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Updated: Nov 23, 2025

A Method to Assess Fc-mediated Effector Functions Induced by Influenza Hemagglutinin Specific Antibodies

A Method to Assess Fc-mediated Effector Functions Induced by Influenza Hemagglutinin Specific Antibodies

Published on: February 23, 2018

Hierarchical Multivalent Effects Control Influenza Host Specificity.

Nico J Overeem¹, P H Erik Hamming¹, Oliver C Grant²

¹Molecular Nanofabrication Group, MESA+ Institute for Nanotechnology, Faculty of Science and Technology, University of Twente, P.O. Box 217, 7500 AE Enschede, The Netherlands.

ACS Central Science

|December 30, 2020

Summary

This summary is machine-generated.

Influenza viruses bind host cells through hemagglutinin (HA) proteins interacting with cell surface glycans. Receptor density, length, and type determine virus binding strength (avidity) and host specificity, impacting zoonotic potential.

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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

Area of Science:

Virology
Biophysics
Glycobiology

Background:

Influenza virus entry into host cells is mediated by hemagglutinin (HA) proteins binding to sialic acid-terminated glycans.
Multivalent interactions between viral HA and host cell receptors influence virus selectivity, pathogenicity, and transmissibility.
Understanding these interactions is crucial for assessing the zoonotic potential of emerging influenza strains.

Purpose of the Study:

To investigate how intrinsic differences in avian- and human-type receptor interactions with influenza HA affect virus avidity and specificity.
To determine the role of receptor length and density in modulating influenza virus binding to host cells.
To establish a method for measuring virus avidity based on receptor density gradients.

Main Methods:

Development of a novel method to measure virus avidity using receptor density gradients.
Characterization of individual receptor-ligand interactions between influenza HA and both avian- and human-type receptors.
Analysis of how receptor length and density influence the overall avidity and specificity of influenza viruses.

Main Results:

Influenza virus avidity and specificity are determined by a combination of sialic acid linkage, receptor length, and receptor density.
Stable virus attachment requires a minimum of approximately 8 HA-glycan interactions.
Shorter, human-type receptors necessitate more HA-glycan interactions for stable binding compared to avian-type receptors.

Conclusions:

Threshold receptor densities play a critical role in determining virus tropism.
Receptor characteristics significantly influence influenza virus virulence and zoonotic potential.
Findings provide insights into the molecular mechanisms underlying influenza virus host adaptation and emergence.