Abstract
Infection of human epidermoid carcinoma No. 2 cells with herpes simplex virus type 1 (HSV-1) leads to a reorganization of antigens associated with both the small and heterogeneous nuclear ribonucleoprotein complexes (snRNP and hnRNP). The hnRNP core protein antigens remain associated with the host chromatin, which appears to collapse into internal aggregates and along the nuclear envelope. More striking is the formation of prominent clusters of snRNP antigens (both general and U1 snRNP specific), which appear to condense throughout the nucleus then migrate to the periphery. These snRNP clusters have been identified at the fine structure level by immuno-electron microscopy. The HSV-1 presumed transcriptional activator ICP4, DNA-binding protein ICP8, and two capsid proteins ICP5 and p40 are not detectably associated with the snRNP clusters. Similar reorganization of snRNP occurs with HSV-2 and upon infection of African green monkey VERO cells with HSV-1. We speculate that the snRNP clusters arise from an increase in size and density of the interchromatin granule region of the host cell as a result of the partial inactivation of snRNP and host pre-mRNA splicing.
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- Bastow K. F., Bouchard J., Ren X. J., Cheng Y. C. Synthesis of dihydrofolate reductase and metabolism of related RNA in a methotrexate resistant human cell line infected with herpes simplex virus type 2. Virology. 1986 Mar;149(2):199–207. doi: 10.1016/0042-6822(86)90121-2. [DOI] [PubMed] [Google Scholar]
- Bernhard W. A new staining procedure for electron microscopical cytology. J Ultrastruct Res. 1969 May;27(3):250–265. doi: 10.1016/s0022-5320(69)80016-x. [DOI] [PubMed] [Google Scholar]
- Beyer A. L., Christensen M. E., Walker B. W., LeStourgeon W. M. Identification and characterization of the packaging proteins of core 40S hnRNP particles. Cell. 1977 May;11(1):127–138. doi: 10.1016/0092-8674(77)90323-3. [DOI] [PubMed] [Google Scholar]
- Bibor-Hardy V., Bernard M., Simard R. Nuclear matrix modifications at different stages of infection by herpes simplex virus type 1. J Gen Virol. 1985 May;66(Pt 5):1095–1103. doi: 10.1099/0022-1317-66-5-1095. [DOI] [PubMed] [Google Scholar]
- Bibor-Hardy V., Pouchelet M., St-Pierre E., Herzberg M., Simard R. The nuclear matrix is involved in herpes simplex virogenesis. Virology. 1982 Sep;121(2):296–306. doi: 10.1016/0042-6822(82)90169-6. [DOI] [PubMed] [Google Scholar]
- Billings P. B., Allen R. W., Jensen F. C., Hoch S. O. Anti-RNP monoclonal antibodies derived from a mouse strain with lupus-like autoimmunity. J Immunol. 1982 Mar;128(3):1176–1180. [PubMed] [Google Scholar]
- Brown S. W. Heterochromatin. Science. 1966 Jan 28;151(3709):417–425. doi: 10.1126/science.151.3709.417. [DOI] [PubMed] [Google Scholar]
- De Mey J., Moeremans M., Geuens G., Nuydens R., De Brabander M. High resolution light and electron microscopic localization of tubulin with the IGS (immuno gold staining) method. Cell Biol Int Rep. 1981 Sep;5(9):889–899. doi: 10.1016/0309-1651(81)90204-6. [DOI] [PubMed] [Google Scholar]
- Dreyfuss G. Structure and function of nuclear and cytoplasmic ribonucleoprotein particles. Annu Rev Cell Biol. 1986;2:459–498. doi: 10.1146/annurev.cb.02.110186.002331. [DOI] [PubMed] [Google Scholar]
- Fakan S., Leser G., Martin T. E. Immunoelectron microscope visualization of nuclear ribonucleoprotein antigens within spread transcription complexes. J Cell Biol. 1986 Oct;103(4):1153–1157. doi: 10.1083/jcb.103.4.1153. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Fakan S., Leser G., Martin T. E. Ultrastructural distribution of nuclear ribonucleoproteins as visualized by immunocytochemistry on thin sections. J Cell Biol. 1984 Jan;98(1):358–363. doi: 10.1083/jcb.98.1.358. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Geoghegan W. D., Ackerman G. A. Adsorption of horseradish peroxidase, ovomucoid and anti-immunoglobulin to colloidal gold for the indirect detection of concanavalin A, wheat germ agglutinin and goat anti-human immunoglobulin G on cell surfaces at the electron microscopic level: a new method, theory and application. J Histochem Cytochem. 1977 Nov;25(11):1187–1200. doi: 10.1177/25.11.21217. [DOI] [PubMed] [Google Scholar]
- Gratzner H. G. Monoclonal antibody to 5-bromo- and 5-iododeoxyuridine: A new reagent for detection of DNA replication. Science. 1982 Oct 29;218(4571):474–475. doi: 10.1126/science.7123245. [DOI] [PubMed] [Google Scholar]
- Jones R. E., Okamura C. S., Martin T. E. Immunofluorescent localization of the proteins of nuclear ribonucleoprotein complexes. J Cell Biol. 1980 Jul;86(1):235–243. doi: 10.1083/jcb.86.1.235. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Knipe D. M., Spang A. E. Definition of a series of stages in the association of two herpesviral proteins with the cell nucleus. J Virol. 1982 Jul;43(1):314–324. doi: 10.1128/jvi.43.1.314-324.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kwong A. D., Frenkel N. Herpes simplex virus-infected cells contain a function(s) that destabilizes both host and viral mRNAs. Proc Natl Acad Sci U S A. 1987 Apr;84(7):1926–1930. doi: 10.1073/pnas.84.7.1926. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Lerner E. A., Lerner M. R., Janeway C. A., Jr, Steitz J. A. Monoclonal antibodies to nucleic acid-containing cellular constituents: probes for molecular biology and autoimmune disease. Proc Natl Acad Sci U S A. 1981 May;78(5):2737–2741. doi: 10.1073/pnas.78.5.2737. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Leser G. P., Escara-Wilke J., Martin T. E. Monoclonal antibodies to heterogeneous nuclear RNA-protein complexes. The core proteins comprise a conserved group of related polypeptides. J Biol Chem. 1984 Feb 10;259(3):1827–1833. [PubMed] [Google Scholar]
- McLean I. W., Nakane P. K. Periodate-lysine-paraformaldehyde fixative. A new fixation for immunoelectron microscopy. J Histochem Cytochem. 1974 Dec;22(12):1077–1083. doi: 10.1177/22.12.1077. [DOI] [PubMed] [Google Scholar]
- Mount S. M., Pettersson I., Hinterberger M., Karmas A., Steitz J. A. The U1 small nuclear RNA-protein complex selectively binds a 5' splice site in vitro. Cell. 1983 Jun;33(2):509–518. doi: 10.1016/0092-8674(83)90432-4. [DOI] [PubMed] [Google Scholar]
- Nii S., Morgan C., Rose H. M. Electron microscopy of herpes simplex virus. II. Sequence of development. J Virol. 1968 May;2(5):517–536. doi: 10.1128/jvi.2.5.517-536.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Puvion-Dutilleul F., Pichard E., Sheldrick P., Amalric F., Puvion E. Appearance of host-specific nucleolar proteins in intranuclear "dense bodies" following herpes simplex infection. Eur J Cell Biol. 1986 Jan;39(2):458–468. [PubMed] [Google Scholar]
- Quinlan M. P., Chen L. B., Knipe D. M. The intranuclear location of a herpes simplex virus DNA-binding protein is determined by the status of viral DNA replication. Cell. 1984 Apr;36(4):857–868. doi: 10.1016/0092-8674(84)90035-7. [DOI] [PubMed] [Google Scholar]
- Rixon F. J., Atkinson M. A., Hay J. Intranuclear distribution of herpes simplex virus type 2 DNA synthesis: examination by light and electron microscopy. J Gen Virol. 1983 Sep;64(Pt 9):2087–2092. doi: 10.1099/0022-1317-64-9-2087. [DOI] [PubMed] [Google Scholar]
- Sass H., Pederson T. Transcription-dependent localization of U1 and U2 small nuclear ribonucleoproteins at major sites of gene activity in polytene chromosomes. J Mol Biol. 1984 Dec 25;180(4):911–926. doi: 10.1016/0022-2836(84)90263-8. [DOI] [PubMed] [Google Scholar]
- Schek N., Bachenheimer S. L. Degradation of cellular mRNAs induced by a virion-associated factor during herpes simplex virus infection of Vero cells. J Virol. 1985 Sep;55(3):601–610. doi: 10.1128/jvi.55.3.601-610.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Schwartz J., Roizman B. Similarities and Differences in the Development of Laboratory Strains and Freshly Isolated Strains of Herpes Simplex Virus in HEp-2 Cells: Electron Microscopy. J Virol. 1969 Dec;4(6):879–889. doi: 10.1128/jvi.4.6.879-889.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Sharp P. A. Splicing of messenger RNA precursors. Science. 1987 Feb 13;235(4790):766–771. doi: 10.1126/science.3544217. [DOI] [PubMed] [Google Scholar]
- Showalter S. D., Zweig M., Hampar B. Monoclonal antibodies to herpes simplex virus type 1 proteins, including the immediate-early protein ICP 4. Infect Immun. 1981 Dec;34(3):684–692. doi: 10.1128/iai.34.3.684-692.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Slot J. W., Geuze H. J. A new method of preparing gold probes for multiple-labeling cytochemistry. Eur J Cell Biol. 1985 Jul;38(1):87–93. [PubMed] [Google Scholar]
- Wagner E. K., Roizman B. Ribonucleic acid synthesis in cells infected with herpes simplex virus. I. Patterns of ribonucleic acid synthesis in productively infected cells. J Virol. 1969 Jul;4(1):36–46. doi: 10.1128/jvi.4.1.36-46.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Williamson D. H., Fennell D. J. The use of fluorescent DNA-binding agent for detecting and separating yeast mitochondrial DNA. Methods Cell Biol. 1975;12:335–351. doi: 10.1016/s0091-679x(08)60963-2. [DOI] [PubMed] [Google Scholar]