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• W2170294980 endingPage "783" @default.
• W2170294980 startingPage "776" @default.
• W2170294980 abstract "Abstract We analyzed the capacity of B cells to process and present a peptide from the variable region of an endogenous immunoglobulin heavy (H) chain to a major histocompatibility complex (MHC) class I‐restricted cytotoxic T lymphocyte (CTL) clone. The H‐chain gene was engineered to express 14‐amino acid peptide from the sequence of the influenza virus nucleoprotein (NP) antigen in the third complementarity‐determining region (CDR3). This NP peptide is presented in association with the D b allele in H−2 b mice. We demonstrate that B lymphoma cells (H‐2 b ) harboring the antigenized H‐chain gene process and present the NP peptide in association with the D b molecule and are lysed by a CTL clone specific for that peptide in an MHC‐restricted way. In contrast, the soluble antigenized antibody failed to mediate lysis of H−2 b target cells. The endogenously processed immunoglobulin CDR3 peptide could be eluted from surface D b molecules in transfected cells. This study formally demonstrates that peptides from the hypervariable loops of endogenous immunoglobulin are processed through the endogenous degradative pathway and are presented to CD8 + T cells in the context of MHC class I molecules. The implication of these findings for processing and presentation of endogenous immunoglobulin peptides in B cells and network regulation by idiopeptides is discussed." @default.
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• W2170294980 date "1995-03-01" @default.
• W2170294980 modified "2023-10-11" @default.
• W2170294980 title "Major histocompatibility complex class I‐restricted presentation of influenza virus nucleoprotein peptide by B lymphoma cells harboring an antibody gene antigenized with the virus peptide" @default.
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• W2170294980 doi "https://doi.org/10.1002/eji.1830250323" @default.
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• W2170294980 hasPublicationYear "1995" @default.
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