1887

Abstract

The matrix (M) protein isolated from influenza A/WSN/33 virus, when reconstituted with ribonucleo-protein (RNP) cores of vesicular stomatitis virus (VSV), resulted in inhibition of VSV transcription . The presence of endogenous wild-type (wt) or mutant (O23) VSV matrix (M) protein on RNP cores did not prevent down-regulation of VSV transcription by reconstituted influenza virus M protein. In fact, endogenous VSV wt M protein augmented transcription inhibition by M protein reconstituted with RNP/M protein cores, whereas mutant O23 M protein endogenous to RNP cores had no effect on down-regulation of VSV transcription by M protein. These data suggest that VSV M protein and influenza virus M protein recognize two different sites on RNP cores responsible for down-regulation of VSV transcription. Monoclonal antibodies (MAbs) directed to epitope 2 of M protein had been previously shown to reverse transcription inhibition by M protein on influenza virus RNP cores, but the same epitope 2-specific MAb had little effect on transcription inhibition by M protein reconstituted with VSV RNP cores. VSV M protein bears a striking resemblance biologically and genetically to the M protein, including, as shown here, their capacity to bind viral RNA. However, the VSV wt M protein exhibited no capacity to down-regulate transcription by influenza virus RNP cores. The significance of these studies is the identification on VSV RNP templates of at least two separate sites for recognition of protein factors that repress VSV transcription.

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1992-03-01
2022-01-25
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References

  1. Both G. W., Air G. M. 1977; Nucleotide sequence coding for the N-terminal region of the matrix protein of influenza. European Journal of Biochemistry 96:363–371
    [Google Scholar]
  2. Bowen B., Steinberg J., Laemmli U. K., Weintraub H. 1980; The detection of DNA-binding protein by protein blotting. Nucleic Acids Research 8:1–20
    [Google Scholar]
  3. Carroll A. R., Wagner R. R. 1979; Role of the membrane (M) protein in endogenous inhibition of in vitro transcription by vesicular stomatitis virus. Journal of Virology 29:134–142
    [Google Scholar]
  4. Emerson S. U. 1987; The transcription of vesicular stomatitis virus. In The Rhabdoviruses pp 245–269 Edited by Wagner R. R. New York: Plenum Press;
    [Google Scholar]
  5. Gregoriades A. 1973; The membrane protein of influenza virion extracted from virus and infected cells with acidic chloroform-methanol. Virology 54:369–383
    [Google Scholar]
  6. Gregoriades A., Frangione B. 1981; Insertion of influenza M protein into the viral lipid bilayer and localization of site of insertion. Journal of Virology 40:323–328
    [Google Scholar]
  7. Kaptur P. E., Rhodes R. B., Lyles D. S. 1991; Sequences of the vesicular stomatitis virus matrix protein involved in binding to nucleocapsids. Journal of Virology 65:1057–1065
    [Google Scholar]
  8. Lamb R. A., Choppin P. W. 1983; The structure and replication of influenza virus. Annual Review of Biochemistry 52:467–506
    [Google Scholar]
  9. Lamb R. A., Zebedee S. L. 1985; Influenza M2 protein is an integral membrane protein expressed on the infected cell surface. Cell 40:627–633
    [Google Scholar]
  10. Ogden J. R., Pal R., Wagner R. R. 1986; Mapping regions of the matrix protein of vesicular stomatitis virus which bind to ribonucleocapsids, liposomes and monoclonal antibodies. Journal of Virology 59:860–868
    [Google Scholar]
  11. Pal R., Grinnell B. W., Snyder R. M., Wiener J. R., Volk W. A., Wagner R. R. 1985; Monoclonal antibodies for the M protein of vesicular stomatitis virus (Indiana serotype) and to a cDNA M-gene expression product. Journal of Virology 55:298–306
    [Google Scholar]
  12. Pons M. W., Hirst G. K. 1969; The single- and double-stranded RNAs and the protein of incomplete influenza virus. Virology 38:68–72
    [Google Scholar]
  13. Rose J. K., Gallione C. J. 1981; Nucleotide sequences of the mRNAs encoding the vesicular stomatitis virus G and M proteins determined from cDNA clones containing the complete coding regions. Journal of Virology 39:519–528
    [Google Scholar]
  14. Rose J. K., Doolittle R. F., Anilionis A., Curtis P. J., Wunner W. H. 1982; Homology between the glycoproteins of vesicular stomatitis virus and rabies. Journal of Virology 43:361–364
    [Google Scholar]
  15. van Wyke K. L., Yewdell J. W., Reck L. J., Murphy B. R. 1984; Antigenic characterization of influenza A virus matrix protein with monoclonal antibodies. Journal of Virology 49:248–252
    [Google Scholar]
  16. Wagner R. R. 1987; Rhabdovirus biology and infection: an overview. In The Rhabdoviruses pp 9–74 Edited by Wagner R. R. New York: Plenum Press;
    [Google Scholar]
  17. Wakefield L., Brownlee G. G. 1989; RNA binding properties of influenza virus matrix protein M1 . Nucleic Acids Research 17:8569–8580
    [Google Scholar]
  18. Wiener J. R., Pal R., Barenholz Y., Wagner R. R. 1983; Influence of the peripheral matrix protein of vesicular stomatitis virus on the membrane dynamics of mixed phospholipid vesicles: fluorescence studies. Biochemistry 22:2162–2170
    [Google Scholar]
  19. Winter G., Fields S. 1980; Cloning of influenza cDNA into M13: the sequence of the RNA segment encoding the A/PR/8/34 matrix protein. Nucleic Acids Research 8:1965–1974
    [Google Scholar]
  20. Ye Z., Pal R., Fox J. W., Wagner R. R. 1987; Functional and antigenic domains of the matrix (M1) protein of influenza A virus. Journal of Virology 61:239–246
    [Google Scholar]
  21. YE Z., Baylor N. W., Wagner R. R. 1989; Transcription-inhibition and RNA-binding domains of influenza A virus matrix protein mapped with anti-idiotypic antibodies and synthetic peptides. Journal of Virology 63:3586–3594
    [Google Scholar]
  22. Zvonarjev A. Y., Ghendon Y. Z. 1980; Influence of membrane (M) protein on influenza A virus virion transcriptase activity in vitro and its susceptibility to rimantadine. Journal of Virology 33:583–586
    [Google Scholar]
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