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Different class I antigen oligosaccharides on a murine tumor and a lectin‐resistant variant are not responsible for the differential recognition of the tumors by CTL
Author(s) -
Degen Eric,
Laferte Suzanne,
Elliott Bruce E.,
Williams David B.
Publication year - 1989
Publication title -
international journal of cancer
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.475
H-Index - 234
eISSN - 1097-0215
pISSN - 0020-7136
DOI - 10.1002/ijc.2910430515
Subject(s) - ctl* , biology , cytotoxic t cell , major histocompatibility complex , wheat germ agglutinin , antigen , lectin , human leukocyte antigen , microbiology and biotechnology , immunology , biochemistry , in vitro
Previous studies have shown that whereas a highly malignant mouse cell line termed MDAY‐D2 (d haplotype) does not elicit a detectable response by cytotoxic T lymphocytes (CTL) in DBA/2 mice, strong anti‐tumor CTL are generated against a wheat‐germ‐agglutinin‐resistant variant, designated MDW3. Additional evidence suggests these anti‐MDW3 CTL may not be a consequence of a unique antigenic determinant on the variant cells. Because MDW3 cells are expected to differ from MDAY‐D2 cells in their surface carbohydrate structures (due to their lectin resistance) and Class 1 major histocompatibility molecules play a crucial role in CTL‐mediated responses, we speculated that the Asn‐linked oligosaccharides present on Class 1 molecules of MDAY‐D2 and MDW3 might be different and could potentially influence recognition by the anti‐MDW3 CTL. High‐resolution gel filtration analyses and Con A‐Sepharose affinity chromatography clearly demonstrated that the oligosaccharides isolated from the H‐2D d molecule of MDAY‐D2 cells are larger and more highly branched than those of the MDW3 variant. Taken together with the finding that anti‐MDW3 CTL are restricted by H‐2D d , these results suggested that the larger H‐2D D oligosaccharides on MDAY‐D2 cells could potentially mask or perturb determinants required for recognition by these CTL. To test this postulate, the surface Class I oligosaccharides of both MDAY‐D2 and MDW3 cells were converted to simpler hybrid structures by treatment with the oligosaccharide processing inhibitor, swainsonine. However, no effect was observed on the lysis or binding of either MDAY‐D2 or MDW3 cells by anti‐MDW3 CTL. Thus, the results do not support the possibility that the larger H‐2D d oligosaccharides on MDAY‐D2 cells are, in themselves, responsible for the poor recognition of the parent tumor by anti‐MDW3 CTL. Our data to indicate, however, that CTL target binding and effector functions are not dependent on the fine structure of complex Asnlinked carbohydrates present on Class 1 molecules and possibly on other, accessory molecules at the target cell surface, since MDW3 cells maintained their sensitivity to lysis by CTL following swainsonine treatment.