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In Vitro Disassembly of Influenza A Virus Capsids by Gradient Centrifugation
07:24

In Vitro Disassembly of Influenza A Virus Capsids by Gradient Centrifugation

Published on: March 27, 2016

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[pH-dependent rearrangements in the influenza A virus]

O P Zhirnov, A A Manykin

    Voprosy Virusologii
    |October 23, 2014
    PubMed

    Insights

    Influenza virus infectivity depends on hemagglutinin cleavage. Acidic conditions alter virus structure, impacting permeability and M1-RNP interactions, crucial for viral function.

    Area of Science:

    • Virology
    • Structural Biology
    • Biochemistry

    Context:

    • Influenza virus structure comprises internal ribonucleoprotein (RNP) and an external lipid envelope.
    • Key surface glycoproteins include hemagglutinin (HA) and neuraminidase (NA), with matrix protein M1 linking internal and external components.

    Purpose:

    • To investigate the effect of acidic pH on influenza virus grown in MDCK-H cells.
    • To determine how hemagglutinin cleavage influences virus sensitivity to acidic conditions and its structural integrity.

    Summary:

    • Influenza A/Aichi/68 (H3N2) virus grown in MDCK-H cells showed uncleaved HA0, low infectivity, and resistance to acidic pH.
    • Acidic treatment of trypsin-activated virus (cleaved HA1+HA2) led to increased permeability, reduced infectivity, and enhanced M1-RNP interaction.

    Impact:

    • Cleavage of hemagglutinin (HA) is critical for influenza virus infectivity and response to acidic environments.
    • The cleaved HA1+HA2 structure mediates transmembrane interactions, linking surface glycoproteins to internal viral components.

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