Viruses and interferon: a fight for supremacy (original) (raw)

• Samuel, C. E. Antiviral actions of interferons. Clin. Microbiol. Rev. 14, 778–809 (2001).
  Article CAS PubMed PubMed Central Google Scholar
• Levy, D. E. & Garcia-Sastre, A. The virus battles: IFN induction of the antiviral state and mechanisms of viral evasion. Cytokine Growth Factor Rev. 12, 143–156 (2001).
  Article CAS PubMed Google Scholar
• Grander, D., Sangfelt, O. & Erickson, S. How does interferon exert its cell growth inhibitory effect? Eur. J. Haematol. 59, 129–135 (1997).
  Article CAS PubMed Google Scholar
• Biron, C. A. Interferons-α and -β as immune regulators — a new look. Immunity 14, 661–664 (2001).
  Article CAS PubMed Google Scholar
• Doly, J., Civas, A., Navarro, S. & Uze, G. Type I interferons: expression and signalization. Cell. Mol. Life Sci. 54, 1109–1121 (1998).
  Article CAS PubMed Google Scholar
• Hwang, S. Y. et al. A null mutation in the gene encoding a type I interferon receptor component eliminates antiproliferative and antiviral responses to interferons-α and -β and alters macrophage responses. Proc. Natl Acad. Sci. USA 92, 11284–11288 (1995).Mice with a null mutation in the Ifnar1 gene were generated and it was shown that the type I IFN system is an important acute antiviral defence.
  Article CAS PubMed PubMed Central Google Scholar
• Kamijo, R. et al. Biological functions of IFN-γ and IFN-α/β: lessons from studies in gene knockout mice. Hokkaido Igaku Zasshi. 69, 1332–1338 (1994).
  CAS PubMed Google Scholar
• Barnes, B., Lubyova, B. & Pitha, P. M. Review: on the role of IRF in host defense. J. Interferon Cytokine Res. 22, 59–71 (2002).
  Article CAS PubMed Google Scholar
• Barnes, B. J., Moore, P. A. & Pitha, P. M. Virus-specific activation of a novel interferon regulatory factor, IRF-5, results in the induction of distinct interferon-α genes. J. Biol. Chem. 276, 23382–23390 (2001).
  Article CAS PubMed Google Scholar
• Juang, Y. et al. Primary activation of interferon A and interferon B gene transcription by interferon regulatory factor 3. Proc. Natl Acad. Sci. USA 95, 9837–9842 (1998).This study identified IRF3 and CBP/p300 as integral components of the virus-induced complex that stimulates type I IFN gene transcription, and indicated a new mechanism by which adenovirus might overcome the antiviral effects of the IFN pathway.
  Article CAS PubMed PubMed Central Google Scholar
• Levy, D. E., Marie, I., Smith, E. & Prakash, A. Enhancement and diversification of IFN induction by IRF-7-mediated positive feedback. J. Interferon Cytokine Res. 22, 87–93 (2002).
  Article CAS PubMed Google Scholar
• Yeow, W. S. et al. Reconstitution of virus-mediated expression of interferon-α genes in human fibroblast cells by ectopic interferon regulatory factor-7. J. Biol. Chem. 275, 6313–6320 (2000).
  Article CAS PubMed Google Scholar
• Biron, C. A. & Sen, G. C. in Fields Virology (eds Knipe, D. M. & Howley, P. M.) 321–352 (Lippincott, Williams & Wilkins, Philadelphia, 2001).
  Google Scholar
• de Veer, M. J. et al. Functional classification of interferon-stimulated genes identified using microarrays. J. Leukocyte Biol. 69, 912–920 (2001).
  CAS PubMed Google Scholar
• Der, S. D., Zhou, A., Williams, B. R. & Silverman, R. H. Identification of genes differentially regulated by interferon-α, -β or -γ using oligonucleotide arrays. Proc. Natl Acad. Sci. USA 95, 15623–15628 (1998).Using microarray-based mRNA profiling of IFN-treated human cells, this study showed the usefulness of oligonucleotide arrays for monitoring mammalian gene expression and provided new insights into the basic mechanisms of IFN actions.
  Article CAS PubMed PubMed Central Google Scholar
• Meurs, E. et al. Molecular cloning and characterization of the human double-stranded RNA-activated protein kinase induced by interferon. Cell 62, 379–390 (1990).
  Article CAS PubMed Google Scholar
• Gale, M. Jr & Katze, M. G. Molecular mechanisms of interferon resistance mediated by viral-directed inhibition of PKR, the interferon-induced protein kinase. Pharmacol. Ther. 78, 29–46 (1998).
  Article CAS PubMed Google Scholar
• Ghosh, S. K. et al. Cloning, sequencing and expression of two murine 2′-5′-oligoadenylate synthetases. Structure–function relationships. J. Biol. Chem. 266, 15293–15299 (1991).
  CAS PubMed Google Scholar
• Zhou, A., Hassel, B. A. & Silverman, R. H. Expression cloning of 2-5A-dependent RNAase: a uniquely regulated mediator of interferon action. Cell 72, 753–765 (1993).
  Article CAS PubMed Google Scholar
• Zhou, A. et al. Interferon action and apoptosis are defective in mice devoid of 2′,5′-oligoadenylate-dependent RNase L. EMBO J. 16, 6355–6363 (1997).
  Article CAS PubMed PubMed Central Google Scholar
• Staeheli, P. & Haller, O. Interferon-induced Mx protein: a mediator of cellular resistance to influenza virus. Interferon 8, 1–23 (1987).
  CAS PubMed Google Scholar
• Kochs, G., Janzen, C., Hohenberg, H. & Haller, O. Antivirally active MxA protein sequesters La Crosse virus nucleocapsid protein into perinuclear complexes. Proc. Natl Acad. Sci. USA 99, 3153–3158 (2002).
  Article CAS PubMed PubMed Central Google Scholar
• Patterson, J. B., Thomis, D. C., Hans, S. L. & Samuel, C. E. Mechanism of interferon action: double-stranded RNA-specific adenosine deaminase from human cells is inducible by α- and γ-interferons. Virology 210, 508–511 (1995).
  Article CAS PubMed Google Scholar
• Biron, C. A. Role of early cytokines, including α- and β-interferons (IFN-α/β), in innate and adaptive immune responses to viral infections. Semin. Immunol. 10, 383–390 (1998).
  Article CAS PubMed Google Scholar
• Guidotti, L. G. & Chisari, F. V. Noncytolytic control of viral infections by the innate and adaptive immune response. Annu. Rev. Immunol. 19, 65–91 (2001).
  Article CAS PubMed Google Scholar
• Taniguchi, T. & Takaoka, A. The interferon-α/β system in antiviral responses: a multimodal machinery of gene regulation by the IRF family of transcription factors. Curr. Opin. Immunol. 14, 111–116 (2002).
  Article CAS PubMed Google Scholar
• Nguyen, H., Hiscott, J. & Pitha, P. M. The growing family of interferon regulatory factors. Cytokine Growth Factor Rev. 8, 293–312 (1997).
  Article CAS PubMed Google Scholar
• Zimring, J. C., Goodbourn, S. & Offermann, M. K. Human herpesvirus 8 encodes an interferon regulatory factor (IRF) homolog that represses IRF-1-mediated transcription. J. Virol. 72, 701–707 (1998).
  CAS PubMed PubMed Central Google Scholar
• Cebulla, C. M., Miller, D. M. & Sedmak, D. D. Viral inhibition of interferon signal transduction. Intervirology 42, 325–330 (1999).
  Article CAS PubMed Google Scholar
• Goodbourn, S., Didcock, L. & Randall, R. E. Interferons: cell signalling, immune modulation, antiviral response and virus countermeasures. J. Gen. Virol. 81, 2341–2364 (2000).
  Article CAS PubMed Google Scholar
• Garcia-Sastre, A. Mechanisms of inhibition of the host interferon-α/β-mediated antiviral responses by viruses. Microbes Infect. 4, 647–655 (2002).
  Article CAS PubMed Google Scholar
• Isaacs, A. & Lindenmann, J. Virus interference. I. The interferon. Proc. R. Soc. Lond. B 147, 258–267 (1957).
  Article CAS PubMed Google Scholar
• Haller, O., Frese, M. & Kochs, G. Mx proteins: mediators of innate resistance to RNA viruses. Rev. Sci. Tech. 17, 220–230 (1998).
  Article CAS PubMed Google Scholar
• Bergmann, M. et al. Influenza virus NS1 protein counteracts PKR-mediated inhibition of replication. J. Virol. 74, 6203–6206 (2000).
  Article CAS PubMed PubMed Central Google Scholar
• Garcia-Sastre, A. et al. Influenza A virus lacking the NS1 gene replicates in interferon-deficient systems. Virology 252, 324–330 (1998).
  Article CAS PubMed Google Scholar
• Garcia-Sastre, A. Inhibition of interferon-mediated antiviral responses by influenza A viruses and other negative-strand RNA viruses. Virology 279, 375–384 (2001).
  Article CAS PubMed Google Scholar
• Lee, T. G., Tang, N., Thompson, S., Miller, J. & Katze, M. G. The 58,000-dalton cellular inhibitor of the interferon-induced double-stranded RNA-activated protein kinase (PKR) is a member of the tetratricopeptide-repeat family of proteins. Mol. Cell. Biol. 14, 2331–2342 (1994).
  Article CAS PubMed PubMed Central Google Scholar
• Gale, M. Jr et al. Regulation of interferon-induced protein kinase PKR: modulation of P58IPK inhibitory function by a novel protein, P52rIPK. Mol. Cell. Biol. 18, 859–871 (1998).
  Article CAS PubMed PubMed Central Google Scholar
• Melville, M. W. et al. The cellular inhibitor of the PKR protein kinase, P58(IPK), is an influenza virus-activated co-chaperone that modulates heat-shock protein 70 activity. J. Biol. Chem. 274, 3797–3803 (1999).
  Article CAS PubMed Google Scholar
• Polyak, S. J., Tang, N., Wambach, M., Barber, G. N. & Katze, M. G. The P58 cellular inhibitor complexes with the interferon-induced, double-stranded RNA-dependent protein kinase, PKR, to regulate its autophosphorylation and activity. J. Biol. Chem. 271, 1702–1707 (1996).
  Article CAS PubMed Google Scholar
• Wang, X. Z. et al. Signals from the stressed endoplasmic reticulum induce C/EBP-homologous protein (CHOP/GADD153). Mol. Cell. Biol. 16, 4273–4280 (1996).
  Article CAS PubMed PubMed Central Google Scholar
• Geiss, G. K. et al. Cellular transcriptional profiling in influenza virus-infected lung epithelial cells: the role of the nonstructural NS1 protein in the evasion of the host innate defense and its potential contribution to pandemic influenza. Proc. Natl Acad. Sci. USA 99, 10736–10741 (2002).This study examined the effects of NS1 protein expression during influenza A virus infection on global cellular mRNA levels using high-density microarrays. It indicated that the cellular IFN response to influenza A virus infection in lung epithelial cells is influenced markedly by the sequence of the NS1 gene, and it characterized a virus that contains the 1918 pandemic influenza NS1 gene.
  Article CAS PubMed PubMed Central Google Scholar
• Krebs, D. L. & Hilton, D. J. SOCS proteins: negative regulators of cytokine signaling. Stem Cells 19, 378–387 (2001).
  Article CAS PubMed Google Scholar
• He, Y. & Katze, M. G. To interfere and to anti-interfere: the interplay between hepatitis C virus and interferon. Viral Immunol. 15, 95–119 (2002).
  Article CAS PubMed Google Scholar
• Tan, S. L. & Katze, M. G. How hepatitis C virus counteracts the interferon response: the jury is still out on NS5A. Virology 284, 1–12 (2001).
  Article CAS PubMed Google Scholar
• Taylor, D. R. Hepatitis C virus and interferon resistance: it's more than just PKR. Hepatology 33, 1547–1549 (2001).
  Article CAS PubMed Google Scholar
• Bartenschlager, R. & Lohmann, V. Novel cell-culture systems for the hepatitis C virus. Antiviral Res. 52, 1–17 (2001).
  Article CAS PubMed Google Scholar
• Gale, M. Jr & Beard, M. R. Molecular clones of hepatitis C virus: applications to animal models. ILAR J. 42, 139–151 (2001).
  Article PubMed Google Scholar
• Pawlotsky, J. M. Hepatitis C virus resistance to antiviral therapy. Hepatology 32, 889–896 (2000).
  Article CAS PubMed Google Scholar
• Bukh, J., Miller, R. H. & Purcell, R. H. Genetic heterogeneity of hepatitis C virus: quasispecies and genotypes. Semin. Liver Dis. 15, 41–63 (1995).
  Article CAS PubMed Google Scholar
• Enomoto, N. et al. Comparison of full-length sequences of interferon-sensitive and -resistant hepatitis C virus 1b. Sensitivity to interferon is conferred by amino-acid substitutions in the NS5A region. J. Clin. Invest. 96, 224–230 (1995).
  Article CAS PubMed PubMed Central Google Scholar
• Enomoto, N. et al. Mutations in the nonstructural protein 5A gene and response to interferon in patients with chronic hepatitis C virus 1b infection. N. Engl. J. Med. 334, 77–81 (1996).This study analysed the HCV NS5A ISDR sequences in patients with chronic HCV1b infection before and after IFN therapy, and concluded that there was a substantial correlation between responses to IFN and mutations in the NS5A gene.
  Article CAS PubMed Google Scholar
• Nakano, I. et al. Why is the interferon sensitivity-determining region (ISDR) system useful in Japan? J. Hepatol. 30, 1014–1022 (1999).
  Article CAS PubMed Google Scholar
• Witherell, G. W. & Beineke, P. Statistical analysis of combined substitutions in nonstructural 5A region of hepatitis C virus and interferon response. J. Med. Virol. 63, 8–16 (2001).
  Article CAS PubMed Google Scholar
• Lohmann, V. et al. Replication of subgenomic hepatitis C virus RNAs in a hepatoma cell line. Science 285, 110–113 (1999).
  Article CAS PubMed Google Scholar
• Blight, K. J., Kolykhalov, A. A. & Rice, C. M. Efficient initiation of HCV RNA replication in cell culture. Science 290, 1972–1974 (2000).
  Article CAS PubMed Google Scholar
• Frese, M., Pietschmann, T., Moradpour, D., Haller, O. & Bartenschlager, R. Interferon-α inhibits hepatitis C virus subgenomic RNA replication by an MxA-independent pathway. J. Gen. Virol. 82, 723–733 (2001).
  Article CAS PubMed Google Scholar
• Guo, J. T., Bichko, V. V. & Seeger, C. Effect of α-interferon on the hepatitis C virus replicon. J. Virol. 75, 8516–8523 (2001).
  Article CAS PubMed PubMed Central Google Scholar
• Sumpter, R. Jr & Gale, M. Jr. in American Society for Virology 21st Annual Meeting W33-3 (Lexington, Kentucky, 2002).
  Google Scholar
• Whitley, R. J. in Fields Virology (eds Knipe, D. M. & Howley, P. M.) 2461–2509 (Lippincott, Williams & Wilkins, Philadelphia, 2001).
  Google Scholar
• Tan, S. L. & Katze, M. G. HSV.com: maneuvering the internetworks of viral neuropathogenesis and evasion of the host defense. Proc. Natl Acad. Sci. USA 97, 5684–5686 (2000).
  Article CAS PubMed PubMed Central Google Scholar
• Roizman, B. & Knipe, D. M. in Fields Virology (eds Knipe, D. M. & Howley, P. M.) 2399–2460 (Lippincott, Williams & Wilkins, Philadelphia, 2001).
  Google Scholar
• Ankel, H., Westra, D. F., Welling-Wester, S. & Lebon, P. Induction of interferon-α by glycoprotein D of herpes simplex virus: a possible role of chemokine receptors. Virology 251, 317–326 (1998).
  Article CAS PubMed Google Scholar
• Kumar-Sinha, C., Varambally, S., Sreekumar, A. & Chinnaiyan, A. M. Molecular cross-talk between the TRAIL and interferon signaling pathways. J. Biol. Chem. 277, 575–585 (2002).
  Article CAS PubMed Google Scholar
• Preston, C. M., Harman, A. N. & Nicholl, M. J. Activation of interferon response factor-3 in human cells infected with herpes simplex virus type 1 or human cytomegalovirus. J. Virol. 75, 8909–8916 (2001).
  Article CAS PubMed PubMed Central Google Scholar
• Eidson, K. M., Hobbs, W. E., Manning, B. J., Carlson, P. & DeLuca, N. A. Expression of herpes simplex virus ICP0 inhibits the induction of interferon-stimulated genes by viral infection. J. Virol. 76, 2180–2191 (2002).
  Article CAS PubMed PubMed Central Google Scholar
• Mossman, K. L. & Smiley, J. R. Herpes simplex virus ICP0 and ICP34.5 counteract distinct interferon-induced barriers to virus replication. J. Virol. 76, 1995–1998 (2002).
  Article CAS PubMed PubMed Central Google Scholar
• Harle, P., Sainz, B. Jr, Carr, D. J. & Halford, W. P. The immediate-early protein, ICP0, is essential for the resistance of herpes simplex virus to interferon-α/β. Virology 293, 295–304 (2002).
  Article PubMed CAS Google Scholar
• He, B., Gross, M. & Roizman, B. The γ(1)34.5 protein of herpes simplex virus 1 complexes with protein phosphatase 1α to dephosphorylate the α-subunit of the eukaryotic translation initiation factor 2 and preclude the shutoff of protein synthesis by double-stranded RNA-activated protein kinase. Proc. Natl Acad. Sci. USA 94, 843–848 (1997).This study indicated a unique mechanism by which HSV γ(1)34.5 interacts with and redirects protein phosphatase 1α to dephosphorylate eIF-2α to allow continued protein synthesis despite the presence of activated PKR.
  Article CAS PubMed PubMed Central Google Scholar
• Cassady, K. A. & Gross, M. The herpes simplex virus type 1 U(S)11 protein interacts with protein kinase R in infected cells and requires a 30-amino-acid sequence adjacent to a kinase substrate domain. J. Virol. 76, 2029–2035 (2002).
  Article CAS PubMed PubMed Central Google Scholar
• Leib, D. A., Machalek, M. A., Williams, B. R., Silverman, R. H. & Virgin, H. W. Specific phenotypic restoration of an attenuated virus by knockout of a host resistance gene. Proc. Natl Acad. Sci. USA 97, 6097–6101 (2000).Using recombinant viruses to infect animals that have null mutations in host-defence genes, this study showed that a virus that was attenuated by deletion of ICP34.5 showed wild-type replication and virulence in a host from which the PKR gene had been deleted, exemplifying a formal genetic test for identifying in vivo mechanisms and targets of microbial virulence genes.
  Article CAS PubMed PubMed Central Google Scholar
• Poppers, J., Mulvey, M., Khoo, D. & Mohr, I. Inhibition of PKR activation by the proline-rich RNA-binding domain of the herpes simplex virus type 1 US11 protein. J. Virol. 74, 11215–11221 (2000).
  Article CAS PubMed PubMed Central Google Scholar
• Esposito, J. J. & Fenner, F. in Fields Virology (eds Knipe, D. M. & Howley, P. M.) 2849–2884 (Lippincott, Williams & Wilkins, Philadelphia, 2001).
  Google Scholar
• Moss, B. in Fields Virology (eds Knipe, D. M. & Howley, P. M.) 2885–2922 (Lippincott, Williams & Wilkins, Philadelphia, 2001).
  Google Scholar
• Cohen, J. Bioterrorism. Smallpox vaccinations: how much protection remains? Science 294, 985 (2001).
  Article CAS PubMed Google Scholar
• Smith, G. L. & McFadden, G. Smallpox: anything to declare? Nature Rev. Immunol. 2, 521–527 (2002).
  Article CAS Google Scholar
• Alcami, A. & Smith, G. L. Receptors for γ-interferon encoded by poxviruses: implications for the unknown origin of vaccinia virus. Trends Microbiol. 4, 321–326 (1996).
  Article CAS PubMed Google Scholar
• Alcami, A. & Smith, G. L. Soluble interferon-α receptors encoded by poxviruses. Comp. Immunol. Microbiol. Infect. Dis. 19, 305–317 (1996).
  Article CAS PubMed Google Scholar
• McFadden, G. & Murphy, P. M. Host-related immunomodulators encoded by poxviruses and herpesviruses. Curr. Opin. Microbiol. 3, 371–378 (2000).
  Article CAS PubMed Google Scholar
• Lalani, A. S. et al. Use of chemokine receptors by poxviruses. Science 286, 1968–1971 (1999).
  Article CAS PubMed Google Scholar
• Alcami, A. & Smith, G. L. Vaccinia, cowpox and camelpox viruses encode soluble γ-interferon receptors with novel broad species specificity. J. Virol. 69, 4633–4639 (1995).
  CAS PubMed PubMed Central Google Scholar
• Alcami, A. & Smith, G. L. Cytokine receptors encoded by poxviruses: a lesson in cytokine biology. Immunol. Today 16, 474–478 (1995).
  Article CAS PubMed Google Scholar
• McFadden, G., Lalani, A., Everett, H., Nash, P. & Xu, X. Virus-encoded receptors for cytokines and chemokines. Semin. Cell Dev. Biol. 9, 359–368 (1998).
  Article CAS PubMed Google Scholar
• Colamonici, O. R., Domanski, P., Sweitzer, S. M., Larner, A. & Buller, R. M. Vaccinia virus B18R gene encodes a type I interferon-binding protein that blocks interferon-α transmembrane signaling. J. Biol. Chem. 270, 15974–15978 (1995).
  Article CAS PubMed Google Scholar
• Symons, J. A., Alcami, A. & Smith, G. L. Vaccinia virus encodes a soluble type I interferon receptor of novel structure and broad species specificity. Cell 81, 551–560 (1995).This study characterized the vaccinia-virus soluble type I IFN receptor encoded by the B18R gene, which has broad species specificity and might have aided vaccinia-virus replication in many host species during evolution.
  Article CAS PubMed Google Scholar
• Verardi, P. H., Jones, L. A., Aziz, F. H., Ahmad, S. & Yilma, T. D. Vaccinia virus vectors with an inactivated γ-interferon receptor homolog gene (B8R) are attenuated in vivo without a concomitant reduction in immunogenicity. J. Virol. 75, 11–18 (2001).
  Article CAS PubMed PubMed Central Google Scholar
• Sroller, V., Ludvikova, V., Maresova, L., Hainz, P. & Nemeckova, S. Effect of IFN-γ receptor gene deletion on vaccinia-virus virulence. Arch. Virol. 146, 239–249 (2001).
  Article CAS PubMed Google Scholar
• Akkaraju, G. R., Whitaker-Dowling, P., Youngner, J. S. & Jagus, R. Vaccinia-specific kinase inhibitory factor prevents translational inhibition by double-stranded RNA in rabbit reticulocyte lysate. J. Biol. Chem. 264, 10321–10325 (1989).
  CAS PubMed Google Scholar
• Watson, J. C., Chang, H. W. & Jacobs, B. L. Characterization of a vaccinia virus-encoded double-stranded RNA-binding protein that may be involved in inhibition of the double-stranded RNA-dependent protein kinase. Virology 185, 206–216 (1991).
  Article CAS PubMed Google Scholar
• Chang, H. W., Watson, J. C. & Jacobs, B. L. The E3L gene of vaccinia virus encodes an inhibitor of the interferon-induced, double-stranded RNA-dependent protein kinase. Proc. Natl Acad. Sci. USA 89, 4825–4829 (1992).
  Article CAS PubMed PubMed Central Google Scholar
• Beattie, E., Paoletti, E. & Tartaglia, J. Distinct patterns of IFN sensitivity observed in cells infected with vaccinia K3L- and E3L-mutant viruses. Virology 210, 254–263 (1995).
  Article CAS PubMed Google Scholar
• Beattie, E., Tartaglia, J. & Paoletti, E. Vaccinia virus-encoded eIF-2α homolog abrogates the antiviral effect of interferon. Virology 183, 419–422 (1991).
  Article CAS PubMed Google Scholar
• Davies, M. V., Elroy-Stein, O., Jagus, R., Moss, B. & Kaufman, R. J. The vaccinia virus K3L gene product potentiates translation by inhibiting double-stranded-RNA-activated protein kinase and phosphorylation of the α-subunit of eukaryotic initiation factor 2. J. Virol. 66, 1943–1950 (1992).
  CAS PubMed PubMed Central Google Scholar
• Massung, R. F. et al. Analysis of the complete genome of smallpox variola major virus strain Bangladesh-1975. Virology 201, 215–240 (1994).
  Article CAS PubMed Google Scholar
• Shchelkunov, S. N. et al. Comparison of the genetic maps of variola and vaccinia viruses. FEBS Lett. 327, 321–324 (1993).
  Article CAS PubMed Google Scholar
• Davies, M. V., Chang, H. W., Jacobs, B. L. & Kaufman, R. J. The E3L and K3L vaccinia virus gene products stimulate translation through inhibition of the double-stranded RNA-dependent protein kinase by different mechanisms. J. Virol. 67, 1688–1692 (1993).
  CAS PubMed PubMed Central Google Scholar
• Sharp, T. V. et al. The vaccinia virus E3L gene product interacts with both the regulatory and the substrate-binding regions of PKR: implications for PKR autoregulation. Virology 250, 302–315 (1998).
  Article CAS PubMed Google Scholar
• Carroll, K., Elroy-Stein, O., Moss, B. & Jagus, R. Recombinant vaccinia virus K3L gene product prevents activation of double-stranded RNA-dependent, initiation factor 2α-specific protein kinase. J. Biol. Chem. 268, 12837–12842 (1993).
  CAS PubMed Google Scholar
• Rivas, C., Gil, J., Melkova, Z., Esteban, M. & Diaz-Guerra, M. Vaccinia virus E3L protein is an inhibitor of the interferon (IFN)-induced 2–5A synthetase enzyme. Virology 243, 406–414 (1998).
  Article CAS PubMed Google Scholar
• Smith, E. J., Marie, I., Prakash, A., Garcia-Sastre, A. & Levy, D. E. IRF3 and IRF7 phosphorylation in virus-infected cells does not require double-stranded RNA-dependent protein kinase R or IκB kinase but is blocked by vaccinia virus E3L protein. J. Biol. Chem. 276, 8951–8957 (2001).
  Article CAS PubMed Google Scholar
• Liu, Y., Wolff, K. C., Jacobs, B. L. & Samuel, C. E. Vaccinia virus E3L interferon resistance protein inhibits the interferon-induced adenosine deaminase A-to-I editing activity. Virology 289, 378–387 (2001).
  Article CAS PubMed Google Scholar
• Brandt, T. A. & Jacobs, B. L. Both carboxy- and amino-terminal domains of the vaccinia virus interferon resistance gene, E3L, are required for pathogenesis in a mouse model. J. Virol. 75, 850–856 (2001).
  Article CAS PubMed PubMed Central Google Scholar
• Najarro, P., Traktman, P. & Lewis, J. A. Vaccinia virus blocks γ-interferon signal transduction: viral VH1 phosphatase reverses Stat1 activation. J. Virol. 75, 3185–3196 (2001).
  Article CAS PubMed PubMed Central Google Scholar
• Cummings, C. A. & Relman, D. A. Using DNA microarrays to study host–microbe interactions. Emerg. Infect. Dis. 6, 513–525 (2000).
  Article CAS PubMed PubMed Central Google Scholar
• Fruh, K., Simmen, K., Luukkonen, B. G., Bell, Y. C. & Ghazal, P. Virogenomics: a novel approach to antiviral drug discovery. Drug Discov. Today 6, 621–627 (2001).
  Article CAS PubMed Google Scholar
• Manger, I. D. & Relman, D. A. How the host 'sees' pathogens: global gene expression responses to infection. Curr. Opin. Immunol. 12, 215–218 (2000).
  Article CAS PubMed Google Scholar
• Dongre, A. R., Opiteck, G., Cosand, W. L. & Hefta, S. A. Proteomics in the post-genome age. Biopolymers 60, 206–211 (2001).
  Article CAS PubMed Google Scholar
• Uetz, P. et al. A comprehensive analysis of protein–protein interactions in Saccharomyces cerevisiae. Nature 403, 623–627 (2000).
  Article CAS PubMed Google Scholar
• Kellam, P. Post-genomic virology: the impact of bioinformatics, microarrays and proteomics on investigating host and pathogen interactions. Rev. Med. Virol. 11, 313–329 (2001).
  Article CAS PubMed Google Scholar
• Ideker, T., Galitski, T. & Hood, L. A new approach to decoding life: systems biology. Annu. Rev. Genomics Hum. Genet. 2, 343–372 (2001).
  Article CAS PubMed Google Scholar
• Ideker, T. et al. Integrated genomic and proteomic analyses of a systematically perturbed metabolic network. Science 292, 929–934 (2001).
  Article CAS PubMed Google Scholar
• Simmen, K. A. et al. Global modulation of cellular transcription by human cytomegalovirus is initiated by viral glycoprotein B. Proc. Natl Acad. Sci. USA 98, 7140–7145 (2001).Using high-density microarrays, this study identified the specific viral component that triggers the cellular IFN response as the envelope glycoprotein B (gB), highlighting a pioneering paradigm for the consequences of virus–receptor interactions.
  Article CAS PubMed PubMed Central Google Scholar
• Mossman, K. L. et al. Herpes simplex virus triggers and then disarms a host antiviral response. J. Virol. 75, 750–758 (2001).
  Article CAS PubMed PubMed Central Google Scholar
• Geiss, G. K. et al. Global impact of influenza virus on cellular pathways is mediated by both replication-dependent and -independent events. J. Virol. 75, 4321–4331 (2001).
  Article CAS PubMed PubMed Central Google Scholar
• Geiss, G. et al. A comprehensive view of regulation of gene expression by double-stranded RNA-mediated cell signaling. J. Biol. Chem. 276, 30178–30182 (2001).
  Article CAS PubMed Google Scholar
• Gale, M. Jr et al. Control of PKR protein kinase by hepatitis C virus nonstructural 5A protein: molecular mechanisms of kinase regulation. Mol. Cell. Biol. 18, 5208–5218 (1998).This study investigated the mechanisms of NS5A-mediated PKR regulation and the effect of ISDR mutations on this regulatory process, and proposed a model of PKR regulation by NS5A, which might have implications for therapeutic strategies against HCV.
  Article CAS PubMed PubMed Central Google Scholar
• Gale, M. J. Jr et al. Evidence that hepatitis C virus resistance to interferon is mediated through repression of the PKR protein kinase by the nonstructural 5A protein. Virology 230, 217–227 (1997).
  Article CAS PubMed Google Scholar
• Noguchi, T. et al. Effects of mutation in hepatitis C virus nonstructural protein 5A on interferon resistance mediated by inhibition of PKR kinase activity in mammalian cells. Microbiol. Immunol. 45, 829–840 (2001).
  Article CAS PubMed Google Scholar
• Polyak, S. J. et al. Hepatitis C virus nonstructural 5A protein induces interleukin-8, leading to partial inhibition of the interferon-induced antiviral response. J. Virol. 75, 6095–6106 (2001).
  Article CAS PubMed PubMed Central Google Scholar
• Girard, S. et al. An altered cellular response to interferon and up-regulation of interleukin-8 induced by the hepatitis C viral protein NS5A uncovered by microarray analysis. Virology 295, 272–283 (2002).
  Article CAS PubMed Google Scholar
• Bigger, C. B., Brasky, K. M. & Lanford, R. E. DNA microarray analysis of chimpanzee liver during acute resolving hepatitis C virus infection. J. Virol. 75, 7059–7066 (2001).
  Article CAS PubMed PubMed Central Google Scholar
• Toshchakov, V. et al. TLR4, but not TLR2, mediates IFN-β-induced STAT1α/β-dependent gene expression in macrophages. Nature Immunol. 3, 392–398 (2002).This study highlighted the cross-talk between TLRs and IFN — two pivotal host anti-microbial pathways — and provided the first explanation for the mechanistic basis of the differential patterns of gene expression that are activated by different TLR agonists.
  Article CAS Google Scholar
• Mita, Y., Dobashi, K., Shimizu, Y., Nakazawa, T. & Mori, M. Toll-like receptor 2 and 4 surface expressions on human monocytes are modulated by interferon-γ and macrophage colony-stimulating factor. Immunol. Lett. 78, 97–101 (2001).
  Article CAS PubMed Google Scholar
• Miettinen, M., Sareneva, T., Julkunen, I. & Matikainen, S. IFNs activate toll-like receptor gene expression in viral infections. Genes Immun. 2, 349–355 (2001).
  Article CAS PubMed Google Scholar
• Aderem, A. & Ulevitch, R. J. Toll-like receptors in the induction of the innate immune response. Nature 406, 782–787 (2000).
  Article CAS PubMed Google Scholar
• Alexopoulou, L., Holt, A. C., Medzhitov, R. & Flavell, R. A. Recognition of double-stranded RNA and activation of NF-κB by Toll-like receptor 3. Nature 413, 732–738 (2001).This study showed that mammalian TLR3 recognizes dsRNA and TLR3 activation induces type I IFN production. It was also found that TLR3-deficient mice have reduced responses to poly(inosine:cytosine).
  Article CAS PubMed Google Scholar
• Zhou, A., Paranjape, J. M., Der, S. D., Williams, B. R. & Silverman, R. H. Interferon action in triply deficient mice reveals the existence of alternative antiviral pathways. Virology 258, 435–440 (1999).
  Article CAS PubMed Google Scholar
• Horng, T., Barton, G. M. & Medzhitov, R. TIRAP: an adapter molecule in the Toll signaling pathway. Nature Immunol. 2, 835–841 (2001).
  Article CAS Google Scholar
• O'Shea, J. J., Gadina, M. & Schreiber, R. D. Cytokine signaling in 2002: new surprises in the Jak/Stat pathway. Cell 109, S121–S131 (2002).
  Article CAS PubMed Google Scholar
• Aaronson, D. S. & Horvath, C. M. A road map for those who know JAK–STAT. Science 296, 1653–1655 (2002).
  Article CAS PubMed Google Scholar
• Heim, M. H. The Jak–STAT pathway: cytokine signalling from the receptor to the nucleus. J. Recept. Signal Transduct. Res. 19, 75–120 (1999).
  Article CAS PubMed Google Scholar
• Yeh, T. C. & Pellegrini, S. The Janus kinase family of protein tyrosine kinases and their role in signaling. Cell. Mol. Life Sci. 55, 1523–1534 (1999).
  Article CAS PubMed Google Scholar
• Meraz, M. A. et al. Targeted disruption of the Stat1 gene in mice reveals unexpected physiologic specificity in the JAK–STAT signaling pathway. Cell 84, 431–442 (1996).This study generated and characterized Stat1-deficient mice, which have a complete lack of response to IFNs and are highly sensitive to microbial and viral infection, showing that STAT1 has an obligate and dedicated role in mediating IFN-dependent biological responses.
  Article CAS PubMed Google Scholar
• Cox, N. J. & Subbarao, K. Global epidemiology of influenza: past and present. Annu. Rev. Med. 51, 407–421 (2000).
  Article CAS PubMed Google Scholar
• Patterson, K. D. & Pyle, G. F. The geography and mortality of the 1918 influenza pandemic. Bull. Hist. Med. 65, 4–21 (1991).
  CAS PubMed Google Scholar
• Basler, C. F. et al. Sequence of the 1918 pandemic influenza virus nonstructural gene (NS) segment and characterization of recombinant viruses bearing the 1918 NS genes. Proc. Natl Acad. Sci. USA 98, 2746–2751 (2001).By generating recombinant influenza viruses from cloned cDNAs, the group tested the 1918 pandemic flu NS1 gene in a mouse model. The results indicate that interaction of the NS1 protein with host-cell factors is important for viral pathogenesis.
  Article CAS PubMed PubMed Central Google Scholar
• Taubenberger, J. K., Reid, A. H., Janczewski, T. A. & Fanning, T. G. Integrating historical, clinical and molecular genetic data in order to explain the origin and virulence of the 1918 Spanish influenza virus. Phil. Trans. R. Soc. Lond. B 356, 1829–1839 (2001).
  Article CAS Google Scholar
• Patten, P. A., Howard, R. J. & Stemmer, W. P. Applications of DNA shuffling to pharmaceuticals and vaccines. Curr. Opin. Biotechnol. 8, 724–733 (1997).
  Article CAS PubMed Google Scholar
• Harayama, S. Artificial evolution by DNA shuffling. Trends Biotechnol. 16, 76–82 (1998).
  Article CAS PubMed Google Scholar
• Pekrun, K. et al. Evolution of a human immunodeficiency virus type 1 variant with enhanced replication in pig-tailed macaque cells by DNA shuffling. J. Virol. 76, 2924–2935 (2002).
  Article CAS PubMed PubMed Central Google Scholar
• Chang, C. C. et al. Evolution of a cytokine using DNA family shuffling. Nature Biotechnol. 17, 793–797 (1999).This study used DNA shuffling of a family of human IFN-α genes to derive variants that have increased antiviral activities in mouse cells, and showed that diverse cytokine gene families can be used as starting material to rapidly evolve cytokines that are more active than the native form.
  Article CAS Google Scholar
• Weber, H., Valenzuela, D., Lujber, G., Gubler, M. & Weissmann, C. Single amino-acid changes that render human IFN-α2 biologically active on mouse cells. EMBO J. 6, 591–598 (1987).
  Article CAS PubMed PubMed Central Google Scholar