐specific monoclonal antibody (Mab) which is capable of recognizing and neutralizing all short‐chain toxin variants that have been tested including those with widely divergent sequences. The epitope incorporates the three invariant residues Lys‐27 Trp‐29 and Lys‐47 which form part of the site by which the toxins bind to the nicotinic acetylcholine receptor. To our knowledge this is the first Mab which possesses the universal capacity of neutralizing all natural variants of a toxic protein.