Document 0106
 DOCN  M9550106
 TI    Molecular analysis of the same HIV peptide functionally binding to both
       a class I and a class II MHC molecule.
 DT    9505
 AU    Takeshita T; Takahashi H; Kozlowski S; Ahlers JD; Pendleton CD; Moore
       RL; Nakagawa Y; Yokomuro K; Fox BS; Margulies DH; et al; Molecular
       Immunogenetics and Vaccine Research Section, National; Cancer Institute,
       National Institutes of Health, Bethesda, MD; 20892.
 SO    J Immunol. 1995 Feb 15;154(4):1973-86. Unique Identifier : AIDSLINE
       MED/95138543
 AB    Although several peptides have been found to bind to both class I and
       class II molecules, the basis for this binding of the same peptide to
       two classes of MHC molecules has not been compared previously. We have
       analyzed one such peptide, P18 from the V3 loop of HIV-1 gp160, which we
       have previously shown to be recognized by CD8+ CTL with the class I
       molecule H-2Dd, and by CD4+ Th cells with the class II molecule I-Ad.
       With the use of truncated and substituted peptides, we found that the
       minimal core peptides are very similar, that the residues required for
       class I binding precisely fit the recently identified consensus motif
       for peptides binding to Dd (XGPX[R/K/H]XXX(X) [L/I/F]), and that at
       least three of the same residues are involved in binding to class II
       I-Ad. In addition, several of the same residues are involved in TCR
       interaction when the peptide is presented by class I and class II
       molecules. Modeling shows results to be consistent with the crystal
       structure of a peptide-class II MHC complex. Thus, the recognition of
       this versatile peptide by CD4+ Th cells with class II MHC molecules and
       by CD8+ cytotoxic T cells with class I MHC molecules is remarkably
       similar in both the core peptide used and the role of different residues
       in the ternary complex.
 DE    Amino Acid Sequence  Animal  Antigenic Determinants/IMMUNOLOGY  Binding,
       Competitive  Cell Line  Comparative Study  CD4-Positive
       T-Lymphocytes/*IMMUNOLOGY  CD8-Positive T-Lymphocytes/*IMMUNOLOGY  H-2
       Antigens/*IMMUNOLOGY/METABOLISM  Histocompatibility Antigens Class
       II/*IMMUNOLOGY/METABOLISM  HIV Envelope Protein
       gp120/*IMMUNOLOGY/METABOLISM  HIV-1/*IMMUNOLOGY  Lymphocyte
       Transformation  Mice  Mice, Inbred BALB C  Models, Molecular  Molecular
       Sequence Data  Mutagenesis, Site-Directed  Peptide
       Fragments/*IMMUNOLOGY/METABOLISM  Protein Binding  Protein Conformation
       Sequence Alignment  Structure-Activity Relationship  Support, U.S.
       Gov't, P.H.S.  JOURNAL ARTICLE

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