Resistance of human immunodeficiency virus type 1 to neutralization by natural antisera occurs through single amino acid substitutions that cause changes in antibody binding at multiple sites
Resistance of human immunodeficiency virus type 1 to neutralization by natural antisera occurs through single amino acid substitutions that cause changes in antibody binding at multiple sites
复制标题
1 型人类免疫缺陷病毒对天然抗血清中和的抵抗力是通过单个氨基酸取代而发生的，这种取代会导致多个位点的抗体结合发生变化
DOI：
10.1128/jvi.70.12.8431-8437.1996
复制
发表时间：
1996
影响因子：
5.4
通讯作者：
M. Robert
中科院分区：
文献类型：
--
作者：
B. Watkins;S. Buge;K. Aldrich;A. Davis;James A. Robinson;Marvin S. Reitz;M. Robert
The ability of human immunodeficiency virus type 1 (HIV-1) to replicate in the presence of strong immune responses to the virus may be due to its high mutation rate, which provides envelope gene variability for selection of neutralization-resistant variants. Understanding neutralization escape mechanisms is therefore important for the design of HIV-1 vaccines and our understanding of the disease process. In this report, we analyze mutations at amino acid positions 281 and 582 in the HIV-1 envelope, where substitutions confer resistance to broadly reactive neutralizing antisera from seropositive individuals. Neither of these mutations lies within an antibody-binding site, and therefore the mechanism of immune escape in both cases is by alteration of the shape of the envelope proteins. The conformation of the CD4-binding site is shown to be critical with regard to presentation of other discontinuous epitopes. From our analysis of the neutralization of these variants, we conclude that escape from polyclonal sera occurs through alterations at several different epitopes, generally resulting from single amino acid substitutions which influence envelope conformation. Experiments on a double mutant showed that the combination of both mutations is not additive, suggesting that these variants utilized alternate pathways to elicit similar alterations of the HIV-1 envelope structure.
登录
查看更多内容
从受感染的实验室工作人员身上分离出的 HIV-1 V3 环中的自发点突变导致中和表位丢失。
DOI：
--
发表时间：
1993
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
diMarzoVeronese,F;ReitzJr,MS;Gupta,G;Robert-Guroff,M;Boyer-Thompson,C;Louie,A;Gallo,RC;Lusso,P
通讯作者：
Lusso,P
DOI：
10.1073/pnas.85.9.3198
发表时间：
1988-05
影响因子：
11.1
作者：
James R. Rusche;K. Javaherian;Charlene MCDANALt;J. Petro;Debra L. Lynn;R. Grimaila;Alphonse J. LANGLOISt;Robert C. Gallo;P. Fischinger;Dani P. BOLOGNESIt;SCOTr D. Putney;Thomas J. MATTHEWSt
通讯作者：
James R. Rusche;K. Javaherian;Charlene MCDANALt;J. Petro;Debra L. Lynn;R. Grimaila;Alphonse J. LANGLOISt;Robert C. Gallo;P. Fischinger;Dani P. BOLOGNESIt;SCOTr D. Putney;Thomas J. MATTHEWSt
gp120 的第二个保守结构域对于 HIV 感染性和抗体中和很重要。
DOI：
10.1126/science.2830667
发表时间：
1988
期刊：
Science (New York, N.Y.)
影响因子：
--
作者：
Ho,DD;Kaplan,JC;Rackauskas,IE;Gurney,ME
通讯作者：
Gurney,ME
一种 IgG 人单克隆抗体，可与 HIV-1/GP120 发生反应，抑制病毒与细胞结合并中和感染。
DOI：
--
发表时间：
1991
期刊：
Journal of immunology (Baltimore, Md. : 1950)
影响因子：
--
作者：
Posner,MR;Hideshima,T;Cannon,T;Mukherjee,M;Mayer,KH;Byrn,RA
通讯作者：
Byrn,RA
针对 HIV-1 外部糖蛋白的中和单克隆抗体的表征。
影响因子：
4.6
作者：
Pal,R;diMarzoVeronese,F;Nair,BC;Rahman,R;Hoke,G;Mumbauer,SW;Sarngadharan,MG
通讯作者：
Sarngadharan,MG