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相关概念视频

Inhibitors Of Virion Release01:25

Inhibitors Of Virion Release

Viral replication and dissemination rely on efficient mechanisms for host cell entry, genome replication, assembly, and release. Influenza viruses, such as types A and B, are negative-sense single-stranded RNA viruses with a segmented genome, that depend on two critical surface glycoproteins to carry out these processes: hemagglutinin (HA) and neuraminidase (NA). HA initiates infection by binding to sialic acid residues on the surface of host epithelial cells, facilitating receptor-mediated...
Antiviral Nucleoside Inhibitors01:22

Antiviral Nucleoside Inhibitors

Antiviral Nucleoside InhibitorsAntiviral nucleoside inhibitors are structural analogs of natural nucleosides that interfere with viral DNA or RNA synthesis. These compounds selectively target viral polymerases due to their resemblance to host nucleosides, thereby disrupting viral genome replication.Mechanism of Acyclovir ActionAcyclovir is a guanosine analog with a three-carbon acyclic side chain. It selectively targets herpes simplex virus type 1 (HSV-1), herpes simplex virus type 2 (HSV-2),...
Inhibitors of Virion Maturation and Assembly01:19

Inhibitors of Virion Maturation and Assembly

As part of their replication cycle, certain viruses synthesize long precursor proteins called polyproteins within infected host cells. In human immunodeficiency virus (HIV), two major polyproteins are produced: Gag and Gag-Pol. The Gag polyprotein supplies the structural components of the virus, while Gag-Pol includes essential viral enzymes such as reverse transcriptase, integrase, and protease. After synthesis, these polyproteins move to the host cell membrane, where they assemble into an...

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Solution structure of a cyanovirin-N:Man alpha 1-2Man alpha complex: structural basis for high-affinity carbohydrate-mediated binding to gp120.

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相关实验视频

Updated: Jun 21, 2026

Conformational Evaluation of HIV-1 Trimeric Envelope Glycoproteins Using a Cell-based ELISA Assay
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Published on: September 14, 2014

强效的抗艾滋病毒蛋白质cyanovirin-N含有两个新型碳水化合物结合点,可选择性地与Man ((8) D1D3和Man ((9) 结合,具有纳米分子亲和力:对结合HIV包膜蛋白 gp120的影响.

C A Bewley1, S Otero-Quintero

  • 1Laboratory of Bioorganic Chemistry, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0820, USA.

Journal of the American Chemical Society
|July 18, 2001
PubMed
概括
此摘要是机器生成的。

诺维林-N (CVN) 蛋白在HIV的gp120上与特定的N相关碳水化合物结合,解释了其阻断融合的活性. 这种蛋白质可以识别具有纳米分子亲和力的Man{9) GlcNAc{2) 和Man{8) GlcNAc{2).

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科学领域:

  • 生物化学 生物化学
  • 病毒学 病毒学
  • 结构生物学 结构生物学

背景情况:

  • 诺维林-N (CVN) 是一种来自菌的蛋白质,具有强大的抗人类免疫缺陷病毒 (HIV) 活性.
  • 通过干扰细胞融合,CVN主要通过与病毒包膜糖蛋白gp120的相互作用来抑制HIV.
  • 有证据表明,gp120上的N相关碳水化合物在CVN-gp120相互作用中起作用,但缺乏直接的实验证据.

研究的目的:

  • 实验验证N链碳水化合物在CVN与HIV相互作用中的作用 gp120.
  • 通过CVN识别特定的碳水化合物结构并确定结合亲和关系.
  • 为了阐明CVN与gp120碳水化合物相互作用的结合史泰基几何学和机制.

主要方法:

  • 使用定量HIV-1包介导细胞融合试验,选一组N链碳水化合物.
  • 使用异热定位热度计 (ITC) 来确认结合亲和度,并确定固体计.
  • 核磁共振 (NMR) 光谱法被用来绘制CVN上的碳水化合物结合部位.

主要成果:

  • CVN 特别结合Man ((9) GlcNAc ((2) 和Man ((8) GlcNAc ((2) 的 D1D3 异构体,具有纳米分子亲和力.
  • 结合gp120显示平衡关联常数 (K(a)) 是2.4 x 10(7) M(-1) 的,随着每gp120.2 CVN的固态度.
  • ITC和NMR显示,CVN具有不同的高和低亲和结合点,识别了Manalpha1 --> 2Manalpha结构.

结论:

  • 通过在gp120上对寡甘N结合碳水化合物的特定识别,CVN具有强大的HIV-1融合抑制活性.
  • 蛋白质表现出具有不同亲和力的双结位点,使其能够识别特定的碳水化合物和潜在的交叉链接.
  • 了解这些相互作用,可以了解CVN抗病毒作用的机制以及潜在的治疗策略.