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M94A3167.TXT
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1994-10-25
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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).