Hemagglutinin Binding
Hemagglutinin Binding - Related Videos
12:18
Expression of Functional Recombinant Hemagglutinin and Neuraminidase Proteins from the Novel H7N9 Influenza Virus Using the Baculovirus Expression System
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Cited by 182 •
2013
Here we describe a way to express correctly folded and functional influenza virus surface antigens derived from the novel Chinese H7N9 virus in insect cells. The technique can be adapted to express ectodomains of any viral or cellular surface proteins.
10:32
A Miniaturized Glycan Microarray Assay for Assessing Avidity and Specificity of Influenza A Virus Hemagglutinins
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Cited by 9 •
2016
Using a printed glycan microarray strategy, a conventional 96-well plate assay was miniaturized for analysis of influenza A virus hemagglutinin avidity and specificity for sialic acid containing receptors.
08:19
Subnanometer-Resolution Structural Determination of Hemagglutinin from Cryo-Electron Tomography of Influenza Viruses
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Cited by 1 •
2025
This article presents a protocol for data processing of influenza viruses imaged using cryo-electron tomography and subsequent subtomogram averaging of the hemagglutinin glycoprotein. This protocol covers step-by-step data processing, from image preprocessing to final model refinement.
04:47
A Method to Assess Fc-mediated Effector Functions Induced by Influenza Hemagglutinin Specific Antibodies
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Cited by 6 •
2018
We describe a method to measure the activation of Fc-mediated effector functions by antibodies that target the influenza virus hemagglutinin. This assay can also be adapted to assess the ability of monoclonal antibodies or polyclonal sera targeting other viral surface glycoproteins to induce Fc-mediated immunity.
02:18
The Equilibrium Binding Constant and Binding Strength
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2020
The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at equilibrium: where P and L are the unbound protein and ligand, respectively, and PL is the protein-ligand complex. As the amount of bound ligand is also related to the rate of ligand binding, experiments can also determine Kb by examining the rates of protein-ligand association (kon) and dissociation (koff) using the following ratio: Thus,...
FAQs
The linkage connecting sialic acid to the underlying glycan helps determine which host-cell receptors an influenza hemagglutinin can recognize. Viruses with different preferences may attach more efficiently to cells displaying α2,3-linked or α2,6-linked forms. This receptor selectivity contributes to tissue tropism, meaning the types of host tissues that a viral strain can target during infection.
Receptor preference provides a molecular link between hemagglutinin binding and the cells a virus can engage. When mutations change recognition of α2,3- or α2,6-linked sialic acids, the affected strain may show altered host range or transmission potential. Measuring these binding changes therefore helps researchers evaluate biologically important differences among influenza viruses without relying only on genetic comparisons.
A mutation in hemagglutinin may modify how strongly or selectively the protein recognizes host-cell receptor structures. Such a change can shift receptor preference and, consequently, influence tissue tropism, host range, or transmission-related properties. Binding studies are valuable because they connect molecular changes in a viral protein with altered interaction patterns that may have consequences for influenza biology.
Laboratory binding assays provide a way to characterize how different influenza strains interact with receptor structures containing α2,3- or α2,6-linked sialic acids. Researchers can use the resulting binding patterns to identify differences in receptor preference and to monitor changes associated with viral mutations. These comparisons support interpretation of strain-specific attachment behavior and biological variation.
Surveillance programs can use binding measurements to monitor whether circulating influenza strains retain or develop different receptor preferences. Detecting changes in recognition of α2,3- and α2,6-linked sialic acids can provide evidence of altered host-cell interactions. This information complements strain characterization and helps identify viral changes that may warrant closer evaluation for host range or transmission implications.
Hemagglutinin binding data can inform vaccine development by describing receptor-recognition properties that distinguish viral strains. The same information can support evaluation of antiviral strategies designed to disrupt viral attachment or entry. By identifying how a strain engages host-cell glycans, researchers gain a basis for assessing whether an intervention may interfere with an early step in infection.