PMID: 7518534Aug 1, 1994Paper

Differential effects of flanking residues on presentation of epitopes from chimeric peptides

Journal of Virology
Cornelia C BergmannStephen A Stohlman

Abstract

Chimeric peptides in which the optimal H-2d mouse hepatitis virus nucleocapsid (pN) and human immunodeficiency virus type 1 (p18) epitopes, separated by 38, 7, or 2 amino acids, were expressed from a single open reading frame by using recombinant vaccinia viruses to analyze antigen processing of proximal class I-restricted epitopes. Recognition of the carboxy-terminal Dd-restricted p18 epitope was independent of the amino-terminal flanking residues. By contrast, proximity of the carboxy-terminal epitope decreased recognition of the amino-terminal Ld-restricted pN epitope. Immunization resulted in the induction of both p18- and pN-specific antiviral cytotoxic T lymphocytes, irrespective of the number of amino acids separating the epitopes.

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Citations

May 3, 2000·The Journal of Experimental Medicine·A Moreau-AubryR Breathnach
Jun 18, 2002·Immunology and Cell Biology·Anne S De GrootWilliam Martin
Apr 7, 2004·The Journal of Experimental Medicine·Rika DraenertPhilip J R Goulder
Jan 19, 2006·Proceedings of the National Academy of Sciences of the United States of America·Nicole L La GrutaPeter C Doherty
Jan 13, 2000·Immunological Reviews·I A YorkK L Rock
Mar 30, 2010·The Journal of Immunology : Official Journal of the American Association of Immunologists·Daniel LópezMargarita Del Val
May 17, 2005·Immunogenetics·Bjoern PetersAlessandro Sette
Mar 9, 2002·The Journal of Immunology : Official Journal of the American Association of Immunologists·Robert F Rich, William R Green

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