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Structural polypeptides of the murine coronavirus DVIM.

K Sugiyama, R Ishikawa, N Fukuhara

    Archives of Virology
    |January 1, 1986
    PubMed
    Summary

    Murine coronavirus DVIM structural polypeptides were analyzed using SDS-PAGE. DVIM features a unique N-linked glycopolypeptide (gp69) and O-linked glycopolypeptides, distinguishing it from other strains.

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    Area of Science:

    • Virology
    • Molecular Biology
    • Structural Biology

    Background:

    • Murine coronaviruses (Murine Coronaviruses) are significant pathogens.
    • Understanding the structural polypeptides of different strains is crucial for viral characterization.

    Purpose of the Study:

    • To analyze and compare the structural polypeptides of the murine coronavirus DVIM (diarrhoea virus of infant mice) with other strains.
    • To identify strain-specific polypeptides and their glycosylation patterns.

    Main Methods:

    • Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) was employed for polypeptide analysis.
    • Analysis was performed in the presence and absence of reducing agents (2-mercaptoethanol).
    • Tunicamycin treatment was used to investigate glycosylation types.

    Main Results:

    • Three major glycopolypeptides (gp180, gp69, gp25) and one non-glycosylated polypeptide (p58) were detected in DVIM.
    • gp69, a DVIM-specific glycopolypeptide, features N-glycosidic linkages potentially related to viral envelope projections.
    • The gp25 family includes O-linked glycopolypeptides, indicated by tunicamycin resistance, and gp140 is a disulfide-linked dimer of gp69.

    Conclusions:

    • DVIM possesses distinct glycopolypeptide profiles, including a unique N-linked gp69 and O-linked polypeptides within the gp25 family.
    • These structural differences may correlate with specific viral properties and serological relationships.
    • DVIM shows serological relatedness to the MHV-S strain, as confirmed by neutralization assays.

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