Specificity of mouse and human monoclonal antibodies to myelin-associated glycoprotein

E NOBILE-ORAZIO; A. P HAYS; N LATOV; G PERMAN; J GOLIER; M. E SHY; L FREDDO

doi:10.1212/WNL.34.10.1336

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Specificity of mouse and human monoclonal antibodies to myelin-associated glycoprotein

Journal article

Peer reviewed

Specificity of mouse and human monoclonal antibodies to myelin-associated glycoprotein

E NOBILE-ORAZIO, A. P HAYS, N LATOV, G PERMAN, J GOLIER, M. E SHY and L FREDDO

Neurology, Vol.34(10), pp.1336-1342

1984

DOI: 10.1212/WNL.34.10.1336

PMID: 6207463

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Abstract

Some patients with neuropathy have IgM M-proteins that bind to myelin and to myelin-associated glycoprotein (MAG). We compared the binding properties of a human anti-MAG M-protein with three mouse monoclonal anti-MAG antibodies (GEN-S1, GEN-S3, GEN-S8) and with a mouse monoclonal antibody (HNK-1) that binds to both MAG and to human natural killer cells. The antibodies GEN-S1, GEN-S3, and GEN-S8 bound to different epitopes in the polypeptide portion of MAG as shown by peptide mapping, deglycosylation and competitive binding studies. The M-protein and HNK-1 bound to both CNS and PNS MAG and to several additional protein bands of 70K, 30K, 26K, and 23K daltons in peripheral, but not in central myelin; they did not bind to deglycosylated MAG. The M-protein and HNK-1 immunostained myelin diffusely, whereas GEN-S8 immunostained only the periaxonal and outer regions of myelin sheath, and there was no staining with GEN-S1 or GEN-S3. The human M-proteins probably bind to a carbohydrate moiety in MAG that is also present in other PNS myelin proteins. This may explain the observed differences in immunostaining and the sparing of the CNS in patients with anti-MAG M-proteins.

Fundamental and applied biological sciences. Psychology

Antibodies, immunoglobulins

Fundamental immunology

Biological and medical sciences

Molecular immunology

Details

Title: Subtitle: Specificity of mouse and human monoclonal antibodies to myelin-associated glycoprotein
Creators: E NOBILE-ORAZIO - Columbia univ., coll. physicians surgeons, New York NY 10032, United States
A. P HAYS - Columbia univ., coll. physicians surgeons, New York NY 10032, United States
N LATOV - Columbia univ., coll. physicians surgeons, New York NY 10032, United States
G PERMAN - Columbia univ., coll. physicians surgeons, New York NY 10032, United States
J GOLIER - Columbia univ., coll. physicians surgeons, New York NY 10032, United States
M. E SHY - Columbia univ., coll. physicians surgeons, New York NY 10032, United States
L FREDDO - Columbia univ., coll. physicians surgeons, New York NY 10032, United States
Resource Type: Journal article
Publication Details: Neurology, Vol.34(10), pp.1336-1342
Publisher: Lippincott Williams & Wilkins; Hagerstown, MD
DOI: 10.1212/WNL.34.10.1336
PMID: 6207463
ISSN: 0028-3878
eISSN: 1526-632X
Language: English
Date published: 1984
Academic Unit: Neurology; Molecular Physiology and Biophysics; Stead Family Department of Pediatrics; Iowa Neuroscience Institute
Record Identifier: 9984020630602771

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