A structural perspective of the flavivirus life cycle (original) (raw)
Kuno, G., Chang, G. J., Tsuchiya, K. R., Karabatsos, N. & Cropp, C. B. Phylogeny of the genus Flavivirus. J. Virol.72, 73–83 (1998). CASPubMedPubMed Central Google Scholar
Lindenbach, B. D. & Rice, C. M. in Fields Virology (eds Knipe, D. M. & Howley, P. M.) 991–1041 (Lippincott Williams & Wilkins, Philadelphia, 2001). Google Scholar
Burke, D. S. & Monath, T. P. in Fields Virology (eds Knipe, D. M. & Howley, P. M.) 1043–1125 (Lippincott Williams & Wilkins, Philadelphia, 2001). Google Scholar
Gubler, D. J. Epidemic dengue/dengue hemorrhagic fever as a public health, social and economic problem in the 21st century. Trends Microbiol.10, 100–103 (2002). ArticleCASPubMed Google Scholar
Lorenz, I. C., Allison, S. L., Heinz, F. X. & Helenius, A. Folding and dimerization of tick-borne encephalitis virus envelope proteins prM and E in the endoplasmic reticulum. J. Virol.76, 5480–5491 (2002). ArticleCASPubMedPubMed Central Google Scholar
Stadler, K., Allison, S. L., Schalich, J. & Heinz, F. X. Proteolytic activation of tick-borne encephalitis virus by furin. J. Virol.71, 8475–8481 (1997). Demonstrates that prM is cleaved by furin only after exposure to low pH, indicating that a conformational change is necessary before virus maturation can occur. CASPubMedPubMed Central Google Scholar
Allison, S. L., Schalich, J., Stiasny, K., Mandl, C. W. & Heinz, F. X. Mutational evidence for an internal fusion peptide in flavivirus envelope protein E. J. Virol.75, 4268–4275 (2001). ArticleCASPubMedPubMed Central Google Scholar
Allison, S. L. et al. Oligomeric rearrangement of tick-borne encephalitis virus envelope proteins induced by an acidic pH. J. Virol.69, 695–700 (1995). Identification of E trimers at acidic pH and E dimers at neutral pH. The first suggestion of an oligomeric rearrangement during fusion. CASPubMedPubMed Central Google Scholar
Corver, J. et al. Membrane fusion activity of tick-borne encephalitis virus and recombinant subviral particles in a liposomal model system. Virology269, 37–46 (2000). ArticleCASPubMed Google Scholar
Lindenbach, B. D. & Rice, C. M. Molecular biology of flaviviruses. Adv. Virus Res.59, 23–61 (2003). ArticleCASPubMed Google Scholar
Brinton, M. A. The molecular biology of West Nile virus: a new invader of the western hemisphere. Annu. Rev. Microbiol.56, 371–402 (2002). ArticleCASPubMed Google Scholar
Guirakhoo, F., Heinz, F. X., Mandl, C. W., Holzmann, H. & Kunz, C. Fusion activity of flaviviruses: comparison of mature and immature (prM-containing) tick-borne encephalitis virions. J. Gen. Virol.72, 1323–1329 (1991). ArticleCASPubMed Google Scholar
Guirakhoo, F., Bolin, R. A. & Roehrig, J. T. The Murray Valley encephalitis virus prM protein confers acid resistance to virus particles and alters the expression of epitopes within the R2 domain of E glycoprotein. Virology191, 921–931 (1992). ArticleCASPubMed Google Scholar
Elshuber, S., Allison, S. L., Heinz, F. X. & Mandl, C. W. Cleavage of protein prM is necessary for infection of BHK-21 cells by tick-borne encephalitis virus. J. Gen. Virol.84, 183–191 (2003). ArticleCASPubMed Google Scholar
Schalich, J. et al. Recombinant subviral particles from tick-borne encephalitis virus are fusogenic and provide a model system for studying flavivirus envelope glycoprotein functions. J. Virol.70, 4549–4557 (1996). CASPubMedPubMed Central Google Scholar
Mancini, E. J., Clarke, M., Gowen, B. E., Rutten, T. & Fuller, S. D. Cryo-electron microscopy reveals the functional organization of an enveloped virus, Semliki Forest virus. Mol. Cell5, 255–266 (2000). ArticleCASPubMed Google Scholar
Zhang, W. et al. Visualization of membrane protein domains by cryo-electron microscopy of dengue virus. Nature Struct. Biol.10, 907–912 (2003). One of the few structures in which the transmembrane and membrane-associated proteins can be visualized. ArticleCASPubMed Google Scholar
Ma, L., Jones, C. T., Groesch, T. D., Kuhn, R. J. & Post, C. B. Solution structure of dengue virus capsid protein reveals another fold. Proc. Natl Acad. Sci. USA101, 3414–3419 (2004). ArticleCASPubMedPubMed Central Google Scholar
Modis, Y., Ogata, S., Clements, D. & Harrison, S. C. A ligand-binding pocket in the dengue virus envelope glycoprotein. Proc. Natl Acad. Sci. USA100, 6986–6991 (2003). ArticleCASPubMedPubMed Central Google Scholar
Rey, F. A., Heinz, F. X., Mandl, C., Kunz, C. & Harrison, S. C. The envelope glycoprotein from tick-borne encephalitis virus at 2-Å resolution. Nature375, 291–298 (1995). First crystal structure of a class II fusion protein in the pre-fusion conformation. ArticleCASPubMed Google Scholar
Zhang, Y. et al. Conformational changes of the flavivirus E glycoprotein. Structure (Camb)12, 1607–1618 (2004). Details the differences of the E protein structure during the virus life cycle. ArticleCAS Google Scholar
Lescar, J. et al. The fusion glycoprotein shell of Semliki Forest virus: an icosahedral assembly primed for fusogenic activation at endosomal pH. Cell105, 137–148 (2001). ArticleCASPubMed Google Scholar
Choi, H. K. et al. Structural analysis of Sindbis virus capsid mutants involving assembly and catalysis. J. Mol. Biol.262, 151–167 (1996). ArticleCASPubMed Google Scholar
Dokland, T. et al. West Nile virus core protein; tetramer structure and ribbon formation. Structure (Camb)12, 1157–1163 (2004). References 23 and 29 describe the structures of the dengue-2 and Kunjin capsid proteins. ArticleCAS Google Scholar
Konishi, E. & Mason, P. W. Proper maturation of the Japanese encephalitis virus envelope glycoprotein requires cosynthesis with the premembrane protein. J. Virol.67, 1672–1675 (1993). CASPubMedPubMed Central Google Scholar
Allison, S. L., Stadler, K., Mandl, C. W., Kunz, C. & Heinz, F. X. Synthesis and secretion of recombinant tick-borne encephalitis virus protein E in soluble and particulate form. J. Virol.69, 5816–5820 (1995). CASPubMedPubMed Central Google Scholar
Lee, E. & Lobigs, M. Mechanism of virulence attenuation of glycosaminoglycan-binding variants of Japanese encephalitis virus and Murray Valley encephalitis virus. J. Virol.76, 4901–4911 (2002). ArticleCASPubMedPubMed Central Google Scholar
Hung, S. -L. et al. Analysis of the steps involved in dengue virus entry into host cells. Virology257, 156–167 (1999). ArticleCASPubMed Google Scholar
Crill, W. D. & Roehrig, J. T. Monoclonal antibodies that bind to domain III of dengue virus E glycoprotein are the most efficient blockers of virus adsorption to Vero cells. J. Virol.75, 7769–7773 (2001). ArticleCASPubMedPubMed Central Google Scholar
Chiu, M. W. & Yang, Y. L. Blocking the dengue virus 2 infections on BHK-21 cells with purified recombinant dengue virus 2 E protein expressed in Escherichia coli. Biochem. Biophys. Res. Commun.309, 672–678 (2003). ArticleCASPubMed Google Scholar
Chen, Y. et al. Dengue virus infectivity depends on envelope protein binding to target cell heparan sulfate. Nature Med.3, 866–871 (1997). ArticleCASPubMed Google Scholar
Bhardwaj, S., Holbrook, M., Shope, R. E., Barrett, A. D. & Watowich, S. J. Biophysical characterization and vector-specific antagonist activity of domain III of the tick-borne flavivirus envelope protein. J. Virol.75, 4002–4007 (2001). ArticleCASPubMedPubMed Central Google Scholar
Wu, K. P. et al. Structural basis of a flavivirus recognized by its neutralizing antibody: solution structure of the domain III of the Japanese encephalitis virus envelope protein. J. Biol. Chem.278, 46007–46013 (2003). ArticleCASPubMed Google Scholar
Navarro-Sanchez, E. et al. Dendritic-cell-specific ICAM3-grabbing non-integrin is essential for the productive infection of human dendritic cells by mosquito-cell-derived dengue viruses. EMBO Rep.4, 723–728 (2003). ArticleCASPubMedPubMed Central Google Scholar
Mukhopadhyay, S., Kim, B. S., Chipman, P. R., Rossmann, M. G. & Kuhn, R. J. Structure of West Nile virus. Science302, 248 (2003). ArticleCASPubMed Google Scholar
Chen, Y. C., Wang, S. Y. & King, C. C. Bacterial lipopolysaccharide inhibits dengue virus infection of primary human monocytes/macrophages by blockade of virus entry via a CD14-dependent mechanism. J. Virol.73, 2650–2657 (1999). CASPubMedPubMed Central Google Scholar
Jindadamrongwech, S., Thepparit, C. & Smith, D. R. Identification of GRP78 (BiP) as a liver cell expressed receptor element for dengue virus serotype 2. Arch. Virol.149, 915–927 (2004). ArticleCASPubMed Google Scholar
Reyes-del Valle, J. & del Angel, R. M. Isolation of putative dengue virus receptor molecules by affinity chromatography using a recombinant E protein ligand. J. Virol. Methods116, 95–102 (2004). ArticleCASPubMed Google Scholar
Yazi Mendoza, M., Salas-Benito, J., Lanz-Mendoza, H., Hernandez-Martinez, S. & del Angel, R. A putative receptor for dengue virus in mosquito tissues: localization of a 45-kDa glycoprotein. Am. J. Trop. Med. Hyg.67, 76–84 (2002). ArticlePubMed Google Scholar
Salas-Benito, J. S. & del Angel, R. M. Identification of two surface proteins from C6/36 cells that bind dengue type 4 virus. J. Virol.71, 7246–7252 (1997). CASPubMedPubMed Central Google Scholar
Moreno-Altamirano, M. M. B., Sanchez-Garcia, F. J. & Munoz, M. L. Non Fc receptor-mediated infection of human macrophages by dengue virus serotype 2. J. Gen. Virol.83, 1123–1130 (2002). ArticleCASPubMed Google Scholar
Ramos-Castaneda, J., Imbert, J. L., Barron, B. L. & Ramos, C. A 65-kDa trypsin-sensible membrane cell protein as a possible receptor for dengue virus in cultured neuroblastoma cells. J. Neurovirol.3, 435–440 (1997). ArticleCASPubMed Google Scholar
de Lourdes Munoz, M. et al. Putative dengue virus receptors from mosquito cells. FEMS Microbiol. Lett.168, 251–258 (1998). ArticleCAS Google Scholar
Bielefeldt-Ohmann, H. Analysis of antibody-independent binding of dengue viruses and dengue virus envelope protein to human myelomonocytic cells and B lymphocytes. Virus Res.57, 63–79 (1998). ArticleCASPubMed Google Scholar
Bielefeldt-Ohmann, H., Meyer, M., Fitzpatrick, D. R. & Mackenzie, J. S. Dengue virus binding to human leukocyte cell lines: receptor usage differs between cell types and virus strains. Virus Res.73, 81–89 (2001). ArticleCASPubMed Google Scholar
Wei, H. Y., Jiang, L. F., Fang, D. Y. & Guo, H. Y. Dengue virus type 2 infects human endothelial cells through binding of the viral envelope glycoprotein to cell surface polypeptides. J. Gen. Virol.84, 3095–3098 (2003). ArticleCASPubMed Google Scholar
Hilgard, P. & Stockert, R. Heparan sulfate proteoglycans initiate dengue virus infection of hepatocytes. Hepatology32, 1069–1077 (2000). ArticleCASPubMed Google Scholar
Chu, J. J. & Ng, M. L. Characterization of a 105-kDa plasma membrane associated glycoprotein that is involved in West Nile virus binding and infection. Virology312, 458–469 (2003). ArticleCASPubMed Google Scholar
Kimura, T., Kimura-Kuroda, J., Nagashima, K. & Yasui, K. Analysis of virus-cell binding characteristics on the determination of Japanese encephalitis virus susceptibility. Arch. Virol.139, 239–251 (1994). ArticleCASPubMed Google Scholar
Kopecky, J., Grubhoffer, L., Kovar, V., Jindrak, L. & Vokurkova, D. A putative host cell receptor for tick-borne encephalitis virus identified by anti-idiotypic antibodies and virus affinoblotting. Intervirology42, 9–16 (1999). ArticleCASPubMed Google Scholar
Maldov, D. G., Karganova, G. G. & Timofeev, A. V. Tick-borne encephalitis virus interaction with the target cells. Arch. Virol.127, 321–325 (1992). ArticleCASPubMed Google Scholar
Martinez-Barragan, J. J. & del Angel, R. M. Identification of a putative coreceptor on Vero cells that participates in dengue 4 virus infection. J. Virol.75, 7818–7827 (2001). ArticleCASPubMedPubMed Central Google Scholar
Lin, Y. L. et al. Heparin inhibits dengue-2 virus infection of five human liver cell lines. Antiviral Res.56, 93–96 (2002). ArticleCASPubMed Google Scholar
Germi, R. et al. Heparan sulfate-mediated binding of infectious dengue virus type 2 and yellow fever virus. Virology292, 162–168 (2002). ArticleCASPubMed Google Scholar
Su, C. M., Liao, C. L., Lee, Y. L. & Lin, Y. L. Highly sulfated forms of heparin sulfate are involved in Japanese encephalitis virus infection. Virology286, 206–215 (2001). ArticleCASPubMed Google Scholar
Lee, E. & Lobigs, M. Substitutions at the putative receptor-binding site of an encephalitic flavivirus alter virulence and host cell tropism and reveal a role for glycosaminoglycans in entry. J. Virol.74, 8867–8875 (2000). ArticleCASPubMedPubMed Central Google Scholar
Mandl, C. W. et al. Adaptation of tick-borne encephalitis virus to BHK-21 cells results in the formation of multiple heparan sulfate binding sites in the envelope protein and attenuation in vivo. J. Virol.75, 5627–5637 (2001). ArticleCASPubMedPubMed Central Google Scholar
Kroschewski, H., Allison, S. L., Heinz, F. X. & Mandl, C. W. Role of heparan sulfate for attachment and entry of tick-borne encephalitis virus. Virology308, 92–100 (2003). ArticleCASPubMed Google Scholar
Dimitrov, D. S. Virus entry: molecular mechanisms and biomedical applications. Nature Rev. Microbiol.2, 109–122 (2004). ArticleCAS Google Scholar
van der Most, R. G., Corver, J. & Strauss, J. H. Mutagenesis of the RGD motif in the yellow fever virus 17D envelope protein. Virology265, 83–95 (1999). ArticleCASPubMed Google Scholar
Allison, S. L., Stiasny, K., Stadler, K., Mandl, C. W. & Heinz, F. X. Mapping of functional elements in the stem-anchor region of tick-borne encephalitis virus envelope protein E. J. Virol.73, 5605–5612 (1999). CASPubMedPubMed Central Google Scholar
Stiasny, K., Allison, S. L., Marchler-Bauer, A., Kunz, C. & Heinz, F. X. Structural requirements for low-pH-induced rearrangements in the envelope glycoprotein of tick-borne encephalitis virus. J. Virol.70, 8142–8147 (1996). CASPubMedPubMed Central Google Scholar
Stiasny, K., Allison, S. L., Mandl, C. W. & Heinz, F. X. Role of metastability and acidic pH in membrane fusion by tick-borne encephalitis virus. J. Virol.75, 7392–7398 (2001). ArticleCASPubMedPubMed Central Google Scholar
Stiasny, K., Allison, S. L., Schalich, J. & Heinz, F. X. Membrane interactions of the tick-borne encephalitis virus fusion protein E at low pH. J. Virol.76, 3784–3790 (2002). Demonstrates that the stem region of the E protein is not necessary for trimer formation if the trimerization occurs in the presence of lipids. ArticleCASPubMedPubMed Central Google Scholar
Bressanelli, S. et al. Structure of a flavivirus envelope glycoprotein in its low-pH-induced membrane fusion conformation. EMBO J.23, 728–738 (2004). ArticleCASPubMedPubMed Central Google Scholar
Modis, Y., Ogata, S., Clements, D. & Harrison, S. C. Structure of the dengue virus envelope protein after membrane fusion. Nature427, 313–319 (2004). References 71 and 72 describe the first X-ray structures of class II fusion protein in post-fusion conformation. ArticleCASPubMed Google Scholar
Gibbons, D. L. et al. Conformational change and protein–protein interactions of the fusion protein of Semliki Forest virus. Nature427, 320–325 (2004). ArticleCASPubMed Google Scholar
Kiermayr, S., Kofler, R. M., Mandl, C. W., Messner, P. & Heinz, F. X. Isolation of capsid protein dimers from the tick-borne encephalitis (TBE) flavivirus and in vitro assembly of capsid-like particles. J. Virol.78, 8078–8084 (2004). ArticleCASPubMedPubMed Central Google Scholar
Johnson, J. E. Functional implications of protein–protein interactions in icosahedral viruses. Proc. Natl Acad. Sci. USA93, 27–33 (1996). ArticleCASPubMedPubMed Central Google Scholar
Rossmann, M. G. & Johnson, J. E. Icosahedral RNA virus structure. Annu. Rev. Biochem.58, 533–573 (1989). ArticleCASPubMed Google Scholar
Kofler, R. M., Heinz, F. X. & Mandl, C. W. Capsid protein C of tick-borne encephalitis virus tolerates large internal deletions and is a favorable target for attenuation of virulence. J. Virol.76, 3534–3543 (2002). ArticleCASPubMedPubMed Central Google Scholar
Kofler, R. M., Leitner, A., O'Riordain, G., Heinz, F. X. & Mandl, C. W. Spontaneous mutations restore the viability of tick-borne encephalitis virus mutants with large deletions in protein C. J. Virol.77, 443–451 (2003). ArticleCASPubMedPubMed Central Google Scholar
Russell, P. K., Brandt, W. E. & Dalrymple, J. in The Togaviruses (ed. Schlesinger, R. W.) 503–529 (Academic Press, New York, 1980). Book Google Scholar
Ferlenghi, I. et al. Molecular organization of a recombinant subviral particle from tick-borne encephalitis virus. Mol. Cell7, 593–602 (2001). ArticleCASPubMed Google Scholar
Allison, S. L. et al. Two distinct size classes of immature and mature subviral particles from tick-borne encephalitis virus. J. Virol.77, 11357–11366 (2003). ArticleCASPubMedPubMed Central Google Scholar
Konishi, E. et al. Mice immunized with a subviral particle containing the Japanese encephalitis virus prM/M and E proteins are protected from lethal JEV infection. Virology188, 714–720 (1992). ArticleCASPubMed Google Scholar
Kuhn, R. J. et al. Structure of dengue virus: implications for flavivirus organization, maturation, and fusion. Cell108, 717–725 (2002). ArticleCASPubMedPubMed Central Google Scholar
Zhang, Y. et al. Structures of immature flavivirus particles. EMBO J.22, 2604–2613 (2003). The first structures of immature flavivirus particles. ArticleCASPubMedPubMed Central Google Scholar
Caspar, D. L. & Klug, A. Physical principles in the construction of regular viruses. Cold Spring Harb. Symp. Quant. Biol.27, 1–24 (1962). ArticleCASPubMed Google Scholar
Werten, P. J. et al. Progress in the analysis of membrane protein structure and function. FEBS Lett.529, 65–72 (2002). ArticleCASPubMed Google Scholar
Cockburn, J. J., Bamford, J. K., Grimes, J. M., Bamford, D. H. & Stuart, D. I. Crystallization of the membrane-containing bacteriophage PRD1 in quartz capillaries by vapour diffusion. Acta Crystallogr. D Biol. Crystallogr.59, 538–540 (2003). ArticleCASPubMed Google Scholar
Op De Beeck, A. et al. Role of the transmembrane domains of prM and E proteins in the formation of yellow fever virus envelope. J. Virol.77, 813–820 (2003). ArticleCASPubMedPubMed Central Google Scholar
Pletnev, S. V. et al. Locations of carbohydrate sites on α-virus glycoproteins show that E1 forms an icosahedral scaffold. Cell105, 127–136 (2001). ArticleCASPubMedPubMed Central Google Scholar
Wilson, I. A., Skehel, J. J. & Wiley, D. C. Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution. Nature289, 366–373 (1981). ArticleCASPubMed Google Scholar
Skehel, J. J. & Wiley, D. C. Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin. Annu. Rev. Biochem.69, 531–569 (2000). ArticleCASPubMed Google Scholar
Weissenhorn, W. et al. Structural basis for membrane fusion by enveloped viruses. Mol. Membr. Biol.16, 3–9 (1999). ArticleCASPubMed Google Scholar