Neurath A R, Strick N, Fields R, Jiang S
Lindsley F. Kimball Research Institute, New York Blood Center, New York 10021.
AIDS Res Hum Retroviruses. 1991 Aug;7(8):657-62. doi: 10.1089/aid.1991.7.657.
The positions of all 9 intrachain disulfide bonds within the envelope glycoprotein gp120 of the human immunodeficiency virus (HIV-1) have been established recently. Peptides expected to mimic some of the disulfide-bonded domains [(120-133)-(203-221); (133-138)-(164-203); (224-254); (391-425) and (385-392)-(425-452)] were synthesized. All peptides, except (120-133)-(203-221), elicited in immunized rabbits relatively high levels of antibodies reacting with gp120 in enzyme-linked immunosorbent assay (ELISA) and/or Western immunoblot assays. However, these antibodies failed to neutralize the infectivity of HIV-1. Combined with earlier reports concerning other gp120 loop peptides, these results confirm the uniqueness of the V3 (303-338) loop in encompassing a principal determinant(s) involved in virus neutralization.
人类免疫缺陷病毒（HIV-1）包膜糖蛋白gp120内所有9个链内二硫键的位置最近已确定。合成了预期模拟某些二硫键结合结构域[（120 - 133）-（203 - 221）；（133 - 138）-（164 - 203）；（224 - 254）；（391 - 425）和（385 - 392）-（425 - 452）]的肽。除了（120 - 133）-（203 - 221）之外，所有肽在免疫的兔子中均引发了相对高水平的抗体，这些抗体在酶联免疫吸附测定（ELISA）和/或Western免疫印迹测定中与gp120发生反应。然而，这些抗体未能中和HIV-1的感染性。结合有关其他gp120环肽的早期报告，这些结果证实了V3（303 - 338）环在包含参与病毒中和的主要决定簇方面的独特性。
