Main Immunogenic Region of Torpedo Electroplax and Human Muscle Acetylcholine Receptor: Localization and Microheterogeneity Revealed by the Use of Synthetic Peptides

1990 ◽  
Vol 54 (1) ◽  
pp. 51-61 ◽  
Author(s):  
Socrates J. Tzartos ◽  
Heleni V. Loutrari ◽  
Fen Tang ◽  
Anna Kokla ◽  
Susan L. Walgrave ◽  
...  
Keyword(s):  
Acetylcholine Receptor ◽  
Synthetic Peptides ◽  
Human Muscle ◽  
Receptor Localization ◽  
Immunogenic Region

Two-dimensional1H-nmr study of synthetic peptides containing the main immunogenic region of theTorpedo acetylcholine receptor

Biopolymers ◽  
1989 ◽  
Vol 28 (1) ◽  
pp. 465-478 ◽  
Author(s):  
M. T. Cung ◽  
M. Marraud ◽  
I. Hadjidakis ◽  
E. Bairaktari ◽  
C. Sakarellos ◽  
...  
Keyword(s):  
Acetylcholine Receptor ◽  
Synthetic Peptides ◽  
Immunogenic Region ◽  
Nmr Study

scholarly journals The crystal structure of the Fab fragment of a rat monoclonal antibody against the main immunogenic region of the human muscle acetylcholine receptor

2000 ◽  
Vol 267 (8) ◽  
pp. 2389-2397 ◽  
Author(s):  
Maria Kontou ◽  
Demetres D Leonidas ◽  
Efstratia H. Vatzaki ◽  
Panayiota Tsantili ◽  
Avgi Mamalaki ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Monoclonal Antibody ◽  
Acetylcholine Receptor ◽  
Human Muscle ◽  
Fab Fragment ◽  
Immunogenic Region

scholarly journals Antigenic role of single residues within the main immunogenic region of the nicotinic acetylcholine receptor

1990 ◽  
Vol 269 (1) ◽  
pp. 239-245 ◽  
Author(s):  
I Papadouli ◽  
S Potamianos ◽  
I Hadjidakis ◽  
E Bairaktari ◽  
V Tsikaris ◽  
...  
Keyword(s):  
Acetylcholine Receptor ◽  
Electric Organ ◽  
Human Muscle ◽  
Alpha Subunit ◽  
Binding Studies ◽  
Nicotinic Acetylcholine ◽  
Immunogenic Region ◽  
Extracellular Side ◽  
Peptide Analogues

The target of most of the autoantibodies against the acetylcholine receptor (AChR) in myasthenic sera is the main immunogenic region (MIR) on the extracellular side of the AChR alpha-subunit. Binding of anti-MIR monoclonal antibodies (mAbs) has been recently localized between residues alpha 67 and alpha 76 of Torpedo californica electric organ (WNPADYGGIK) and human muscle (WNPDDYGGVK) AChR. In order to evaluate the contribution of each residue to the antigenicity of the MIR, we synthesized peptides corresponding to residues alpha 67-76 from Torpedo and human AChRs, together with 13 peptide analogues. Nine of these analogues had one residue of the Torpedo decapeptide replaced by L-alanine, three had a structure which was intermediate between those of the Torpedo and human alpha 67-76 decapeptides, and one had D-alanine in position 73. Binding studies employing six anti-MIR mAbs and all 15 peptides revealed that some residues (Asn68 and Asp71) are indispensable for binding by all mAbs tested, whereas others are important only for binding by some mAbs. Antibody binding was mainly restricted to residues alpha 68-74, the most critical sequence being alpha 68-71. Fish electric organ and human MIR form two distinct groups of strongly overlapping epitopes. Some peptide analogues enhanced mAb binding compared with Torpedo and human peptides, suggesting that the construction of a very antigenic MIR is feasible.

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