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Related Concept Videos

Influenza01:27

Influenza

Influenza is an acute, highly communicable viral disease that affects the respiratory tract and is responsible for seasonal epidemics worldwide. Influenza A is the most prevalent type associated with widespread outbreaks and is subtyped based on two surface glycoproteins: hemagglutinin (H) and neuraminidase (N), as in H1N1. These glycoproteins are essential for viral infectivity, transmission, and immune recognition. Transmission occurs primarily through respiratory droplets and contaminated...
Leaky Scanning02:28

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 stands for...

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Related Experiment Video

Updated: May 24, 2026

Subnanometer-Resolution Structural Determination of Hemagglutinin from Cryo-Electron Tomography of Influenza Viruses
08:19

Subnanometer-Resolution Structural Determination of Hemagglutinin from Cryo-Electron Tomography of Influenza Viruses

Published on: November 7, 2025

Receptor binding by influenza virus: using computational techniques to extend structural data.

Peter M Kasson1

  • 1Department of Molecular Physiology and Biological Physics and Department of Biomedical Engineering, University of Virginia, Charlottesville, Virginia 22908, United States. kasson@virginia.edu

Biochemistry
|March 14, 2012
PubMed
Summary
This summary is machine-generated.

Influenza hemagglutinin uses flexible glycan binding for host cell attachment. Molecular dynamics simulations aid in understanding these interactions, guiding future research on influenza binding and specificity.

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

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

Published on: May 29, 2016

Area of Science:

  • Biophysics
  • Virology
  • Computational Biology

Background:

  • Influenza virus entry relies on hemagglutinin (HA) binding to host cell surface glycans.
  • These interactions are often low-affinity and involve flexible molecules, complicating structural studies.
  • Understanding HA-glycan dynamics is key to determining viral tissue and host specificity.

Purpose of the Study:

  • To review the application of molecular dynamics (MD) simulations in studying influenza hemagglutinin-glycan interactions.
  • To highlight how MD can analyze flexibility, mutations, and glycosylation effects on binding.
  • To explore the integration of structural and dynamic data using MD.

Main Methods:

  • Review of recent studies utilizing molecular dynamics simulations.
  • Analysis of glycan and protein flexibility in crystallized hemagglutinin-receptor complexes.
  • Evaluation of ligand presentation and its relation to physiological states.

Main Results:

  • Molecular simulations offer insights into the dynamic nature of HA-glycan binding.
  • MD can predict changes in binding affinity due to mutations or altered glycosylation.
  • Simulations help bridge the gap between static structural data and dynamic biological processes.

Conclusions:

  • Molecular dynamics simulations are a powerful tool for characterizing influenza hemagglutinin-glycan interactions.
  • This approach aids in understanding viral specificity and potential therapeutic targets.
  • Future work should focus on integrating diverse data sources with MD for comprehensive analysis.