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


     
 


This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
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 Google Scholar
Google Scholar
Right arrow Articles by Manderson, A. P.
Right arrow Articles by Parish, C. R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Manderson, A. P.
Right arrow Articles by Parish, C. R.
Right arrowPubmed/NCBI databases
*Substance via MeSH
The Journal of Immunology, 2006, 177: 5155-5162.
Copyright © 2006 by The American Association of Immunologists, Inc.

A Novel Mechanism for Complement Activation at the Surface of B Cells Following Antigen Binding1

Anthony P. Manderson2,*,{dagger}, Ben Quah*, Marina Botto{dagger}, Chris C. Goodnow{ddagger}, Mark J. Walport3,{dagger} and Chris R. Parish4,*

* Cancer and Vascular Biology Group, Division of Immunology and Genetics, John Curtin School of Medical Research, Australian National University, Canberra, Australia; {dagger} Rheumatology Section, Division of Medicine, Faculty of Medicine, Imperial College, London, United Kingdom; and {ddagger} Immunogenomics Laboratory, Division of Immunology and Genetics, John Curtin School of Medical Research, Australian National University, Canberra, Australia

Coligation of CD21 with BCR on the surface of B cells provides a costimulatory signal essential for efficient Ab responses to T-dependent Ags. To achieve this, Ag must be directly linked to C3 fragments, but how this occurs in vivo is not fully understood. Using BCR transgenic mice, we demonstrated that C3 was deposited on the surface of B cells following both high- and moderate-affinity Ag binding. This was dependent on the specific binding of IgM to the BCR-bound Ag and can occur independently of soluble immune complex formation. Based on these data, we propose a novel model in which immune complexes can form directly on the surface of the B cell following Ag binding. This model has implications for our understanding of B lymphocyte activation.

The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked advertisement in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

1 This work was supported by Wellcome Trust Biomedical Research Collaboration Grant 063106, Wellcome Trust Programme Grant 071467, and a National Health and Medical Research Council of Australia Program grant.

2 Current address: Institute for Molecular Bioscience, University of Queensland, Brisbane, 4072, Australia.

3 Current address: Wellcome Trust, London NW1 2B6, U.K.

4 Address correspondence and reprint requests to Dr. Chris R. Parish, Division of Immunology and Genetics, John Curtin School of Medical Research, Australian National University, Canberra ACT 2601, Australia. E-mail address: Christopher.Parish{at}anu.edu.au

5 Abbreviations used in this paper: IC, immune complex; DEL, duck egg lysozyme; HEL, hen egg lysozyme.







HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
This Website Copyright © 2006 by The American Association of Immunologists, Inc. All rights reserved.
All Contents Copyright © 2006 by The American Association of Immunologists, Inc. All rights reserved.