Affiliations: [a] Department of Neurology, College of Physicians and Surgeons of Columbia University, New York, NY, USA | [b] Department of Cellular and Molecular Biology, Merck Sharp and Dohme Research Laboratories, Rahway, NJ, USA
Note: [] Address reprint requests to Dr. Linda Spatz, Dept. of Microbiology and Immunology, Forcheimer Bldg. Rm. 405, Albert Einstein College of Medicine of Yeshiva University, 1300 Morris Park Avenue, Bronx, New York 10461, USA.
Note: [] This work was supported by NIH grant NS25187 to N. Latov.
Abstract: 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 CVIP 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.
