The JI PBL Intereron Source
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     
 

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Rinfret, A.
Right arrow Articles by Klein, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Rinfret, A.
Right arrow Articles by Klein, M.
Right arrowPubmed/NCBI databases
*Substance via MeSH

The Journal of Immunology, Vol 145, Issue 3 925-931, Copyright © 1990 by American Association of Immunologists

ARTICLES

Isotype modulation of idiotypic expression in recombinant isotypic variants of MOPC 315

A Rinfret, C Horne, H Boux, A Marks, KJ Dorrington and M Klein
Department of Immunology, University of Toronto, Ontario, Canada.

The influence of the CH1 domains of various isotypes on the expression of four Id of the IgA 2 mouse myeloma protein MOPC 315 was assessed. To this end, mammalian expression vectors containing the rearranged MOPC 315 VH gene along with the H chain genes of various isotypes were constructed. These vectors were then transfected into the L chain- expressing MOPC 315.26 cell line to produce the rIg. The effect of polyvalency on the ability of Ig to bind anti-idiotypic antibodies was tested by comparing idiotypic expression in a competitive ELISA using reduced and nonreduced MOPC 315 IgA and IgM species. Reduction produced a two- to fivefold decrease in their ability to inhibit the binding of three anti-idiotypic antibodies, but not that of the functionally univalent antibody D10. In contrast, reduction of MOPC 315 IgG proteins did not affect the binding of the anti-Id mAb, indicating that reduction of the interchain disulfide bonds did not alter idiotypic expression. The expression of idiotopes on reduced mouse rIgA, IgM and IgG and human IgG MOPC 315 molecules was then compared. The results showed that both human and mouse IgG recombinant antibodies exhibited an enhanced expression of the idiotopes recognized by antibodies D10 and F1, as compared to MOPC 315 IgA and IgM molecules. In contrast, the expression of idiotopes recognized by A2 and G3 mAb was not influenced by the H chain isotype. These data support the hypothesis that the conformation of certain idiotopes is modulated by the isotype of the CH1 domain.


This article has been cited by other articles:


Home page
 J. Immunol.Home page
J. M. Phillips-Quagliata, S. Patel, J.-K. Han, S. Arakelov, T. D. Rao, M. J. Shulman, S. Fazel, R. B. Corley, M. Everett, M. H. Klein, et al.
The IgA/IgM Receptor Expressed on a Murine B Cell Lymphoma Is Poly-Ig Receptor
J. Immunol., September 1, 2000; 165(5): 2544 - 2555.
[Abstract] [Full Text] [PDF]

Home page
 J. Immunol.Home page
E. J. Wiersma, C. Collins, S. Fazel, and M. J. Shulman
Structural and Functional Analysis of J Chain-Deficient IgM
J. Immunol., June 15, 1998; 160(12): 5979 - 5989.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
W. D. Mallender, J. Carrero, and E. W. Voss Jr.
Comparative Properties of the Single Chain Antibody and Fv Derivatives of mAb 4-4-20
J. Biol. Chem., March 8, 1996; 271(10): 5338 - 5346.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
This Website Copyright © 1990 by The American Association of Immunologists, Inc. All rights reserved.
All Contents Copyright © 1990 by The American Association of Immunologists, Inc. All rights reserved.