Dimerization of CD4-C kappa chimeric molecules leads to loss of CD4 epitopes.

Abstract:

:Structural similarities between two members of the immunoglobulin superfamily were explored by making chimeric immunoglobulin/CD4 antigen molecules. A crossover in the middle of the originally proposed J kappa homology unit of the first domain of the CD4 molecule was used to construct a chimeric molecule having human and mouse CD4 antigen sequence through the first 108 amino acids and murine J kappa and C kappa sequence thereafter. This molecule was expressed in the presence and absence of an immunoglobulin heavy chain. The resulting proteins were assayed for the expression of CD4 epitopes that should be present based on epitope mapping data. Monomeric, homodimeric, and heavy chain/light chain tetrameric forms of the recombinant protein were secreted and were all detectable with anti-kappa reagents. CD4 antibodies precipitated only the form of the CD4-C kappa light chain protein which appears as a monomer by polyacrylamide gel electrophoresis. Neither the homodimer nor the heavy chain/light chain tetramer were detected with CD4 monoclonal antibodies. An engineered gene having this CD4 antigen first domain joined to the human IgG1 constant region, when coexpressed with a mouse lambda light chain, also failed to express detectable CD4 epitopes. The structural implications of the presence or absence of CD4 epitopes on these proteins is discussed.

journal_name

Mol Immunol

journal_title

Molecular immunology

authors

Frey T,Estess P,Oi VT

doi

10.1016/0161-5890(93)90002-s

subject

Has Abstract

pub_date

1993-06-01 00:00:00

pages

797-804

issue

9

eissn

0161-5890

issn

1872-9142

journal_volume

30

pub_type

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