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M94A3325.TXT
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1994-10-25
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Document 3325
DOCN M94A3325
TI Possible cooperativity of tryptase TL2 and CD26 on proteolytic cleavage
of V3 loop of HIV-1 gp120.
DT 9412
AU Niwa Y; Ohkubo I; Kido H; Inst. for Enzyme Res., Univ. of Tokushima,
Japan.
SO Int Conf AIDS. 1994 Aug 7-12;10(1):101 (abstract no. PA0021). Unique
Identifier : AIDSLINE ICA10/94369250
AB OBJECTIVES: Infection by HIV-1 is due to virus-cell fusion mediated by
the viral envelope glycoproteins gp120 and gp41 with CD4 and the other
cellular cofactors. In this study, possible cooperativity of cellular
cofactors, such as tryptase TL2 and CD26, on proteolytic cleavage of V3
loop of HIV-1 gp120 was analyzed. METHODS: Tryptase TL2 and CD26 were
purified from human CD4+ T cell line, Molt-4, clone 8 cells and from
human semen, respectively. V3 domain peptide of HTLV-IIIB was
synthesized and the cysteine residues were oxidized to make loop
structure. Proteolytic cleavage sites of the V3 loop by tryptase TL2
and/or CD26 were analyzed by reversed phase HPLC following determination
of amino acid sequences of the peptide fragments. RESULTS AND
CONCLUSIONS: Tryptase TL2, a membrane bound serine protease having both
trypsin- and chymotrypsin-like protease activities, preferentially
cleaved at sites between R317-G318 and/or F323-V324 and newly appeared
aminoterminal sequence glycyl proline of the product was further removed
by incubation with CD26, although CD26 by itself had no proteolytic
effect on the peptide. The results suggest that tryptase TL2 and CD26 on
the surface of T lymphocytes, monocytes and macrophages cooperatively
hydrolyzed V3 loop of HIV-1 gp120 resulting change in tertiary structure
of the gp120 and the viral internalization.
DE Amino Acid Sequence Antigens, Differentiation, T-Lymphocyte/*METABOLISM
Binding Sites Cell Line Human HIV Envelope Protein
gp120/GENETICS/*METABOLISM HIV Infections/ETIOLOGY
HIV-1/*METABOLISM/PHYSIOLOGY/PATHOGENICITY In Vitro Male Peptide
Fragments/GENETICS/*METABOLISM Semen/METABOLISM Serine
Proteinases/*METABOLISM T4 Lymphocytes/METABOLISM/MICROBIOLOGY MEETING
ABSTRACT
SOURCE: National Library of Medicine. NOTICE: This material may be
protected by Copyright Law (Title 17, U.S.Code).