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. 1992 May;66(5):3263–3269. doi: 10.1128/jvi.66.5.3263-3269.1992

Nuclear entry and nucleolar localization of the Newcastle disease virus (NDV) matrix protein occur early in infection and do not require other NDV proteins.

M E Peeples 1, C Wang 1, K C Gupta 1, N Coleman 1
PMCID: PMC241099  PMID: 1560547

Abstract

A large proportion of the Newcastle disease virus (NDV) matrix (M) protein is found in the nuclei of infected chicken embryo cells. Kinetic analysis indicated that much of the M protein enters the nucleus early in infection, concentrating in discrete regions of the nucleus and remaining there throughout infection. The M protein was found in localized regions of the nuclei of a variety of cell lines infected with NDV. Immunostaining for both M protein and nucleolar antigens indicated that most of these regions represent nucleoli. Moreover, this nucleolar localization of the M protein was observed in chicken embryo cells infected with 11 different strains of NDV. Only the M protein of strain HP displayed a modified pattern, concentrating in the nucleolus early in infection but in the cytoplasm late in infection. M protein transiently expressed in COS-1 cells also localized to the nucleus and nucleolus, indicating that the M protein does not require other NDV proteins for this localization.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Blondel D., Harmison G. G., Schubert M. Role of matrix protein in cytopathogenesis of vesicular stomatitis virus. J Virol. 1990 Apr;64(4):1716–1725. doi: 10.1128/jvi.64.4.1716-1725.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bratt M. A., Gallaher W. R. Preliminary analysis of the requirements for fusion from within and fusion from without by Newcastle disease virus. Proc Natl Acad Sci U S A. 1969 Oct;64(2):536–543. doi: 10.1073/pnas.64.2.536. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Bucher D., Popple S., Baer M., Mikhail A., Gong Y. F., Whitaker C., Paoletti E., Judd A. M protein (M1) of influenza virus: antigenic analysis and intracellular localization with monoclonal antibodies. J Virol. 1989 Sep;63(9):3622–3633. doi: 10.1128/jvi.63.9.3622-3633.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Clavell L. A., Bratt M. A. Hemolytic interaction of Newcastle disease virus and chicken erythrocytes. II. Determining factors. Appl Microbiol. 1972 Mar;23(3):461–470. doi: 10.1128/am.23.3.461-470.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Cullen B. R. Trans-activation of human immunodeficiency virus occurs via a bimodal mechanism. Cell. 1986 Sep 26;46(7):973–982. doi: 10.1016/0092-8674(86)90696-3. [DOI] [PubMed] [Google Scholar]
  6. Dunigan D. D., Baird S., Lucas-Lenard J. Lack of correlation between the accumulation of plus-strand leader RNA and the inhibition of protein and RNA synthesis in vesicular stomatitis virus infected mouse L cells. Virology. 1986 Apr 15;150(1):231–246. doi: 10.1016/0042-6822(86)90282-5. [DOI] [PubMed] [Google Scholar]
  7. Faaberg K. S., Peeples M. E. Strain variation and nuclear association of Newcastle disease virus matrix protein. J Virol. 1988 Feb;62(2):586–593. doi: 10.1128/jvi.62.2.586-593.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Gharakhanian E., Kasamatsu H. Two independent signals, a nuclear localization signal and a Vp1-interactive signal, reside within the carboxy-35 amino acids of SV40 Vp3. Virology. 1990 Sep;178(1):62–71. doi: 10.1016/0042-6822(90)90379-6. [DOI] [PubMed] [Google Scholar]
  9. Greenspan D., Palese P., Krystal M. Two nuclear location signals in the influenza virus NS1 nonstructural protein. J Virol. 1988 Aug;62(8):3020–3026. doi: 10.1128/jvi.62.8.3020-3026.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Gregoriades A. Influenza virus-induced proteins in nuclei and cytoplasm of infected cells. Virology. 1977 Jun 15;79(2):449–454. doi: 10.1016/0042-6822(77)90372-5. [DOI] [PubMed] [Google Scholar]
  11. Hamaguchi M., Nishikawa K., Toyoda T., Yoshida T., Hanaichi T., Nagai Y. Transcriptive complex of Newcastle disease virus. II. Structural and functional assembly associated with the cytoskeletal framework. Virology. 1985 Dec;147(2):295–308. doi: 10.1016/0042-6822(85)90132-1. [DOI] [PubMed] [Google Scholar]
  12. Hidaka M., Inoue J., Yoshida M., Seiki M. Post-transcriptional regulator (rex) of HTLV-1 initiates expression of viral structural proteins but suppresses expression of regulatory proteins. EMBO J. 1988 Feb;7(2):519–523. doi: 10.1002/j.1460-2075.1988.tb02840.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Hightower L. E., Bratt M. A. Protein synthesis in Newcastle disease virus-infected chicken embryo cells. J Virol. 1974 Apr;13(4):788–800. doi: 10.1128/jvi.13.4.788-800.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Kalderon D., Roberts B. L., Richardson W. D., Smith A. E. A short amino acid sequence able to specify nuclear location. Cell. 1984 Dec;39(3 Pt 2):499–509. doi: 10.1016/0092-8674(84)90457-4. [DOI] [PubMed] [Google Scholar]
  15. Kubota S., Siomi H., Satoh T., Endo S., Maki M., Hatanaka M. Functional similarity of HIV-I rev and HTLV-I rex proteins: identification of a new nucleolar-targeting signal in rev protein. Biochem Biophys Res Commun. 1989 Aug 15;162(3):963–970. doi: 10.1016/0006-291x(89)90767-5. [DOI] [PubMed] [Google Scholar]
  16. Lopata M. A., Cleveland D. W., Sollner-Webb B. High level transient expression of a chloramphenicol acetyl transferase gene by DEAE-dextran mediated DNA transfection coupled with a dimethyl sulfoxide or glycerol shock treatment. Nucleic Acids Res. 1984 Jul 25;12(14):5707–5717. doi: 10.1093/nar/12.14.5707. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Lyles D. S., Puddington L., McCreedy B. J., Jr Vesicular stomatitis virus M protein in the nuclei of infected cells. J Virol. 1988 Nov;62(11):4387–4392. doi: 10.1128/jvi.62.11.4387-4392.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Malim M. H., Hauber J., Le S. Y., Maizel J. V., Cullen B. R. The HIV-1 rev trans-activator acts through a structured target sequence to activate nuclear export of unspliced viral mRNA. Nature. 1989 Mar 16;338(6212):254–257. doi: 10.1038/338254a0. [DOI] [PubMed] [Google Scholar]
  19. Martin K., Helenius A. Nuclear transport of influenza virus ribonucleoproteins: the viral matrix protein (M1) promotes export and inhibits import. Cell. 1991 Oct 4;67(1):117–130. doi: 10.1016/0092-8674(91)90576-k. [DOI] [PubMed] [Google Scholar]
  20. McGinnes L. W., Morrison T. G. The nucleotide sequence of the gene encoding the Newcastle disease virus membrane protein and comparisons of membrane protein sequences. Virology. 1987 Feb;156(2):221–228. doi: 10.1016/0042-6822(87)90401-6. [DOI] [PubMed] [Google Scholar]
  21. Mehdi H., Ono E., Gupta K. C. Initiation of translation at CUG, GUG, and ACG codons in mammalian cells. Gene. 1990 Jul 16;91(2):173–178. doi: 10.1016/0378-1119(90)90085-6. [DOI] [PubMed] [Google Scholar]
  22. Paine P. L., Moore L. C., Horowitz S. B. Nuclear envelope permeability. Nature. 1975 Mar 13;254(5496):109–114. doi: 10.1038/254109a0. [DOI] [PubMed] [Google Scholar]
  23. Peeples M. E. Differential detergent treatment allows immunofluorescent localization of the Newcastle disease virus matrix protein within the nucleus of infected cells. Virology. 1988 Jan;162(1):255–259. doi: 10.1016/0042-6822(88)90418-7. [DOI] [PubMed] [Google Scholar]
  24. Puddington L., Lively M. O., Lyles D. S. Role of the nuclear envelope in synthesis, processing, and transport of membrane glycoproteins. J Biol Chem. 1985 May 10;260(9):5641–5647. [PubMed] [Google Scholar]
  25. Robbins J., Dilworth S. M., Laskey R. A., Dingwall C. Two interdependent basic domains in nucleoplasmin nuclear targeting sequence: identification of a class of bipartite nuclear targeting sequence. Cell. 1991 Feb 8;64(3):615–623. doi: 10.1016/0092-8674(91)90245-t. [DOI] [PubMed] [Google Scholar]
  26. Silver P. A. How proteins enter the nucleus. Cell. 1991 Feb 8;64(3):489–497. doi: 10.1016/0092-8674(91)90233-o. [DOI] [PubMed] [Google Scholar]
  27. Siomi H., Shida H., Maki M., Hatanaka M. Effects of a highly basic region of human immunodeficiency virus Tat protein on nucleolar localization. J Virol. 1990 Apr;64(4):1803–1807. doi: 10.1128/jvi.64.4.1803-1807.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Siomi H., Shida H., Nam S. H., Nosaka T., Maki M., Hatanaka M. Sequence requirements for nucleolar localization of human T cell leukemia virus type I pX protein, which regulates viral RNA processing. Cell. 1988 Oct 21;55(2):197–209. doi: 10.1016/0092-8674(88)90043-8. [DOI] [PubMed] [Google Scholar]
  29. TRAVER M. I., NORTHROP R. L., WALKER D. L. Site of intracellular antigen production by myxoviruses. Proc Soc Exp Biol Med. 1960 Jun;104:268–273. doi: 10.3181/00379727-104-25803. [DOI] [PubMed] [Google Scholar]
  30. WHEELOCK E. F., TAMM I. Mitosis and division in HeLa cells infected with influenza or Newcastle disease virus. Virology. 1959 Aug;8:532–536. doi: 10.1016/0042-6822(59)90056-x. [DOI] [PubMed] [Google Scholar]
  31. Weiss S. R., Bratt M. A. Polyadenylate sequences on Newcastle disease virus mRNA synthesized in vivo and in vitro. J Virol. 1974 Jun;13(6):1220–1230. doi: 10.1128/jvi.13.6.1220-1230.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Yoshida T., Nagai Y'Yoshii S., Maeno K., Matsumoto T. Membrane (M) protein of HVJ (Sendai virus): its role in virus assembly. Virology. 1976 May;71(1):143–161. doi: 10.1016/0042-6822(76)90101-x. [DOI] [PubMed] [Google Scholar]

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