The fusion domain of HIV gp41 interacts specifically with heparan sulfate on the T-lymphocyte cell surface
The fusion domain of HIV gp41 interacts specifically with heparan sulfate on the T-lymphocyte cell surface
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DOI：
10.1093/emboj/20.1.19
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发表时间：
2001-01-15
期刊：
影响因子：
11.4
通讯作者：
O'Shea, P
中科院分区：
文献类型：
--
作者：
Cladera, J;Martin, I;O'Shea, P
本文报道了人免疫缺陷病毒糖蛋白gp 41（FD）的16个氨基酸的融合肽结构域（gp 41（FD））与T淋巴细胞相互作用的研究结果。用荧光法测定了gp 41（FD）与T淋巴细胞相互作用后细胞膜表面静电势和偶极电位的变化，结果表明gp 41（FD）与细胞表面硫酸乙酰肝素相互作用。这种相互作用被白细胞介素-8阻断，并通过用肝素酶预处理细胞来消除。还通过观察到可溶性硫酸乙酰肝素与细胞膜相互作用竞争，而可溶性肝素（在所用水平）不竞争，评估了反应的特异性。在与硫酸乙酰肝素结合后，与膜的相互作用似乎以与gp 41（FD）三聚体的形成协同的方式发生。然而，在更简单的磷脂膜中，三聚体复合物似乎不是主要的相互作用模式。最后，通过在成像方案内重复这些研究中的一些，看来gp 41（FD）-T细胞相互作用发生在细胞表面上的特定区域内，以类似地定位硫酸乙酰肝素部分。
Studies of the interaction of the 16 residue fusion peptide domain of human immunodeficiency virus glycoprotein gp41 (gp41(FD)) with T lymphocytes are outlined, Fluorescence measurements of changes in the electrostatic surface and dipole potentials of the plasma membrane following the interaction with gp41(FD) are described, The results show that gp41(FD) interacts with heparan sulfate located on the cell surface. This interaction is blocked by interleukin-8 and abolished by pre-treating the cells with heparitinase. The specificity of the reaction was also assessed by observations that soluble heparan sulfate competes with the cell membrane interaction whereas soluble heparin (at the levels utilized) does not. Following binding to heparan sulfate, the interaction with the membrane seems to take place in a cooperative manner with the formation of gp41(FD) trimers, In simpler phospholipid membranes, however, a trimeric complex does not appear to be the dominant mode of interaction, Finally, by repeating some of these studies within an imaging regime, it appears that the gp41(FD)-T-cell interaction takes place within specific domains on the cell surface to similarly localized heparan sulfate moieties.