Kido H, Fukutomi A, Katunuma N
Institute for Enzyme Research, University of Tokushima, Japan.
FEBS Lett. 1991 Jul 29;286(1-2):233-6. doi: 10.1016/0014-5793(91)80981-8.
A novel membrane-bound serine esterase in cultured human T4+ lymphocytes, recently purified and named tryptase TL2, binds specifically to the external envelope protein gp 120 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-IIIB. These findings suggest that tryptase TL2 is a binding protein of the V3 domain of HIV-1 envelope glycoprotein.
一种新的膜结合丝氨酸酯酶，最近在培养的人T4 +淋巴细胞中被纯化并命名为类胰蛋白酶TL2，它能特异性结合HIV-1的外膜蛋白gp120，并与其V3结构域相互作用。这种结合可被活性位点具有GPCR序列的类胰蛋白酶TL2抑制剂、与各种具有GPGR序列的HIV-1毒株V3结构域序列相对应的合成肽、抗类胰蛋白酶TL2抗体或抗HTLV-IIIB V3结构域的中和抗体选择性阻断。这些发现表明，类胰蛋白酶TL2是HIV-1包膜糖蛋白V3结构域的结合蛋白。
