AFM force measurements of the gp120-sCD4 and gp120 or CD4 antigen-antibody interactions

被引:18
作者
Chen, Yong [1 ,2 ]
Zeng, Gucheng [2 ]
Chen, Sherry Shiyi [3 ]
Feng, Qian [2 ]
Chen, Zheng Wei [2 ]
机构
[1] Nanchang Univ, Inst Adv Study, Nanchang 330031, Jiangxi, Peoples R China
[2] Univ Illinois, Dept Microbiol & Immunol, Chicago, IL 60612 USA
[3] Duke Univ, Dept Biomed Engn, Durham, NC 27708 USA
基金
美国国家卫生研究院; 中国国家自然科学基金;
关键词
Atomic force microscopy (AFM); Human immunodeficiency virus (HIV); Entry inhibitor; Soluble CD4 (sCD4); gp120; Neutralizing antibody; HUMAN-IMMUNODEFICIENCY-VIRUS; RECOMBINANT SOLUBLE CD4; HIV; SPECTROSCOPY; MICROSCOPY; TYPE-1; CELLS; COMPLEXES; MOLECULES; INFECTION;
D O I
10.1016/j.bbrc.2011.03.006
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
070307 [化学生物学]; 071010 [生物化学与分子生物学];
摘要
Soluble CD4 (sCD4), anti-CD4 antibody, and anti-gp120 antibody have long been regarded as entry inhibitors in human immunodeficiency virus (HIV) therapy. However, the interactions between these HIV entry inhibitors and corresponding target molecules are still poorly understood. In this study, atomic force microscopy (AFM) was utilized to investigate the interaction forces among them. We found that the unbinding forces of sCD4-gp120 interaction, CD4 antigen-antibody interaction, and gp120 antigen-antibody interaction were 25.45 +/- 20.46, 51.22 +/- 34.64, and 89.87 +/- 44.63 pN, respectively, which may provide important mechanical information for understanding the effects of viral entry inhibitors on HIV infection. Moreover, we found that the functionalization of an interaction pair on AFM tip or substrate significantly influenced the results, implying that we must perform AFM force measurement and analyze the data with more caution. (C) 2011 Elsevier Inc. All rights reserved.
引用
收藏
页码:301 / 306
页数:6
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