Fusion of a single influenza virion particle with BLM

G I Maksaev1, A V Samsonov, A S Lipatov

  • 1Frumkin Institute of Electrochemistry, Russian Academy of Sciences, Moscow.

Membrane & Cell Biology
|May 23, 2001
PubMed

Insights

Researchers developed a model system to study influenza virus fusion with cell membranes. This system revealed that M2 channel activity in the virus membrane is crucial for fusion, as evidenced by electrical changes and amantadine inhibition.

Area of Science:

  • Biophysics
  • Virology
  • Cell Biology

Background:

  • Influenza virus infection involves fusion of the viral envelope with the cell's endosome membrane.
  • Understanding this fusion process is critical for developing antiviral strategies.

Purpose of the Study:

  • To investigate the fusion mechanism of single influenza virions with a model bilayer membrane (BLM).
  • To elucidate the role of M2 ion channels in the fusion process.

Main Methods:

  • Development of a specialized model system using fluorescently-labeled influenza virions and a BLM patch on a glass micropipette.
  • Monitoring changes in BLM conductance and integral fluorescence upon low pH-induced fusion.
  • Assessing the effect of amantadine, an M2 channel blocker, on fusion-induced electrical activity.

Main Results:

  • Fusion initiation led to increased fluorescence due to probe redistribution and simultaneous changes in BLM conductance.
  • Observed 2-5 distinct periods of channel activity per fusion event, likely representing individual virion fusions.
  • Amantadine completely inhibited the observed electrical activity, implicating M2 channels.

Conclusions:

  • The study successfully modeled influenza virus-BLM fusion, enabling real-time observation of individual fusion events.
  • The findings strongly suggest that M2 ion channel activity within the viral membrane is essential for the fusion process and subsequent electrical changes observed.
  • The developed model system provides a valuable tool for further investigation of viral fusion mechanisms.

Related Concept Videos

Viral Recombination00:57

Viral Recombination

Cells are sometimes infected by more than one virus at once. When two viruses disassemble to expose their genomes for replication in the same cell, similar regions of their genomes can pair together and exchange sequences in a process called recombination. Alternatively, viruses with segmented genomes can swap segments in a process called reassortment.
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...
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...
Inhibitors Of Virion Release01:25

Inhibitors Of Virion Release

Viral replication and dissemination rely on efficient mechanisms for host cell entry, genome replication, assembly, and release. Influenza viruses, such as types A and B, are negative-sense single-stranded RNA viruses with a segmented genome, that depend on two critical surface glycoproteins to carry out these processes: hemagglutinin (HA) and neuraminidase (NA). HA initiates infection by binding to sialic acid residues on the surface of host epithelial cells, facilitating receptor-mediated...