Second conserved domain of gp120 is important for HIV infectivity and antibody neutralization.
Second conserved domain of gp120 is important for HIV infectivity and antibody neutralization.
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gp120 的第二个保守结构域对于 HIV 感染性和抗体中和很重要。
DOI：
10.1126/science.2830667
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发表时间：
1988
期刊：
影响因子：
--
通讯作者：
Gurney,ME
中科院分区：
文献类型：
--
作者：
Ho,DD;Kaplan,JC;Rackauskas,IE;Gurney,ME
兔抗血清针对与人类免疫缺陷病毒（HIV）的外囊膜糖蛋白（gp 120）的第二个保守结构域具有序列同源性的三个重叠的合成肽。所有的抗血清免疫沉淀包膜糖蛋白。特别是，针对氨基酸254至274 ofenv的抗血清在体外有效中和三种不同的HIV分离株，而不影响病毒与CD4阳性细胞的结合。因此，gp120的这个保守区域在病毒穿透过程中的后结合事件中似乎是至关重要的，并且可能代表HIV抗体中和的靶点。这些发现可能适用于获得性免疫缺陷综合征疫苗的设计。
Rabbit antisera were raised against three overlapping synthetic peptides with sequence homology to the second conserved domain of the external envelope glycoprotein (gp120) of the human immunodeficiency virus (HIV). All of the antisera immunoprecipitated the envelope glycoprotein. In particular, an antiserum directed against amino acids 254 to 274 ofenvwas efficient in neutralizing three different isolates of HIV in vitro, without affecting the binding of the virus to CD4-positive cells. Therefore, this conserved region of gp120 appears to be critical in a postbinding event during virus penetration and may represent a target for antibody neutralization of HIV. These findings may be applicable in the design of a vaccine for the acquired immunodeficiency syndrome.