International Immunology, Vol 9, 889-896, Copyright © 1997 by Oxford University Press
S Weenink, H Averdunk, T Boston, V Boswarva, JC Guery, L Adorini, E Mellins, J McCluskey and AM Gautam
The inability of certain antigen processing mutant cell lines to present
intact proteins to T cells and to form SDS-stable MHC class II dimers has
been shown to result from defective expression of HLA- encoded DMA and DMB
genes. We have utilized some of these mutants to determine species
compatibility of antigen presentation components. Mouse MHC class II I-Ad
cDNA was transfected into the human B cell lymphoblastoid cell lines 8.1.6,
7.9.6 (a mutant cell line derived from 8.1.6) and an independent deletion
mutant T2 (called 8.1.6d, 7.9.6d and T2.d respectively). These cells were
than examined for various functions in antigen presentation. Interestingly,
none of the cells transfected with I-Ad presented peptides derived from
intact proteins to specific T cell hybridomas. However, presentation of
synthetic peptides by these cells was normal. The ability to form
SDS-stable dimers was dramatically reduced in the transfectants. In
addition, I-Ad molecules at the cell surface appeared loaded predominantly
with the invariant chain peptides, CLIP. These properties of the I-Ad
transfectants are identical to those described for HLA class II molecules
expressed in HLA-DM mutants. Perhaps the most interesting finding was the
inability of I-Ad in 8.1.6 to present protein antigens. Since 8.1.6 cells
present antigens to HLA-DR, DP, DQ-restricted T cells and also have intact
HLA-DM and invariant chain (II) functions, these results argue that some
component of human antigen processing machinery is incompatible with I-Ad
molecules.
ARTICLES
Impaired antigen presentation by murine I-Ad class II MHC molecules expressed in normal and HLA-DM-defective human B cell lines
Division of Molecular Medicine, John Curtin School of Medical Research, Australian National University, Canberra, Australia.
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