Mimicry between receptors and antibodies. Identification of snake toxin determinants recognized by the acetylcholine receptor and an acetylcholine receptor-mimicking monoclonal antibody. 1996

F Ducancel, and K Mérienne, and C Fromen-Romano, and O Trémeau, and L Pillet, and P Drevet, and S Zinn-Justin, and J C Boulain, and A Ménez
Département d'Ingénierie et d'Etudes des Protéines, DSV, CEA, Saclay, 91191 Gif-sur-Yvette, France.

In several instances, a monoclonal antibody raised against a receptor ligand has been claimed to mimic the ligand receptor. Thus, a specific monoclonal antibody (Malpha2-3) raised against a short-chain toxin from snake was proposed to mimic the nicotinic acetylcholine receptor (AChR) (). Further confirming this mimicry, we show that (i) like AChR, Malpha2-3 elicits anti-AChR antibodies, which in turn elicit anti-toxin antibodies; and (ii) the region 106-122 of the alpha-chain of AChR shares 66% primary structure identity with complementarity-determining regions of Malpha2-3. Also, a mutational analysis of erabutoxin a reveals that the epitope recognized by Malpha2-3 consists of 10 residues, distributed within the three toxin loops. Eight of these residues also belong to the 10-residue epitope recognized by AChR, a result that offers an explanation as to the functional similarities between the receptor and the antibody. Strikingly, however, most of the residues common to the two epitopes contribute differentially to the energetic formation of the antibody-toxin and the receptor-toxin complexes. Together, the data suggest that the mimicry between AChR and Malpha2-3 is partial only.

UI MeSH Term Description Entries
D008958 Models, Molecular Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures. Molecular Models,Model, Molecular,Molecular Model
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D011950 Receptors, Cholinergic Cell surface proteins that bind acetylcholine with high affinity and trigger intracellular changes influencing the behavior of cells. Cholinergic receptors are divided into two major classes, muscarinic and nicotinic, based originally on their affinity for nicotine and muscarine. Each group is further subdivided based on pharmacology, location, mode of action, and/or molecular biology. ACh Receptor,Acetylcholine Receptor,Acetylcholine Receptors,Cholinergic Receptor,Cholinergic Receptors,Cholinoceptive Sites,Cholinoceptor,Cholinoceptors,Receptors, Acetylcholine,ACh Receptors,Receptors, ACh,Receptor, ACh,Receptor, Acetylcholine,Receptor, Cholinergic,Sites, Cholinoceptive
D003039 Cobra Neurotoxin Proteins Toxins, contained in cobra (Naja) venom that block cholinergic receptors; two specific proteins have been described, the small (short, Type I) and the large (long, Type II) which also exist in other Elapid venoms. Cobra Neurotoxins,Cobrotoxin,Neurotoxin Proteins, Cobra,Neurotoxins, Cobra,Proteins, Cobra Neurotoxin
D003429 Cross Reactions Serological reactions in which an antiserum against one antigen reacts with a non-identical but closely related antigen. Cross Reaction,Reaction, Cross,Reactions, Cross
D003472 Curare Plant extracts from several species, including genera STRYCHNOS and Chondodendron, which contain TETRAHYDROISOQUINOLINES that produce PARALYSIS of skeletal muscle. These extracts are toxic and must be used with the administration of artificial respiration.
D004870 Erabutoxins Toxins isolated from the venom of Laticauda semifasciata, a sea snake (Hydrophid); immunogenic, basic polypeptides of 62 amino acids, folded by four disulfide bonds, block neuromuscular end-plates irreversibly, thus causing paralysis and severe muscle damage; they are similar to Elapid neurotoxins.
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D000911 Antibodies, Monoclonal Antibodies produced by a single clone of cells. Monoclonal Antibodies,Monoclonal Antibody,Antibody, Monoclonal

Related Publications

F Ducancel, and K Mérienne, and C Fromen-Romano, and O Trémeau, and L Pillet, and P Drevet, and S Zinn-Justin, and J C Boulain, and A Ménez
February 1998, Proteins,
F Ducancel, and K Mérienne, and C Fromen-Romano, and O Trémeau, and L Pillet, and P Drevet, and S Zinn-Justin, and J C Boulain, and A Ménez
April 1986, Molecular immunology,
F Ducancel, and K Mérienne, and C Fromen-Romano, and O Trémeau, and L Pillet, and P Drevet, and S Zinn-Justin, and J C Boulain, and A Ménez
October 1979, FEBS letters,
F Ducancel, and K Mérienne, and C Fromen-Romano, and O Trémeau, and L Pillet, and P Drevet, and S Zinn-Justin, and J C Boulain, and A Ménez
January 1987, Journal of immunology (Baltimore, Md. : 1950),
F Ducancel, and K Mérienne, and C Fromen-Romano, and O Trémeau, and L Pillet, and P Drevet, and S Zinn-Justin, and J C Boulain, and A Ménez
February 1996, Experimental hematology,
F Ducancel, and K Mérienne, and C Fromen-Romano, and O Trémeau, and L Pillet, and P Drevet, and S Zinn-Justin, and J C Boulain, and A Ménez
February 2017, Poultry science,
F Ducancel, and K Mérienne, and C Fromen-Romano, and O Trémeau, and L Pillet, and P Drevet, and S Zinn-Justin, and J C Boulain, and A Ménez
March 1989, Infection and immunity,
F Ducancel, and K Mérienne, and C Fromen-Romano, and O Trémeau, and L Pillet, and P Drevet, and S Zinn-Justin, and J C Boulain, and A Ménez
August 2009, Biochemical and biophysical research communications,
F Ducancel, and K Mérienne, and C Fromen-Romano, and O Trémeau, and L Pillet, and P Drevet, and S Zinn-Justin, and J C Boulain, and A Ménez
April 2015, Journal of molecular recognition : JMR,
F Ducancel, and K Mérienne, and C Fromen-Romano, and O Trémeau, and L Pillet, and P Drevet, and S Zinn-Justin, and J C Boulain, and A Ménez
September 1991, Journal of neurochemistry,
Copied contents to your clipboard!