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Related Experiment Video

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Changes in sialic acid binding associated with egg adaptation decrease live attenuated influenza virus replication in

Harrison Powell1, Hsuan Liu1, Andrew Pekosz1

  • 1W. Harry Feinstone Department of Molecular Microbiology and Immunology, Johns Hopkins University Bloomberg School of Public Health, United States.

Vaccine
|May 14, 2021
PubMed
Summary
This summary is machine-generated.

Egg adaptation mutations in live attenuated influenza virus (LAIV) hemagglutinin (HA) can alter receptor binding and reduce viral replication. These changes may decrease LAIV vaccine efficacy by affecting virus growth in the nasal epithelium.

Keywords:
Egg adaptionInfluenzaLAIVNasal epithelial cellsVaccines

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Area of Science:

  • Virology
  • Vaccinology
  • Immunology

Background:

  • Live attenuated influenza virus (LAIV) replicates in the sinonasal epithelium.
  • Egg-based vaccine manufacturing can introduce mutations in the hemagglutinin (HA) protein, potentially altering its receptor binding and antigenic properties.
  • Specific mutations in the 2012-2013 H3N2 vaccine strain were suspected to decrease efficacy.

Purpose of the Study:

  • To investigate the impact of egg adaptation mutations in the HA protein on LAIV replication and receptor binding.
  • To assess how altered sialic acid binding affects LAIV replication in cell culture and human nasal epithelial cells.

Main Methods:

  • Recombinant LAIV viruses were engineered with wild-type (WT) HA, egg-adapted (EA) HA, or EA HA with enhanced α2,3 sialic acid binding (2,3 EA HA).
  • Sialic acid binding preferences were analyzed.
  • Viral replication was assessed in MDCK cells at different temperatures and in human nasal epithelial cell (hNEC) cultures.
  • Interferon-lambda (IFN-λ) production and cell infection rates were measured.

Main Results:

  • WT HA LAIV preferentially bound α2,6 sialic acid, while EA HA and 2,3 EA HA LAIVs showed increased binding to α2,3 sialic acid.
  • EA HA LAIV replicated similarly to WT HA LAIV at 32°C but showed reduced titers at 37°C.
  • 2,3 EA HA LAIV exhibited poor replication at both tested temperatures.
  • WT HA LAIV demonstrated the highest IFN-λ induction and infected more hNECs compared to the other strains.

Conclusions:

  • Egg adaptation mutations in HA that enhance α2,3 sialic acid binding can impair LAIV replication.
  • These replication deficits may contribute to reduced live attenuated influenza vaccine efficacy.
  • Understanding HA-receptor interactions is crucial for developing effective influenza vaccines.