HIV ENV GLYCOPROTEIN SHARES A CROSS-REACTING EPITOPE WITH A SURFACE PROTEIN PRESENT ON ACTIVATED HUMAN-MONOCYTES AND INVOLVED IN ANTIGEN PRESENTATION

HIV ENV GLYCOPROTEIN SHARES A CROSS-REACTING EPITOPE WITH A SURFACE PROTEIN PRESENT ON ACTIVATED HUMAN-MONOCYTES AND INVOLVED IN ANTIGEN PRESENTATION
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DOI:
10.1002/eji.1830171218
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发表时间:
1987-12-01
影响因子:
5.4
通讯作者:
SICCARDI, AG
SICCARDI, AG
中科院分区:
医学3区
文献类型:
--
作者:
BERETTA, A;GRASSI, F;SICCARDI, AG

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人类免疫缺陷病毒(HIV)的env gp120糖蛋白与人类细胞表面蛋白之间的血清学交叉反应性已被一种针对HIV的单克隆抗体(M38)确定。细胞抗原是一种约80 kDa的蛋白,在外周血和淋巴结的一小部分单核细胞中表达。该蛋白表现为单核细胞谱系的激活抗原,因为它在塑料粘附培养条件下由单核细胞和干扰素- γ表达。单核细胞和前单核细胞U937。该蛋白参与抗原呈递,因为该抗体在自体破伤风类毒素呈递试验中有效抑制反应性淋巴细胞的增殖。在T淋巴母细胞样细胞系H9中,该蛋白以极少量存在,不受干扰素- γ诱导。在感染艾滋病毒后会增加。淋巴腺病综合征和获得性免疫缺陷综合征(艾滋病)患者的血清虽然含有与gp120反应的抗体,但无法检测到细胞蛋白。我们提出单克隆抗体(mAb)识别的病毒和细胞结构都参与了与T辅助淋巴细胞CD4分子的相互作用,这种分子模仿可能与HIV感染的病理有关。这一观点得到了以下发现的支持:一种CD4特异性单抗BL/10T4与M38结合,从而中和其与HIV和单核细胞的相互作用,mAb M38因此充当CD4的内部图像。这个单一的性质可以解释它所有不同的结合特性。
A serological cross-reactivity between env gp120 glycoprotein of the human immunodeficiency virus (HIV) and a human cellular surface protein has been defined by a monoclonal antibody (M38) raised against HIV. The cellular antigen is a protein of ca. 80 kDa expressed on a small fraction of mononuclear cells in peripheral blood and in lymph nodes. The protein behaves as an activation antigen of the monocytic lineage since it is expressed by monocytes in plastic-adherent culture conditions and by interferon-.gamma.-treated monocytes and pro-monocytic U937 cells. The protein is involved in antigen presentation since the antibody efficiently inhibits the proliferation of responsive lymphocytes in autologous tetanus toxoid presentation assays. In the T lymphoblastoid line H9, the protein is present in very small amounts, is not induced by interferon-.gamma. and increases after HIV infection. Sera from lymphoadenopathy syndrome and acquired immunodeficiency syndrome (AIDS) patients fail to detect the cellular protein, although containing antibodies reacting with gp120. We propose that both viral and cellular structures recognized by the monoclonal antibody (mAb) are involved in interactions with CD4 molecules of T helper lymphocytes and that such molecular mimicry might be relevant in the pathology of HIV infection. This view is supported by the finding that BL/10T4, a CD4-specific mAb, binds to M38 neutralizing its interactions with HIV and with monocytes, mAb M38 thus behaves as the internal image of CD4. This single property would explain all its diverse binding characteristics.