Hansen J E, Clausen H, Nielsen C, Teglbjaerg L S, Hansen L L, Nielsen C M, Dabelsteen E, Mathiesen L, Hakomori S I, Nielsen J O
Department of Infectious Diseases, Hvidovre Hospital, Denmark.
J Virol. 1990 Jun;64(6):2833-40. doi: 10.1128/JVI.64.6.2833-2840.1990.
Carbohydrate structures are often involved in the initial adhesion of pathogens to target cells. In the present study, a panel of anticarbohydrate monoclonal antibodies (MAbs) was tested for their ability to inhibit in vitro human immunodeficiency virus infectivity. MAbs against three different N- and O-linked carbohydrate epitopes (LeY, A1, and sialyl-Tn) were able to block infection by cell-free virus as well as inhibit syncytium formation. Inhibition of virus infectivity was independent of virus strain (HTLVIIIB or patient isolate SSI-002), the cell line used for virus propagation (H9 or MT4), and the cell type used as the infection target (MT4, PMC, or selected T4 lymphocytes). Inhibition was observed when viruses were preincubated with MAbs but not when cells were preincubated with MAbs before inoculation, and the MAbs were shown to precipitate 125I-labeled gp120. The MAbs therefore define carbohydrate structures expressed by the viral envelope glycoprotein gp120, indicating that glycans of the viral envelope are possible targets for immunotherapy or vaccine development or both.
碳水化合物结构常常参与病原体与靶细胞的初始黏附过程。在本研究中，对一组抗碳水化合物单克隆抗体（MAb）抑制体外人类免疫缺陷病毒感染性的能力进行了测试。针对三种不同的N-和O-连接碳水化合物表位（LeY、A1和唾液酸化-Tn）的单克隆抗体能够阻断无细胞病毒的感染，并抑制合胞体形成。病毒感染性的抑制与病毒株（HTLVIIIB或患者分离株SSI-002）、用于病毒增殖的细胞系（H9或MT4）以及用作感染靶标的细胞类型（MT4、PMC或选定的T4淋巴细胞）无关。当病毒与单克隆抗体预孵育时观察到抑制作用，但在接种前细胞与单克隆抗体预孵育时未观察到抑制作用，并且这些单克隆抗体被证明能沉淀125I标记的gp120。因此，这些单克隆抗体确定了病毒包膜糖蛋白gp120所表达的碳水化合物结构，表明病毒包膜聚糖可能是免疫治疗或疫苗开发或两者的靶点。
