Skip Navigation


International Immunology Advance Access originally published online on July 28, 2006
International Immunology 2006 18(9):1385-1396; doi:10.1093/intimm/dxl072
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
18/9/1385    most recent
dxl072v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (2)
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Siegers, G. M.
Right arrow Articles by Schamel, W. W. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Siegers, G. M.
Right arrow Articles by Schamel, W. W. A.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?


© The Japanese Society for Immunology. 2006. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

Identification of disulfide bonds in the Ig-{alpha}/Ig-ß component of the B cell antigen receptor using the Drosophila S2 cell reconstitution system

Gabrielle M. Siegers, Jianying Yang, Claudia U. Duerr, Peter J. Nielsen, Michael Reth and Wolfgang W. A. Schamel

Max Planck-Institut für Immunbiologie and University of Freiburg, Biologie III Stübeweg 51, 79108 Freiburg, Germany

Correspondence to: W. W. A. Schamel; E-mail: schamel{at}immunbio.mpg.de

Structural information about immune receptor complexes is important for understanding signal transduction mechanisms. We have used the Drosophila S2 cell reconstitution system for identification of disulfide bonds within and between CD79a (Ig-{alpha}) and CD79b (Ig-ß), the heterodimeric signal transducing element of the B cell antigen receptor (BCR). Cysteines 113 and 135 of Ig-{alpha} and Ig-ß, respectively, form the intermolecular disulfide bridge stabilizing the Ig-{alpha}/Ig-ß heterodimer in both S2 cells and the B cell line J558L. Furthermore, using transfected S2 cells, two putative intramolecular disulfide bonds in the Ig-like domain of Ig-ß were identified. Ig-ßC65 and Ig-ßC120 form the canonical Ig fold disulfide bond. In addition, Ig-ßC43 and Ig-ßC124 also bind covalently. Individual cysteine to serine mutations in Ig-{alpha} had no influence on membrane-bound Ig (mIg)-M expression on the surface of S2 cells. In contrast, mIgM expression on the surface of B cells expressing Ig-{alpha}C113S was reduced, indicating that this intermolecular bond is prerequisite for efficient IgM-BCR formation. Our data also suggest that the Ig-{alpha}/Ig-ß heterodimer can assemble into oligomers.

Keywords: BCR assembly, cysteine mutants, Ig-{alpha}/Ig-ß heterodimer, Ig fold, surface mIgM expression

Transmitting editor: I. Pecht


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 J. Immunol.Home page
A. K. Dobbs, T. Yang, D. Farmer, L. Kager, O. Parolini, and M. E. Conley
Cutting Edge: A Hypomorphic Mutation in Igbeta (CD79b) in a Patient with Immunodeficiency and a Leaky Defect in B Cell Development
J. Immunol., August 15, 2007; 179(4): 2055 - 2059.
[Abstract] [Full Text] [PDF]


Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.