NMR mapping of the antigenic determinant recognized by an anti-gp120, human immunodeficiency virus neutralizing antibody.
NMR mapping of the antigenic determinant recognized by an anti-gp120, human immunodeficiency virus neutralizing antibody.
复制标题
抗 gp120（人类免疫缺陷病毒中和抗体）识别的抗原决定簇的 NMR 图谱。
DOI：
10.1111/j.1432-1033.1995.0178l.x
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发表时间：
1995
期刊：
影响因子：
--
通讯作者：
J. Anglister
中科院分区：
文献类型：
--
作者：
A. Zvi;I. Kustanovich;D. Feigelson;R. Levy;M. Eisenstein;S. Matsushita;P. Richalet;M. H. Regenmortel;J. Anglister
24个氨基酸的RP135(NNTRKSIRIQRGPGRAFVTIGKIG)在氨基酸序列上与人类免疫缺陷病毒1型IIIB分离株(HIV-1IIIB，包膜糖蛋白gp120的308-331残基)的主要中和决定簇相对应。为了定位0.5β识别的抗原决定簇，用二维核磁共振波谱研究了RP135与抗gp120 HIV中和抗体0.5β的相互作用。利用同核Hartmann Hahn二维实验和在水中测量的Fab/肽复合体的旋转框架Overhauser增强光谱相结合的方法，消除了Fab和紧密结合的多肽残基的共振，并对结合时保持相当流动性的多肽部分进行了顺序指定。以这种方式，共有14个残基(Ser6-Thr19)被证明是抗体0.5β识别的抗原决定簇的一部分。发现Lys5和Ile20在结合的多肽中保持了相当大的流动性，而它们的酰胺质子在结合时发生了显著的化学位移变化。这一观察表明，这两个残基位于抗体识别的决定簇的边界上。使用截短肽的竞争结合实验有力地支持了核磁共振的观察结果。
The 24-amino-acid peptide RP135 (NNTRKSIRIQRGPGRAFVTIGKIG) corresponds in its amino acid sequence to the principal neutralizing determinant of the human immunodeficiency virus type-1, IIIB isolate (HIV-1IIIB, residues 308-331 of the envelope glycoprotein gp120). In order to map the antigenic determinant recognized by 0.5 beta, the complex of RP135 with an anti-gp120 HIV neutralizing antibody, 0.5 beta, which cross reacts with the peptide, was studied by using two-dimensional NMR spectroscopy. A combination of homonuclear Hartmann Hahn two-dimensional experiment and roating-frame Overhauser enhancement spectroscopy of the Fab/peptide complex measured in H2O was used to eliminate the resonances of the Fab and the tightly bound peptide residues and to obtain sequential assignments for those parts of the peptide which retain considerable mobility upon binding. In this manner, a total of 14 residues (Ser6-Thr19) were shown to be part of the antigenic determinant recognized by the antibody 0.5 beta. Lys5 and Ile20 were found to retain considerable mobility in the bound peptide while their amide protons undergo significant change in chemical shift upon binding. This observation suggests that these two residues are at the boundaries of the determinant recognized by the antibody. Competitive binding experiments using truncated peptides strongly support the NMR observations.
影响因子：
56.9
作者：
RINI, JM;SCHULZEGAHMEN, U;WILSON, IA
通讯作者：
WILSON, IA
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
影响因子：
56.9
作者：
STANFIELD, RL;FIESER, TM;WILSON, IA
通讯作者：
WILSON, IA