Document 0467
 DOCN  M9460467
 TI    A simple assay for detection of peptides promoting the assembly of HLA
       class I molecules.
 DT    9404
 AU    Connan F; Hlavac F; Hoebeke J; Guillet JG; Choppin J; Institut Cochin de
       Genetique Moleculaire (ICGM), INSERM U152,; Paris, France.
 SO    Eur J Immunol. 1994 Mar;24(3):777-80. Unique Identifier : AIDSLINE
       MED/94170859
 AB    Synthetic peptides derived from influenza virus and human
       immunodeficiency virus were tested for their ability to promote the
       assembly of HLA-A2 and HLA-B51 molecules in T2 cell lysates. Specific
       assembly was detected by an enzyme-linked immunosorbent assay. The most
       significant HLA-A2 assembly was obtained in the presence of peptides
       known to be targets for HLA-A2-restricted cytotoxic T lymphocytes
       (influenza matrix M.58-66 and HIV Pol 476-484). Three of a batch of Nef
       peptides corresponding to epitopic regions for cytotoxic T lymphocytes,
       caused significant assembly of HLA-A2 (Nef 83-91, 137-145 and 144-153),
       but only at high concentrations (100 microM). As these peptides bound
       relatively weakly, it is unlikely that they are good candidates for
       HLA-A2-restricted CTL epitopes. Peptides matrix M.60-68, Nef 186-194,
       and Plasmodium falciparum sh.77-85 produced the most significant
       assembly of HLA-B51. These peptides have a dominant hydrophobic anchor
       residue (V, L. I) at position 9 that could occupy pocket F. Our results
       also suggest that another hydrophobic residue (V, L) at position 3 or 4
       may anchor to hydrophobic pocket D of HLA-B51. Proline at position 2
       greatly increases HLA-B51 anchoring.
 DE    Amino Acid Sequence  Animal  Antigens, Protozoan/CHEMISTRY/*METABOLISM
       Antigens, Viral/CHEMISTRY/*METABOLISM  Gene Products,
       nef/CHEMISTRY/METABOLISM  HLA-A2 Antigen/*METABOLISM  HLA-B
       Antigens/*METABOLISM  Macromolecular Systems  Molecular Sequence Data
       Orthomyxovirus Type A, Human/IMMUNOLOGY  Peptides/*IMMUNOLOGY/METABOLISM
       Plasmodium falciparum/IMMUNOLOGY  Protein Binding  Structure-Activity
       Relationship  JOURNAL ARTICLE

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