Burton D R, Pyati J, Koduri R, Sharp S J, Thornton G B, Parren P W, Sawyer L S, Hendry R M, Dunlop N, Nara P L
Department of Immunology, Scripps Research Institute, La Jolla, CA 92037.
Science. 1994 Nov 11;266(5187):1024-7. doi: 10.1126/science.7973652.
The ability of antibodies to neutralize diverse primary isolates of human immunodeficiency virus-type 1 in vitro has been questioned, with implications for the likely efficacy of vaccines. A recombinant human antibody to envelope glycoprotein gp120 was generated and used to show that primary isolates are not refractory to antibody neutralization. The recombinant antibody neutralized more than 75 percent of the primary isolates tested at concentrations that could be achieved by passive immunization, for example, to interrupt maternal-fetal transmission of virus. The broad specificity and efficacy of the antibody implies the conservation of a structural feature on gp120, which could be important in vaccine design.
抗体在体外中和多种人类免疫缺陷病毒1型原始分离株的能力受到质疑,这对疫苗可能的疗效产生了影响。一种针对包膜糖蛋白gp120的重组人抗体被制备出来,并用于证明原始分离株对抗体中和并非具有抗性。该重组抗体在通过被动免疫可达到的浓度下,中和了超过75%的所测试的原始分离株,例如,用于阻断病毒的母婴传播。该抗体的广泛特异性和有效性意味着gp120上存在一种保守的结构特征,这在疫苗设计中可能很重要。