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• W2029609407 endingPage "440" @default.
• W2029609407 startingPage "433" @default.
• W2029609407 abstract "Surface expression of the majority of class I major histocompatibility complex (MHC) heavy chains is known to require assembly with β2 microglobulin (β2m). To define other factors involved in class I MHC assembly, we have studied two tumor cell lines that are deficient in cell surface class I (H-2) expression. The BC2 fibrosarcoma and the CMT lung carcinoma express only intracellular unassociated heavy chains despite the presence of β2m. As described previously, when these cell lines are treated with interferon-γ (IFN-γ), they are capable of assembling and transporting class I molecules to the cell surface. In this study, we have shown that in the absence of IFN-γ these mutant cells are unable to present intracelluar viral antigens, although they can be lysed by specific cytotoxic T lymphocyte (CTL) after pre-incubation with the corresponding synthetic peptide. Flow cytometric analysis demonstrated that extracellular peptide was capable of increasing twofold the surface expression of β2m-heavy chain complexes. Furthermore, immunoprecipitation experiments confirmed that peptide stabilizes chain association in the BC2 cell lysates. However, infecting these mutants with vectors expressing either pre-processed antigen or rapidly degraded antigen, failed to overcome their defect in the presentation of endogenous peptide to specific CTL or to mediate surface expression of class I MHC. Preincubation with IFN-γ completely reversed the endogenous peptide presentation defect, even in mutant cells transfected with a vector encoding a cDNA for the H-2 molecule restricting CTL recognition. This last result suggests that IFN-γ corrects the defect by a mechanism separate from simple enhancement of the number of class I molecules produced by the cell. Because there is growing evidence that endogenous peptides can participate in class I MHC assembly, the defect in these mutants could be ascribed to the lack of access to class I molecules by the endogenous peptide. This would prevent stable association of the heavy and light chains and their subsequent transport. Our data suggests that IFN-γ reestablishes class I MHC surface expression by restoring access of endogenously synthesized peptide to class I molecules." @default.
• W2029609407 created "2016-06-24" @default.
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• W2029609407 date "1992-02-01" @default.
• W2029609407 modified "2023-09-27" @default.
• W2029609407 title "A defect in the presentation of intracellular viral antigens is restored by interferon-γ in cell lines with impaired major histocompatibility complex class I assembly" @default.
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• W2029609407 doi "https://doi.org/10.1002/eji.1830220222" @default.
• W2029609407 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/1537379" @default.
• W2029609407 hasPublicationYear "1992" @default.
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