Schwartz O, Alizon M, Heard J M, Danos O
Département SIDA et Rétrovirus, Institut Pasteur, Paris, France.
Virology. 1994 Jan;198(1):360-5. doi: 10.1006/viro.1994.1042.
A CD4+ human T cell clone (SPB21) or primary blood mononuclear cells were grown in the presence of HeLa cells stably expressing functional human immunodeficiency virus type 1 envelope glycoprotein complexes at their surface. After a short cocultivation, SPB21 cells lost their ability to proliferate in response to T cell receptor (TCR) stimulations and died by apoptosis, whereas interleukin-2 stimulation was still effective. Incubation with soluble monomeric gp120 did not alter TCR responsiveness. A selective decrease in the proportion of CD4+ cells was also observed among primary lymphocytes after cocultivation and OKT3 stimulation. We propose that binding of oligomeric membrane-bound envelope glycoprotein induces a multimerization of CD4 molecules that impairs normal TCR stimulation.
一个CD4 +人类T细胞克隆(SPB21)或原代血液单核细胞在表面稳定表达功能性人类免疫缺陷病毒1型包膜糖蛋白复合物的HeLa细胞存在的情况下培养。短暂共培养后,SPB21细胞失去了对T细胞受体(TCR)刺激作出增殖反应的能力,并通过凋亡死亡,而白细胞介素-2刺激仍然有效。与可溶性单体gp120孵育不会改变TCR反应性。共培养和OKT3刺激后,原代淋巴细胞中CD4 +细胞的比例也出现选择性下降。我们提出,寡聚膜结合包膜糖蛋白的结合会诱导CD4分子多聚化,从而损害正常的TCR刺激。