TY - JOUR
T1 - 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
AU - Billetta, Rosario
AU - Filaci, Gilberto
AU - Zanetti, Maurizio
PY - 1995/3
Y1 - 1995/3
N2 - 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 Db allele in H-2b mice. We demonstrate that B lymphoma cells (H-2b) harboring the antigenized H-chain gene process and present the NP peptide in association with the Db 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-2b target cells. The endogenously processed immunoglobulin CDR3 peptide could be eluted from surface Db 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.
AB - 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 Db allele in H-2b mice. We demonstrate that B lymphoma cells (H-2b) harboring the antigenized H-chain gene process and present the NP peptide in association with the Db 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-2b target cells. The endogenously processed immunoglobulin CDR3 peptide could be eluted from surface Db 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.
KW - Antigenized genes
KW - Engineered cells
KW - Major histocompatibility complex class I presentation in B cells
UR - http://www.scopus.com/inward/record.url?scp=0028947160&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0028947160&partnerID=8YFLogxK
U2 - 10.1002/eji.1830250323
DO - 10.1002/eji.1830250323
M3 - Article
C2 - 7705408
AN - SCOPUS:0028947160
VL - 25
SP - 776
EP - 783
JO - European Journal of Immunology
JF - European Journal of Immunology
SN - 0014-2980
IS - 3
ER -