Abstract
The B cell antigen receptor (BCR) functions to initiate signaling and to internalize antigen for processing from within Lyn kinase-enriched membrane lipid rafts. The signaling function of the BCR is blocked by Epstein-Barr Virus (EBV) latent membrane protein 2A (LMP2A), which is constitutively phosphorylated by Lyn. Here, we show that LMP2A resides in lipid rafts and excludes the BCR from entering rafts by Lyn-dependent mechanisms, thus blocking both BCR signaling and antigen transport. Mutant LMP2A that permits BCR signaling and raft translocation still blocks antigen trafficking, indicating independent control of these BCR functions. Thus, EBV coopts the lipid rafts to disarm both the signaling and antigen-processing functions of the BCR by independent mechanisms.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 57-67 |
| Number of pages | 11 |
| Journal | Immunity |
| Volume | 14 |
| Issue number | 1 |
| DOIs | |
| State | Published - 2001 |
Funding
M. L. D. was supported in part by a training grant from the National Institutes of Health, T32 GM08061. R. L. is supported by Public Health Service grants CA62234 and CA73507 from the National Cancer Institute and DE13127 from the National Institute of Dental and Craniofacial Research. R. L. is a Scholar of the Leukemia Lymphoma Society. We are grateful for the contributions of Ceida Chan and Anna Morrison to this work and to Dr. Douglas T. Fearon of the University of Cambridge, who provided the rat monoclonal antibody YL1/2, specific for tubulin.
ASJC Scopus subject areas
- Immunology and Allergy
- Immunology
- Infectious Diseases
