Document 0493
 DOCN  M9480493
 TI    Differential effects of flanking residues on presentation of epitopes
       from chimeric peptides.
 DT    9410
 AU    Bergmann CC; Tong L; Cua R; Sensintaffar J; Stohlman S; Department of
       Neurology, University of Southern California School; of Medicine, Los
       Angeles 90033.
 SO    J Virol. 1994 Aug;68(8):5306-10. Unique Identifier : AIDSLINE
       MED/94309203
 AB    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.
 DE    Amino Acid Sequence  Animal  Antigenic Determinants/*IMMUNOLOGY  Base
       Sequence  Capsid/*IMMUNOLOGY  DNA, Viral  Gene Products, gag/*IMMUNOLOGY
       Human  HIV-1/*IMMUNOLOGY  Molecular Sequence Data  Open Reading Frames
       Support, Non-U.S. Gov't  Support, U.S. Gov't, P.H.S.  T-Lymphocytes,
       Cytotoxic/IMMUNOLOGY  Viral Core Proteins/*IMMUNOLOGY  JOURNAL ARTICLE

       SOURCE: National Library of Medicine.  NOTICE: This material may be
       protected by Copyright Law (Title 17, U.S.Code).