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MicroRNA-based Regulation of Picornavirus Tropism
09:05

MicroRNA-based Regulation of Picornavirus Tropism

Published on: February 6, 2017

Myristylation of picornavirus capsid protein VP4 and its structural significance

M Chow, J F Newman, D Filman

    Nature
    |June 11, 1987
    PubMed

    Insights

    Poliovirus and picornavirus particles are modified with myristic acid, a fatty acid, covalently attached to capsid proteins. This myristylation may influence virus assembly and cell entry.

    Area of Science:

    • Virology
    • Structural Biology
    • Biochemistry

    Background:

    • Picornaviruses, including poliovirus, are significant human pathogens.
    • Viral capsid proteins play crucial roles in virus structure and function.
    • Post-translational modifications can alter protein function and localization.

    Purpose of the Study:

    • To investigate the specific modifications of poliovirus and other picornavirus particles.
    • To determine the location and nature of these modifications within the virus structure.
    • To explore the potential functional implications of these modifications.

    Main Methods:

    • Covalent binding analysis of myristic acid to viral capsid proteins.
    • High-resolution electron density mapping of poliovirus particles.
    • Comparative analysis with other myristylated proteins.

    Main Results:

    • Evidence obtained for specific covalent binding of myristic acid to picornavirus capsid proteins.
    • Electron density map confirmed the precise location of the myristate molecule within the poliovirus particle.
    • Identified myristylation as a specific modification in these viruses.

    Conclusions:

    • Myristic acid is covalently bound to capsid proteins in poliovirus and other picornaviruses.
    • The myristate moiety is precisely located within the virus particle.
    • Myristylation may play a role in picornavirus capsid assembly or cellular entry.

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