Effect of deoxynojirimycin derivatives on morphogenesis of hepatitis C virus

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• 作者：A. V. Timokhova (1)
  L. V. Bakinovskii (2)
  A. I. Zinin (2)
  V. I. Popenko (1)
  A. V. Ivanov (1)
  P. M. Rubtsov (1)
  S. N. Kochetkov (1)
  S. N. Belzhelarskaya (1) belj@eimb.ru
• 关键词：baculovirus AcMNPV – ; hepatitis C virus (HCV) – ; HCV structural proteins – ; HCV glycoproteins – ; HCV ; like particles (VLPs) – ; Sf9 insect cells – ; deoxynojirimycin (DNJ) – ; NBnDNJ – ; NPnDNJ – ; NBDNJ – ; α ; glucosidase – ; calnexin – ; calreticulin
• 刊名：Molecular Biology
• 出版年：2012
• 出版时间：July 2012
• 年：2012
• 卷：46
• 期：4
• 页码：579-587
• 全文大小：482.0 KB
• 参考文献：1. Chou R., Clark E., Helfand M. 2004. Screening for hepatitis C virus infection: A reiew of the evidence for the U.S. Preventive Services Task Force. Ann. Intern. Med. 140, 465–479.
  2. Durantel D., Carrouee-Durantel S., Branza-Nichita N., Dwek R.A., Zitzmann N. 2004. Effects of interferon, ribavirin, and iminosugar derivatives on cells persistently infected with noncytopathic bovine viral diarrhea virus. Antimicrob. Agents Chemother. 48, 497–504.
  3. Fried M.W., Shiffman M.L., Reddy K.R., et al. 2002. Peginterferon alfa-2a plus ribavirin for chronic hepatitis C virus infection. N. Engl. J. Med. 347, 975–982.
  4. Dudley T., O’Donnell K., Haydon G., Mutimer D. 2006. Disappointing results of combination therapy for HCV. Gut. 55, 1362–1363.
  5. El-Gogo S., Staib C., Lasarte J.J., Sutter G., Adler H. 2008. Protective vaccination with hepatitis C virus NS3 but not core antigen in a novel mouse challenge model. J. Gene Med. 10, 177–186.
  6. Reed K.E., Rice C.M. 2000. Overview of hepatitis C virus genome structure, polyprotein processing and protein properties. Curr. Top. Microbiol. Immunol. 242, 55–84.
  7. Ivanov A.V., Kuzyakin A.O., Kochetkov S.N. 2005. Molecular biology of hepatitis C virus. Usp. Biokhim. 45, 37–86.
  8. Karpas A., Fleet G.W., Dwek R.A., Petursson S., Namgoong S.K., Ramsden N.G., Jacob G.S., Rademacher T.W. 1988. Aminosugar derivatives as potential anti-immunodeficiency virus agents. Proc. Natl. Acad. Sci. U. S. A. 85, 9229–9233.
  9. Courageot M.-P., Frenkiel M.-P., Dos Santos C.-D., Deubel V., Despr猫s Ph. 2000. α-Glucosidase inhibitors reduce dengue virus production by affecting the initial steps of virion morphogenesis in the endoplasmic reticulum. J. Virol. 74, 564–572.
  10. Durantel D., Branza-Nichita N., Carrouee-Durantel S., Butters T.D., Dwek R.A., Zitzmann N. 2001. Study of the mechanism of antiviral action of iminosugar derivatives against bovine viral diarrhea virus. J. Virol. 75, 8987–8998.
  11. Branza-Nichita N., Durantel D., Carrouee-Durantel S., Dwek R.A., Zitzmann N. 2001. Antiviral effect of N-butyldeoxynojirimycin against bovine viral diarrhea virus correlates with misfolding of E2 envelope proteins and impairment of their association into E1-E2 heterodimers. J. Virol. 75, 3527–3536.
  12. Chapel C., Garcia C., Bartosch B., et al. 2007. Reduction of the infectivity of hepatitis C virus pseudoparticles by incorporation of misfolded glycoproteins induced by glucosidase inhibitors. J. Gen. Virol. 88, 1133–1143.
  13. Chapel C., Garcia C., Roingeard Ph., Zitzmann N., Dubuisson J., et al. 2006. Antiviral effect of α-glucosidase inhibitors on viral morphogenesis and binding properties of hepatitis C virus-like particles. J. Gen. Virol. 87, 861–871.
  14. Helle F., Goffard A., Morel V., Duverlie G., McKeating J., Keck Z.-Y., Foung S., Penin F., Dubuisson J., Voisset C. 2007. The neutralizing activity of anti-hepatitis C virus antibodies is modulated by specific glycans on the E2 envelope protein. J. Virol. 81, 8101–8111.
  15. Baumert T.F., Ito S., Wong D.T., Liang T.J. 1998. Hepatitis C virus structural proteins assemble into virus-like particles in insect cells. J. Virol. 72, 3827–3836.
  16. Choo Q.L., Kuo G., Weiner A.J., Overby L.R., Bradley D.W., Houghton M. 1989. Isolation of a cDNA clone derived from blood-borne non-A, non-B viral hepatitis genome. Science. 244, 359–362.
  17. Dubuisson J., Rice C.M. 1996. Hepatitis C virus glycoprotein folding: Disulfide bond formation and association with calnexin. J. Virol. 70, 778–786.
  18. Kornfeld R., Kornfeld S. 1985. Assembly of asparagine-linked oligosaccharides. Annu. Rev. Biochem. 54, 631–664.
  19. Yanjie Li., Wenxia F., Lei Zh., Haomiao O., Hui Zh., Yuanming Luo, Cheng Jin1. 2009. Class IIC α-mannosidase AfAms1 is required for morphogenesis and cellular function in Aspergillus fumigates. Yanjie Glycobiol. 19, 624–632.
  20. Glycoproteins: The History of Glycoprotein Research, Personal View. 1995. Eds. Montreuil J., Vliegenthart J.F., Schachter H. Amsterdam: Elsevier, pp.1–12.
  21. Jones D.M., McLauchlan J. 2010. Hepatitis C virus: Assembly and release of virus particles J. Biol. Chem. 285, 22733–22739.
  22. Burda P., Aebi M. 1999 The dolichol pathway of N-linked glycosylation. Biochim. Biophys. Acta. 1426, 239–257.
  23. Trombetta E.S. 2003. The contribution of N-glycans and their processing in the endoplasmic reticulum to glycoprotein biosynthesis. Glycobiology. 13, 77R–91R
  24. Kornfeld R., Kornfeld S. 1985. Assembly of asparagine-linked oligosaccharides. Annu. Rev. Biochem. 54, 631–664.
  25. Goldman C., Petry H., Frye S., et al. 1999. Molecular cloning and expression of major structural protein VP1 of the human polyomavirus JC virus: Formation of virus-like particles useful for immunological and therapeutic studies. J. Virol. 73, 4465–4469.
  26. Xiang J., Wunschmann S., George S.L., Klinzman D., Schmidt W.N., LaBrecque D.R., Stapleton J.T. 2002. Recombinant hepatitis C virus-like particles, expressed by baculovirus: Utility in cell-binding and antibody detection assays. J. Med. Virol. 68, 537–43.
  27. Maniatis T., Fritsch E.F., Sambrook J. 1982. Molecular Cloning: A Laboratory Manual. Cold Spring Harbor, NY: Cold Spring Harbor Lab. Press.
  28. Bac-to-Bac Baculovirus Expression System: Instruction Manual. 1993. St. Louis, MO: Life Technologies, Inc.
  29. Belzhelarskaya S.N., Koroleva N.N., Popenko V.I., Drutza V.L., Orlova O.V., Rubtzov P.M., Kochetkov S.N. 2010. Hepatitis C virus structural proteins and virus-like particles produced in recombinant baculovirus-infected insect cells. Mol. Biol. (Moscow). 44, 97–108.
  30. King L.A., Possee R.D. 1992. The Baculovirus Expression System: a Laboratory Guide. London: Chapman and Hall.
  31. Borenfreund E., Babich H., Martin-Alguacil N. 1988. Comparisons of two in vitro cytotoxicity assay: The Neutral Red (NR) and tetrazolium MTT tests. Toxicol. in vitro. 2, 1–6.
  32. Borenfreund E., Puerner J.A. 1985. Toxicity determined in vitro by morphological alterations and neutral red absorption. Toxicol. Lett. 24, 119–124.
  33. Medzihradsky F., Marks M.J. 1975. Measures of viability in isolated cells. Biochem. Med. 13, 164–177.
  34. Mokhonov V.V., Novikov D.V., Samokhvalov E.I., Shatalov A.G., Selivanov N.A., Prilipov A.G., L’vov D.K. 2002. Genome analysis of hepatitis C virus strain 274933RU, isolated in Russian Federation. Vopr. Virusol. 47, 9–12.
  35. Ke A., Gillock E.T., Sweat J.A., Reeves W.M., Consigli R.A. 1999. Use of baculovirus system to assemble polyomavirus capsid-like particles with different polyomavirus structural proteins: analysis of the recombinant assembled capsid-like particles. J. Gen. Virol. 80, 1009–1016.
• 作者单位：1. Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, 119991 Russia2. Zelinskii Institute of Organic Chemistry, Russian Academy of Sciences, Moscow, 119991 Russia
• ISSN：1608-3245

文摘

Viral hepatitis C is a dangerous, widespread human disease. The choice of drugs for treatment of chronic hepatitis C virus (HCV) infection is limited, and prophylactic vaccines do not exist. Thus, the development of new antiviral strategies and substances is an issue of great importance. The targeting of viral morphogenesis might be used as an alternative approach to existing strategies of HCV blocking. The glycosylation of viral envelope proteins is an important step of viral particle morphogenesis, which determines the correct assembly of HCV virions. Derivatives of a glucose analog deoxynojirimycin (DNJ) act as an α-glucosidase inhibitor and can impair the assembly of structural proteins and HCV particle formation. In the present work, the effects of alkylated DNJ derivatives, N-pentyl-DNJ and N-benzyl-DNJ, on HCV morphogenesis were studied in a model system of insect cells that produce three viral structural proteins with the formation of virus-like particles. It was shown that DNJ derivatives impair the intracellular N-glycosylation of HCV envelope glycoproteins. At the concentration of 1 mM, these substances cause an increase in the levels of gpE1 and gpE2 glycoproteins and a decrease in their electrophoretic mobility, apparently due to the inhibition of α-glucosidase in the endoplasmic reticulum and the accumulation of hyperglycosylated N-glycans in HCV glycoproteins. The interaction of the latter with calnexin results in the formation of unproductive dimers and blocks the productive assembly of virus-like particles.