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
R. Billetta et al., 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, European Journal of Immunology, 25(3), 1995, pp. 776-783
We analyzed the capacity of B cells to process and present a peptide f
rom the variable region of an endogenous immunoglobulin heavy (H) chai
n to a major histocompatibility complex (MHC) class I-restricted cytot
oxic Tlymphocyte (CTL) clone. The H-chain gene was engineered to expre
ss 14-amino acid peptide from the sequence of the influenza virus nucl
eoprotein (NP) antigen in the third complementarity-determining region
(CDR3). This NP peptide is presented in association with the D-b alle
le in H-2(b) mice, We demonstrate that B lymphoma cells (H-2(b)) harbo
ring the antigenized H-chain gene process and present the NP peptide i
n association with the D-b molecule and are lysed by a CTL clone speci
fic for that peptide in an MHC-restricted way. In contrast, the solubl
e antigenized antibody failed to mediate lysis of H-2(b) target cells.
The endogenously processed immunoglobulin CDR3 peptide could be elute
d 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 pathw
ay and are presented to CD8(+) T cells in the context of MHC class I m
olecules. The implication of these findings for processing and present
ation of endogenous immunoglobulin peptides in B cells and network reg
ulation by idiopeptides is discussed.