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Science 3 May 1991:
Vol. 252. no. 5006, pp. 724 - 727
DOI: 10.1126/science.1902593
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Articles

Science, Vol 252, Issue 5006, 724-727
Copyright © 1991 by American Association for the Advancement of Science

articles

Effect of light chain V region duplication on IgG oligomerization and in vivo efficacy

W Shuford, HV Raff, JW Finley, J Esselstyn, and LJ Harris

Department of Immune Sciences, Bristol-Myers Squibb Pharmaceutical Research Institute-Seattle, WA 98121.

A human immunoglobulin G1 (IgG1) antibody oligomer was isolated from a transfected myeloma cell line that produced a monoclonal antibody to group B streptococci. Compared to the IgG1 monomer, the oligomer was significantly more effective at protecting neonatal rats from infection in vivo. The oligomer was also shown to cross the placenta and to be stable in neonatal rats. Immunochemical analysis and complementary DNA sequencing showed that the transfected cell line produced two distinct kappa light chains: a normal light chain (Ln) with a molecular mass of 25 kilodaltons and a 37-kilodalton species (L37), the domain composition of which was variable-variable-constant (V-V-C). Cotransfection of vectors encoding the heavy chain and L37 resulted in production of oligomeric IgG.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
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Cancer Res. 68, 8384-8392
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Homodimerization of tumor-reactive monoclonal antibodies markedly increases their ability to induce growth arrest or apoptosis of tumor cells.
M.-A. Ghetie, E. M. Podar, A. Ilgen, B. E. Gordon, J. W. Uhr, and E. S. Vitetta (1997)
PNAS 94, 7509-7514
   Abstract »    Full Text »    PDF »


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