TRYPTASE-TL2 IN THE MEMBRANE OF HUMAN LYMPHOCYTES-T4+ IS A NOVEL BINDING-PROTEIN OF THE V3 DOMAIN OF HIV-1 ENVELOPE GLYCOPROTEIN-GP120

被引：50
作者：
KIDO, H
FUKUTOMI, A
KATUNUMA, N
机构：
[1] Division of Enzyme Chemistry, Institute for Enzyme Research, The University of Tokushima, Tokushima
来源：
FEBS LETTERS | 1991年 / 286卷 / 1-2期
关键词：
AIDS; HIV-1; GP120; V3; DOMAIN; SERINE ESTERASE; BINDING PROTEIN;
D O I：
10.1016/0014-5793(91)80981-8
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
A novel membrane-bound serine esterase in cultured human T4+ lymphocytes, recently purified and named tryptase TL2, binds specifically to the external envelope protein gp120 of HIV-1, interacting with its V3 domain. This binding was selectively blocked by inhibitors of tryptase TL2 with a GPCR sequence in their reactive site, synthetic peptides corresponding with the sequences of the V3 domains of various HIV-1 strains with the GPGR sequence, and antibody against tryptase TL2, or neutralizing antibody against the V3 domain of HTLV-III(B). These findings suggest that tryptase TL2 is a binding protein of the V3 domain of HIV-1 envelope glycoprotein.
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页码：233 / 236
页数：4
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