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Role of cell cytoskeleton in Mo-MuLV env transport and processing: implications in ts1 neuropathology

M M Soong, W A Tompkins

    Experimental and Molecular Pathology
    |June 1, 1987
    PubMed

    Insights

    Cytochalasin B and monensin disrupt Moloney murine leukemia virus (Mo-MuLV) replication by affecting the processing and transport of the viral envelope precursor (gPr80env). The cytoskeleton plays a crucial role in this process, influencing oligosaccharide modification and viral glycoprotein maturation.

    Area of Science:

    • Virology
    • Cell Biology
    • Molecular Biology

    Background:

    • Moloney murine leukemia virus (Mo-MuLV) infection leads to the production of viral progeny.
    • The viral envelope precursor, gPr80env, undergoes complex processing and transport for maturation into surface glycoproteins.
    • Disruptions in these processes can affect viral yield and potentially lead to disease.

    Purpose of the Study:

    • To investigate the role of the cytoskeleton in the processing and transport of the Mo-MuLV env precursor, gPr80env.
    • To determine the impact of microfilament disruption and glycoprotein transport inhibition on viral replication.
    • To elucidate the relationship between oligosaccharide modification and gPr80env maturation.

    Main Methods:

    • Treatment of Mo-MuLV-infected cells with cytochalasin B (CB) and monensin.
    • Pulse-chase experiments using [3H]leucine labeling.
    • Analysis of viral protein processing and cell surface expression.
    • Biochemical fractionation of cell cytoskeletons and analysis of associated proteins via SDS-PAGE and immunoprecipitation.
    • Endoglycosidase H (Endo-H) sensitivity assays.

    Main Results:

    • CB and monensin treatment reduced Mo-MuLV yield and inhibited gPr80env processing.
    • Both drugs caused accumulation of gPr80env in the cytoskeleton-rich fraction, with a shift towards Endo-H resistant forms.
    • Mo-MuLV ts1 mutant, defective in env processing, also showed gPr80env accumulation in the cytoskeleton.
    • gp70, the mature surface glycoprotein, was absent on the cell surface of treated cells and ts1 mutant at restrictive temperatures.

    Conclusions:

    • The cytoskeleton is integral to the transport and processing of Mo-MuLV gPr80env.
    • Oligosaccharide conversion is a critical step in gPr80env maturation and transport.
    • Accumulation of gPr80env on the cytoskeleton may contribute to neurological disorders associated with Mo-MuLV ts1 infection.

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