Document 3167 DOCN M94A3167 TI Functional analysis of retroviral env peptide recognized by T helper clones. DT 9412 AU Yamagishi H; Shimizu T; Uenishi H; Teramura Y; Iwashiro M; Kuribayashi K; Dept. Biophysics, Fac. Science, Kyoto University, Japan. SO Int Conf AIDS. 1994 Aug 7-12;10(1):138 (abstract no. PA0172). Unique Identifier : AIDSLINE ICA10/94369408 AB OBJECTIVE: We studied peptide-MHC interactions and their subsequent recognition by murine retroviral env122-141 specific Th cells. METHODS: We used the target peptide of decreasing length to define the preferred size of peptide and the variant peptide with single alanine substitutions to identify key amino acids required for binding to MHC molecules and for stimulating Th clones in vitro. RESULTS: Systematic analysis defined the minimum core length of 13 amino acids (LTSLTPRCNTAWN). Th clones were different in reactivity toward varying peptide length and the variant peptides. Peptide analog possessing minimum requirement for length of 13 residues and 5 key contact residues did not initiate full T-cell signaling of a high responsive clone but restored full T-cell activity when linked to an octavalent antigen peptide system (MAPS). DISCUSSION AND CONCLUSIONS: Eight dendritic arms of MAP-peptide may increase the local density of TcR-MHC complexes to lead to T cell activation. Thus, the MAP-peptide may provide a powerful tool in eliciting retroviral peptide specific T helper responses. DE Amino Acid Sequence Animal Clone Cells Comparative Study Gene Products, env/*IMMUNOLOGY Lymphocyte Transformation Major Histocompatibility Complex Mice Molecular Sequence Data Oligopeptides/CHEMICAL SYNTHESIS/IMMUNOLOGY Peptide Fragments/CHEMICAL SYNTHESIS/*IMMUNOLOGY Retroviridae/*IMMUNOLOGY Structure-Activity Relationship T-Lymphocytes/*IMMUNOLOGY MEETING ABSTRACT SOURCE: National Library of Medicine. NOTICE: This material may be protected by Copyright Law (Title 17, U.S.Code).