Expression of recombinant human anti-MAG antibodies in non-lymphoid mammalian cells.
The variable heavy and light chain genes of a monoclonal, IgM, anti-MAG antibody from a patient with neuropathy were inserted into expression vectors containing the gamma and kappa constant regions respectively and co-transfected into monkey kidney CV1P cells. The expressed antibody had the same antigenic specificity but significantly lower avidity than the native IgM, anti-MAG, antibody as detected by ELISA. When the variable heavy chain gene of the anti-MAG antibody was co-transfected with the variable light chain gene from another monoclonal, IgM, anti-MAG antibody, a fully assembled antibody was expressed as determined by a trapping ELISA, but it did not bind to (MAG) or to sulfated glucuronic acid paragloboside, indicating that both heavy and light chains contribute to the binding activity.
Spatz
L A
LA
Department of Neurology, College of Physicians and Surgeons of Columbia University, New York, NY.
Daugherty
B L
BL
DeMartino
J A
JA
Mark
G E
GE
Latov
N
N
D000818:Animals; D000911:Antibodies, Monoclonal / Q000235:genetics*; D000915:Antibody Affinity; D000918:Antibody Specificity; D001483:Base Sequence; D002460:Cell Line; D004247:DNA / Q000235:genetics; D015870:Gene Expression; D005803:Genes, Immunoglobulin; D006801:Humans; D007075:Immunoglobulin M / Q000235:genetics; D008969:Molecular Sequence Data; D009185:Myelin Proteins / Q000276:immunology*; D018992:Myelin-Associated Glycoprotein; D014162:Transfection
D000911:Antibodies, Monoclonal; D007075:Immunoglobulin M; D009185:Myelin Proteins; D018992:Myelin-Associated Glycoprotein; D004247:DNA