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[Disordered regions in C-domain structure of influenza virus M1 protein]

A L Ksenofontov, E N Dobrov, N V Fedorova

    Molekuliarnaia Biologiia
    |September 30, 2011
    PubMed

    Insights

    Influenza M1 protein

    Area of Science:

    • Virology
    • Structural Biology
    • Biochemistry

    Context:

    • Influenza virus matrix M1 protein is crucial for virion structure and cellular functions.
    • Previous X-ray data only characterized the N-terminal M1 protein domain.
    • The C-terminal domain and inter-domain loops remained structurally uncharacterized.

    Purpose:

    • To investigate the structural organization of the influenza M1 protein, particularly its C-terminal domain and inter-domain loops.
    • To explore the relationship between M1 protein structure and its polyfunctionality in infected cells.

    Summary:

    • Tritium bombardment of M1 protein from A/Puerto Rico/8/34 (H1N1) virus preferentially labeled C-domains and inter-domain loops.
    • Analytical centrifugation and dynamic light scattering indicated increased hydrodynamic parameters, suggesting low structural organization.
    • Computational analysis revealed unfolded regions primarily in the C-domain and inter-domain loops.

    Impact:

    • The study suggests that the polyfunctionality of influenza M1 protein stems from its structural plasticity.
    • This plasticity is attributed to the presence of intrinsically unstructured regions within the M1 protein.
    • Findings contribute to understanding influenza virus assembly and host-pathogen interactions.

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