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J Interferon Res. 1989 Dec;9(6):679-89.

Purification and characterization of a human Mx protein.

Author information

  • 1Laboratory of Viral and Molecular Pathogenesis, National Institute of Neurological Disorders and Stroke, Bethesda, MD 20892.

Abstract

Human interferon-beta (IFN-beta) induces in human embryonic foreskin fibroblasts a cytoplasmic protein with antigenic similarities to mouse Mx protein, a nuclear protein implicated in inhibition of influenza virus replication. The human protein was purified to virtual homogeneity by immunoaffinity chromatography using a monoclonal antibody to mouse Mx protein. The purified protein has an apparent Mr of 78,000 and displays a strong tendency to self-aggregate. It can be resolved on two-dimensional gels into four spots with pIs between 6.0 and 6.2, each of which reacts with antibodies to mouse Mx protein. The partial amino-terminal sequence was determined for the affinity-purified protein. Cytoplasmic microinjection of the affinity-purified protein does not lead to efficient protection against infection with influenza virus. Cytoplasmic microinjection of the monoclonal Mx antibody, which increases suceptibility of IFN-treated mouse Mx cells to influenza virus, does not alter the viral susceptibility of IFN-treated human cells. These results suggest that, unlike the mouse Mx protein, the human Mx protein studied in this communication may not be sufficient to confer to cells a high degree of protection against influenza virus.

PMID:
2607176
[PubMed - indexed for MEDLINE]
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