Molecular mimicry and myasthenia gravis. An autoantigenic site of the acetylcholine receptor α-subunit that has biologic activity and reacts immunochemically with herpes simplex virus

P. L. Schwimmbeck, T. Dyrberg, Daniel B Drachman, M. B A Oldstone

Research output: Contribution to journalArticle

Abstract

The large majority of patients with the autoimmune disease myasthenia gravis characteristically have detectable antibodies against the acetylcholine receptor (AChR). We used synthetic peptides to identify antibodies in sera of myasthenia gravis patients reactive with the human acetylcholine receptor (HuAChR) α-subunit, residues 160-167. Affinity purification of these antibodies, using the HuAChR α-subunit 157-170 peptide immobilized on thiopropyl-Sepharose, yielded IgG antibodies that bound to the native AChR and inhibited the binding of α-bungarotoxin to the receptor. The HuAChR α-subunit 160-167 peptide demonstrated specific immunological cross-reactivity with a shared homologous domain on herpes simplex virus glycoprotein D, residues 286-293, by both binding and inhibition studies. Thus, HuAChR α-subunit, residues 160-167, elicits antibodies in myasthenic patients that binds to the native AChR protein and is capable of eliciting a biologic effect. Immunologic cross-reactivity of this 'self' epitope with herpes simplex virus suggest that this virus may be associated with the initiation of some cases of myasthenia.

Original languageEnglish (US)
Pages (from-to)1174-1180
Number of pages7
JournalJournal of Clinical Investigation
Volume84
Issue number4
StatePublished - 1989
Externally publishedYes

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Molecular Mimicry
Myasthenia Gravis
Cholinergic Receptors
Simplexvirus
Antibodies
Peptides
Bungarotoxins
Antibody Affinity
Muscle Weakness
Autoimmune Diseases
Epitopes
Glycoproteins
Immunoglobulin G
Viruses
Serum

ASJC Scopus subject areas

  • Medicine(all)

Cite this

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title = "Molecular mimicry and myasthenia gravis. An autoantigenic site of the acetylcholine receptor α-subunit that has biologic activity and reacts immunochemically with herpes simplex virus",
abstract = "The large majority of patients with the autoimmune disease myasthenia gravis characteristically have detectable antibodies against the acetylcholine receptor (AChR). We used synthetic peptides to identify antibodies in sera of myasthenia gravis patients reactive with the human acetylcholine receptor (HuAChR) α-subunit, residues 160-167. Affinity purification of these antibodies, using the HuAChR α-subunit 157-170 peptide immobilized on thiopropyl-Sepharose, yielded IgG antibodies that bound to the native AChR and inhibited the binding of α-bungarotoxin to the receptor. The HuAChR α-subunit 160-167 peptide demonstrated specific immunological cross-reactivity with a shared homologous domain on herpes simplex virus glycoprotein D, residues 286-293, by both binding and inhibition studies. Thus, HuAChR α-subunit, residues 160-167, elicits antibodies in myasthenic patients that binds to the native AChR protein and is capable of eliciting a biologic effect. Immunologic cross-reactivity of this 'self' epitope with herpes simplex virus suggest that this virus may be associated with the initiation of some cases of myasthenia.",
author = "Schwimmbeck, {P. L.} and T. Dyrberg and Drachman, {Daniel B} and Oldstone, {M. B A}",
year = "1989",
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AU - Schwimmbeck, P. L.

AU - Dyrberg, T.

AU - Drachman, Daniel B

AU - Oldstone, M. B A

PY - 1989

Y1 - 1989

N2 - The large majority of patients with the autoimmune disease myasthenia gravis characteristically have detectable antibodies against the acetylcholine receptor (AChR). We used synthetic peptides to identify antibodies in sera of myasthenia gravis patients reactive with the human acetylcholine receptor (HuAChR) α-subunit, residues 160-167. Affinity purification of these antibodies, using the HuAChR α-subunit 157-170 peptide immobilized on thiopropyl-Sepharose, yielded IgG antibodies that bound to the native AChR and inhibited the binding of α-bungarotoxin to the receptor. The HuAChR α-subunit 160-167 peptide demonstrated specific immunological cross-reactivity with a shared homologous domain on herpes simplex virus glycoprotein D, residues 286-293, by both binding and inhibition studies. Thus, HuAChR α-subunit, residues 160-167, elicits antibodies in myasthenic patients that binds to the native AChR protein and is capable of eliciting a biologic effect. Immunologic cross-reactivity of this 'self' epitope with herpes simplex virus suggest that this virus may be associated with the initiation of some cases of myasthenia.

AB - The large majority of patients with the autoimmune disease myasthenia gravis characteristically have detectable antibodies against the acetylcholine receptor (AChR). We used synthetic peptides to identify antibodies in sera of myasthenia gravis patients reactive with the human acetylcholine receptor (HuAChR) α-subunit, residues 160-167. Affinity purification of these antibodies, using the HuAChR α-subunit 157-170 peptide immobilized on thiopropyl-Sepharose, yielded IgG antibodies that bound to the native AChR and inhibited the binding of α-bungarotoxin to the receptor. The HuAChR α-subunit 160-167 peptide demonstrated specific immunological cross-reactivity with a shared homologous domain on herpes simplex virus glycoprotein D, residues 286-293, by both binding and inhibition studies. Thus, HuAChR α-subunit, residues 160-167, elicits antibodies in myasthenic patients that binds to the native AChR protein and is capable of eliciting a biologic effect. Immunologic cross-reactivity of this 'self' epitope with herpes simplex virus suggest that this virus may be associated with the initiation of some cases of myasthenia.

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