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本文引用的文献

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The CC-chemokine RANTES increases the attachment of human immunodeficiency virus type 1 to target cells via glycosaminoglycans and also activates a signal transduction pathway that enhances viral infectivity.CC趋化因子RANTES通过糖胺聚糖增加1型人类免疫缺陷病毒与靶细胞的黏附，并且还激活一条增强病毒感染性的信号转导途径。
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Neutralizing antibodies have limited effects on the control of established HIV-1 infection in vivo.中和抗体对体内已建立的HIV-1感染的控制作用有限。
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Epitope mapping of CCR5 reveals multiple conformational states and distinct but overlapping structures involved in chemokine and coreceptor function.CCR5的表位作图揭示了多种构象状态以及参与趋化因子和共受体功能的不同但重叠的结构。
J Biol Chem. 1999 Apr 2;274(14):9617-26. doi: 10.1074/jbc.274.14.9617.
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Human immunodeficiency virus-1 infection requires pertussis toxin sensitive G-protein-coupled signalling and mediates cAMP downregulation.人类免疫缺陷病毒1型感染需要百日咳毒素敏感的G蛋白偶联信号传导，并介导环磷酸腺苷（cAMP）下调。
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Mutations in both gp120 and gp41 are responsible for the broad neutralization resistance of variant human immunodeficiency virus type 1 MN to antibodies directed at V3 and non-V3 epitopes.gp120和gp41中的突变导致了1型变异人类免疫缺陷病毒MN对针对V3和非V3表位的抗体产生广泛的中和抗性。
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1型人类免疫缺陷病毒感染性的抗体介导增强作用由gp120的结构决定，并取决于gp120与CCR5相互作用的调节。

Antibody-mediated enhancement of human immunodeficiency virus type 1 infectivity is determined by the structure of gp120 and depends on modulation of the gp120-CCR5 interaction.

作者信息

Guillon Christophe, Schutten Martin, Boers Patrick H M, Gruters Rob A, Osterhaus Albert D M E

机构信息

Department of Virology, Erasmus University Rotterdam, 3015 GE Rotterdam, The Netherlands.

出版信息

J Virol. 2002 Mar;76(6):2827-34. doi: 10.1128/jvi.76.6.2827-2834.2002.

DOI:10.1128/jvi.76.6.2827-2834.2002
PMID:11861850
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC135957/
Abstract

In this study, we characterized the viral determinants of coreceptor usage in relation to susceptibility to antibody-mediated neutralization or enhancement of infectivity by using chimeras of three highly related human immunodeficiency virus type 1 (HIV-1) isolates of different phenotypes. We found that the V3 region was the main determinant of antibody-mediated enhancement and coreceptor specificity but that the overall structure of gp120 was also important for these properties. Constructs susceptible to antibody-mediated enhancement preferentially use CCR5 as a coreceptor, in contrast to constructs that were neutralized or not affected. Using monoclonal antibodies directed against CD4 or CCR5, we were able to show that antibody-mediated enhancement was CD4 dependent. Altogether, our results suggest that the modulation of the interaction of gp120 with CCR5 is the mechanism underlying antibody-mediated enhancement of HIV-1 infectivity.

摘要

在本研究中，我们通过使用三种不同表型的高度相关的人类免疫缺陷病毒1型（HIV-1）分离株的嵌合体，来确定共受体使用的病毒决定因素与抗体介导的中和作用或感染性增强易感性之间的关系。我们发现，V3区域是抗体介导的增强作用和共受体特异性的主要决定因素，但gp120的整体结构对这些特性也很重要。与被中和或未受影响的构建体相比，易受抗体介导增强作用影响的构建体优先使用CCR5作为共受体。使用针对CD4或CCR5的单克隆抗体，我们能够证明抗体介导的增强作用是CD4依赖性的。总之，我们的结果表明，gp120与CCR5相互作用的调节是抗体介导HIV-1感染性增强的潜在机制。