相关实验视频

Updated: Jul 20, 2025

A Miniaturized Glycan Microarray Assay for Assessing Avidity and Specificity of Influenza A Virus Hemagglutinins

A Miniaturized Glycan Microarray Assay for Assessing Avidity and Specificity of Influenza A Virus Hemagglutinins

Published on: May 29, 2016

主体细胞表面甘氨酸结构对细胞的相关性流感A病毒的特异性

Markus Kastner¹, Andreas Karner¹, Rong Zhu¹

¹Institute for Biophysics, Johannes Kepler University Linz, 4020 Linz, Austria.

|July 29, 2023

概括

流感A病毒 (IAV) 血凝素结合偏好并不总是预测病毒细胞特异性. 单病毒力光谱为研究病毒如何附着于活细胞提供了一种新的方法.

科学领域:

病毒学病毒学
葡萄糖生物学葡萄糖生物学
生物物理学的生物物理.

背景情况:

流感A型病毒 (IAVs) 使用血氨酸 (HA) 结合化甘氨酸进入细胞.
虽然已知HA对单个甘氨酸的特异性,但其与复杂的细胞表面甘氨酸结合的作用尚不清楚.
了解病毒细胞粘附对于开发有效的抗病毒策略至关重要.

研究的目的:

为了比较由HA与单个甘氨酸结合而不是与活宿主细胞结合决定的流感病毒受体特异性.
为了研究宿主细胞葡萄糖对流感病毒粘附的贡献.
评估单个病毒力光谱 (SVFS) 作为一种研究复杂细胞环境中的病毒细胞结合的方法.

主要方法:

利用糖甘阵列来评估流感病毒血质素 (HA) 与特定的化糖甘的结合偏好.
采用单个病毒力光谱 (SVFS) 来测量病毒与活宿主细胞的结合.
从甘氨基阵列和SVFS进行比较的结果来确定病毒细胞特异性.

主要成果:

根据HA与单个甘氨酸的结合来确定流感病毒受体的特异性,并没有一致预测病毒与细胞的结合特异性.
甘氨酸阵列显示了一个结合偏好,而SVFS显示了活细胞上不同的结合特性.
这突出了复杂的细胞甘油对病毒粘附的影响.

结论:

主体细胞的异质葡萄糖显著影响流感病毒的结合,独立于HA的内在受体偏好.
单病毒力光谱 (SVFS) 是准确评估流感病毒与活细胞结合的宝贵工具.
在原生细胞化受体环境的背景下,SVFS可以阐明病毒细胞结合偏好.

关键词:

细胞结合结合的细胞.强力光谱法强力光谱法流感A型病毒感染者

更多相关视频

Engineering Antiviral Agents via Surface Plasmon Resonance

Engineering Antiviral Agents via Surface Plasmon Resonance

Published on: June 14, 2022

Measuring Attachment and Internalization of Influenza A Virus in A549 Cells by Flow Cytometry

Measuring Attachment and Internalization of Influenza A Virus in A549 Cells by Flow Cytometry

Published on: November 4, 2015

相关概念视频

Glycocalyx and its Functions

Glycocalyx and its Functions

The glycocalyx is a carbohydrate-rich, fuzzy-appearing layer on the outer surface of the cell membrane. It is highly hydrophilic, because of this it attracts large amounts of water to the cell's surface. This aids the cell's interaction with the watery environment and also helps it to obtain substances dissolved in the water. It is also important for cell identification, self/non-self determination, and embryonic development and is used in cell-to-cell attachments to form tissues.

Viral Structure

Viral Structure

Viruses are extraordinarily diverse in shape and size, but they all have several structural features in common. All viruses have a core that contains a DNA- or RNA-based genome. The core is surrounded by a protective coat of proteins called the capsid. The capsid is composed of subunits called capsomeres. The capsid and genome-containing core are together known as the nucleocapsid.

Leaky Scanning

Leaky Scanning

During most eukaryotic translation processes, the small 40S ribosome subunit scans an mRNA from its 5' end until it encounters the first start AUG codon. The large 60S ribosomal subunit then joins the smaller one to initiate protein synthesis. The location of the translation initiation is largely determined by the nucleotides near the start codon as there may be multiple translation initiation sites present on the mRNA. Marilyn Kozak discovered that the sequence RCCAUGG (where R...

Membrane Carbohydrates

Membrane Carbohydrates

The plasma membrane is a dynamic barrier composed of lipids, proteins, and carbohydrates. It is the epicenter of many cellular processes required for cell growth and survival. Carbohydrates have unique structural and chemical properties that help the plasma membrane to carry out its functions effectively.
Membrane carbohydrates do not have any hydrophobic region and are exclusively located on the cell's outer surface. The addition of sugar molecules or glycosylation of proteins happens in...

Oligosaccharide Assembly

Oligosaccharide Assembly

Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...

Protein Glycosylation

Protein Glycosylation

Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
Glycosylation occurs in...