Reassociation with beta 2-microglobulin is necessary for Db class I major histocompatibility complex binding of an exogenous influenza peptide

作者: K. L. Rock , S. Gamble , L. Rothstein , B. Benacerraf

DOI: 10.1073/PNAS.88.1.301

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摘要: Abstract A synthetic peptide corresponding to residues 365-380 of the influenza nucleoprotein (NP365-380) has been previously shown associate with class I major histocompatibility complex-encoded molecules and stimulate cytotoxic T lymphocytes [Townsend, A. R. M., Rothbard, J., Gotch, F. Bahadur, G., Wraith, D. & McMichael, J. (1986) Cell 44, 959-968]. We find that intact Db heterodimers on cell surface are unreceptive binding this antigen. However, NP365-380 readily associates plasma membrane in presence exogenous beta 2-microglobulin. In addition, there is a second pathway through which requires energy de novo protein synthesis. These findings have implications for maintaining immunological identity cells use peptides as vaccines priming cytolytic T-cell immunity.

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