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Volumn 86, Issue 21, 2012, Pages 11457-11471

Biochemical, conformational, and immunogenic analysis of soluble trimeric forms of henipavirus fusion glycoproteins

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOSYLPHOSPHATIDYLINOSITOL; HYBRID PROTEIN; MONOCLONAL ANTIBODY; NEUTRALIZING ANTIBODY; PEPTIDE; PHOSPHOLIPASE D; PROTEIN ANTIBODY; PROTEIN PRECURSOR; PROTEINASE; SF GLYCOPROTEIN; UNCLASSIFIED DRUG; VIRUS ANTIBODY; VIRUS GLYCOPROTEIN; VIRUS VACCINE;

EID: 84868338568     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.01318-12     Document Type: Article
Times cited : (52)

References (73)
  • 1
    • 34247557393 scopus 로고    scopus 로고
    • Polybasic KKR motif in the cytoplasmic tail of Nipah virus fusion protein modulates membrane fusion by inside-out signaling
    • Aguilar HC, et al. 2007. Polybasic KKR motif in the cytoplasmic tail of Nipah virus fusion protein modulates membrane fusion by inside-out signaling. J. Virol. 81:4520-4532.
    • (2007) J. Virol. , vol.81 , pp. 4520-4532
    • Aguilar, H.C.1
  • 2
    • 33646447520 scopus 로고    scopus 로고
    • N-Glycans on Nipah virus fusion protein protect against neutralization but reduce membrane fusion and viral entry
    • Aguilar HC, et al. 2006. N-Glycans on Nipah virus fusion protein protect against neutralization but reduce membrane fusion and viral entry. J.Virol. 80:4878-4889.
    • (2006) J.Virol. , vol.80 , pp. 4878-4889
    • Aguilar, H.C.1
  • 4
    • 84866440974 scopus 로고    scopus 로고
    • Nipah encephalitis, human-Bangladesh: Jipurhat
    • Anonymous, Pro-MED-mailArchive no. 20120212.1040138. February 7. International Society for Infectious Diseases, Brookline, MA
    • Anonymous. 2012. Nipah encephalitis, human-Bangladesh: Jipurhat.Pro-MED-mailArchive no. 20120212.1040138. February 7. International Society for Infectious Diseases, Brookline, MA. www.promedmail.org.
    • (2012)
  • 5
    • 79955771535 scopus 로고    scopus 로고
    • Genomic characterization of Nipah virus, West Bengal, India
    • Arankalle VA, et al. 2011. Genomic characterization of Nipah virus, West Bengal, India. Emerg. Infect. Dis. 17:907-909.
    • (2011) Emerg. Infect. Dis. , vol.17 , pp. 907-909
    • Arankalle, V.A.1
  • 6
    • 0029999173 scopus 로고    scopus 로고
    • Cell surface expression of a functional rubella virus E1 glycoprotein by addition of a GPI anchor
    • Bernasconi E, Fasel N, Wittek R. 1996. Cell surface expression of a functional rubella virus E1 glycoprotein by addition of a GPI anchor. J.Cell Sci. 109(Pt 6):1195-1201.
    • (1996) J.Cell Sci. , vol.109 , Issue.PART 6 , pp. 1195-1201
    • Bernasconi, E.1    Fasel, N.2    Wittek, R.3
  • 7
    • 34249793705 scopus 로고    scopus 로고
    • Identification of Hendra virus G glycoprotein residues that are critical for receptor binding
    • Bishop KA, et al. 2007. Identification of Hendra virus G glycoprotein residues that are critical for receptor binding. J. Virol. 81:5893-5901.
    • (2007) J. Virol. , vol.81 , pp. 5893-5901
    • Bishop, K.A.1
  • 8
    • 23044517161 scopus 로고    scopus 로고
    • Ephrin-B2 ligand is a functional receptor for Hendra virus and Nipah virus
    • Bonaparte MI, et al. 2005. Ephrin-B2 ligand is a functional receptor for Hendra virus and Nipah virus. Proc. Natl. Acad. Sci. U.S.A. 102:10652-10657.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 10652-10657
    • Bonaparte, M.I.1
  • 9
    • 21044446226 scopus 로고    scopus 로고
    • Receptor binding, fusion inhibition, and induction of cross-reactive neutralizing antibodies by a soluble G glycoprotein of Hendra virus
    • Bossart KN, et al. 2005. Receptor binding, fusion inhibition, and induction of cross-reactive neutralizing antibodies by a soluble G glycoprotein of Hendra virus. J. Virol. 79:6690-6702.
    • (2005) J. Virol , vol.79 , pp. 6690-6702
    • Bossart, K.N.1
  • 10
    • 24944483017 scopus 로고    scopus 로고
    • Inhibition of henipavirus fusion and infection by heptad-derived peptides of the Nipah virus fusion glycoprotein
    • Bossart KN, et al. 2005. Inhibition of henipavirus fusion and infection by heptad-derived peptides of the Nipah virus fusion glycoprotein. Virol. J.2:57.
    • (2005) Virol. J. , vol.2 , pp. 57
    • Bossart, K.N.1
  • 11
    • 0035841668 scopus 로고    scopus 로고
    • Functional expression and membrane fusion tropism of the envelope glycoproteins of Hendra virus
    • Bossart KN, Wang LF, Eaton BT, Broder CC. 2001. Functional expression and membrane fusion tropism of the envelope glycoproteins of Hendra virus. Virology 290:121-135.
    • (2001) Virology , vol.290 , pp. 121-135
    • Bossart, K.N.1    Wang, L.F.2    Eaton, B.T.3    Broder, C.C.4
  • 12
    • 0036827695 scopus 로고    scopus 로고
    • Membrane fusion tropism and heterotypic functional activities of the Nipah virus and Hendra virus envelope glycoproteins
    • Bossart KN, et al. 2002. Membrane fusion tropism and heterotypic functional activities of the Nipah virus and Hendra virus envelope glycoproteins.J. Virol. 76:11186 -11198.
    • (2002) J. Virol. , vol.76 , pp. 11186-11198
    • Bossart, K.N.1
  • 13
    • 78649584765 scopus 로고    scopus 로고
    • Prevalence of henipavirus and rubulavirus antibodies in pteropid bats, Papua New Guinea
    • Breed AC, et al. 2010. Prevalence of henipavirus and rubulavirus antibodies in pteropid bats, Papua New Guinea. Emerg. Infect. Dis. 16:1997-1999.
    • (2010) Emerg. Infect. Dis. , vol.16 , pp. 1997-1999
    • Breed, A.C.1
  • 14
    • 84859500131 scopus 로고    scopus 로고
    • Henipavirus outbreaks to antivirals: the current status of potential therapeutics
    • Broder CC. 2012. Henipavirus outbreaks to antivirals: the current status of potential therapeutics. Curr. Opin. Virol. 2:176-187.
    • (2012) Curr. Opin. Virol. , vol.2 , pp. 176-187
    • Broder, C.C.1
  • 15
    • 19944415289 scopus 로고    scopus 로고
    • Role of N-linked glycosylation of the Hendra virus fusion protein
    • Carter JR, Pager CT, Fowler SD, Dutch RE. 2005. Role of N-linked glycosylation of the Hendra virus fusion protein. J. Virol. 79:7922-7925.
    • (2005) J. Virol. , vol.79 , pp. 7922-7925
    • Carter J.R.Pager, C.T.1    Fowler, S.D.2    Dutch, R.E.3
  • 16
    • 33644504513 scopus 로고    scopus 로고
    • Nipah virus-associated encephalitis outbreak, Siliguri, India
    • Chadha MS, et al. 2006. Nipah virus-associated encephalitis outbreak, Siliguri, India. Emerg. Infect. Dis. 12:235-240.
    • (2006) Emerg. Infect. Dis. , vol.12 , pp. 235-240
    • Chadha, M.S.1
  • 17
    • 64949139080 scopus 로고    scopus 로고
    • Preparation of recombinant viral glycoproteins for novel and therapeutic antibody discovery
    • Chan YP, Yan L, Feng YR, Broder CC. 2009. Preparation of recombinant viral glycoproteins for novel and therapeutic antibody discovery. Methods Mol. Biol. 525:31-58, xiii.
    • (2009) Methods Mol. Biol. , vol.13 , Issue.525 , pp. 31-58
    • Chan, Y.P.1    Yan, L.2    Feng, Y.R.3    Broder, C.C.4
  • 18
    • 0035950928 scopus 로고    scopus 로고
    • Cloning, expression, and crystallization of the fusion protein of Newcastle disease virus
    • Chen L, et al. 2001. Cloning, expression, and crystallization of the fusion protein of Newcastle disease virus. Virology 290:290-299.
    • (2001) Virology , vol.290 , pp. 290-299
    • Chen, L.1
  • 19
    • 0035083470 scopus 로고    scopus 로고
    • The structure of the fusion glycoprotein of Newcastle disease virus suggests a novel paradigm for the molecular mechanism of membrane fusion
    • Chen L, et al. 2001. The structure of the fusion glycoprotein of Newcastle disease virus suggests a novel paradigm for the molecular mechanism of membrane fusion. Structure (Camb.) 9:255-266.
    • (2001) Structure (Camb.) , vol.9 , pp. 255-266
    • Chen, L.1
  • 20
    • 0034717054 scopus 로고    scopus 로고
    • Nipah virus: a recently emergent deadly paramyxovirus
    • Chua KB, et al. 2000. Nipah virus: a recently emergent deadly paramyxovirus.Science 288:1432-1435.
    • (2000) Science , vol.288 , pp. 1432-1435
    • Chua, K.B.1
  • 21
    • 0036185623 scopus 로고    scopus 로고
    • Isolation of Nipah virus from Malaysian Island flying-foxes
    • Chua KB, et al. 2002. Isolation of Nipah virus from Malaysian Island flying-foxes. Microbes Infect. 4:145-151.
    • (2002) Microbes Infect. , vol.4 , pp. 145-151
    • Chua, K.B.1
  • 22
    • 70350277403 scopus 로고    scopus 로고
    • Bimolecular complementation of paramyxovirus fusion and hemagglutininneuraminidase proteins enhances fusion: implications for the mechanism of fusion triggering
    • Connolly SA, Leser GP, Jardetzky TS, Lamb RA. 2009. Bimolecular complementation of paramyxovirus fusion and hemagglutininneuraminidase proteins enhances fusion: implications for the mechanism of fusion triggering. J. Virol. 83:10857-10868.
    • (2009) J. Virol. , vol.83 , pp. 10857-10868
    • Connolly, S.A.1    Leser, G.P.2    Jardetzky, T.S.3    Lamb, R.A.4
  • 23
    • 33845212315 scopus 로고    scopus 로고
    • Refolding of a paramyxovirus F protein from prefusion to postfusion conformations observed by liposome binding and electron microscopy
    • Connolly SA, Leser GP, Yin HS, Jardetzky TS, Lamb RA. 2006. Refolding of a paramyxovirus F protein from prefusion to postfusion conformations observed by liposome binding and electron microscopy. Proc. Natl. Acad. Sci. U.S.A. 103:17903-17908.
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 17903-17908
    • Connolly, S.A.1    Leser, G.P.2    Yin, H.S.3    Jardetzky, T.S.4    Lamb, R.A.5
  • 24
    • 57049160334 scopus 로고    scopus 로고
    • Measles virus attachment proteins with impaired ability to bind CD46 interact more efficiently with the homologous fusion protein
    • Corey EA, Iorio RM. 2009. Measles virus attachment proteins with impaired ability to bind CD46 interact more efficiently with the homologous fusion protein. Virology 383:1-5.
    • (2009) Virology , vol.383 , pp. 1-5
    • Corey, E.A.1    Iorio, R.M.2
  • 25
    • 23844555503 scopus 로고    scopus 로고
    • The Nipah virus fusion protein is cleaved within the endosomal compartment
    • Diederich S, Moll M, Klenk HD, Maisner A. 2005. The Nipah virus fusion protein is cleaved within the endosomal compartment. J. Biol.Chem. 280:29899-29903.
    • (2005) J. Biol.Chem. , vol.280 , pp. 29899-29903
    • Diederich, S.1    Moll, M.2    Klenk, H.D.3    Maisner, A.4
  • 26
    • 68149166461 scopus 로고    scopus 로고
    • Henipavirus RNA in African bats
    • Drexler JF, et al. 2009. Henipavirus RNA in African bats. PLoS One 4:e6367. doi:10.1371/journal.pone.0006367.
    • (2009) PLoS One , vol.4
    • Drexler, J.F.1
  • 27
    • 84860279802 scopus 로고    scopus 로고
    • Bats host major mammalian paramyxoviruses
    • Drexler JF, et al. 2012. Bats host major mammalian paramyxoviruses. Nat. Commun. 3:796.
    • (2012) Nat. Commun. , vol.3 , pp. 796
    • Drexler, J.F.1
  • 31
    • 34250766432 scopus 로고    scopus 로고
    • Person-to-person transmission of Nipah virus in a Bangladeshi community
    • Gurley ES, et al. 2007. Person-to-person transmission of Nipah virus in a Bangladeshi community. Emerg. Infect. Dis. 13:1031-1037.
    • (2007) Emerg. Infect. Dis. , vol.13 , pp. 1031-1037
    • Gurley, E.S.1
  • 32
    • 81155131372 scopus 로고    scopus 로고
    • Pteropid bats are confirmed as the reservoir hosts of henipaviruses: a comprehensive experimental study of virus transmission
    • Halpin K, et al. 2011. Pteropid bats are confirmed as the reservoir hosts of henipaviruses: a comprehensive experimental study of virus transmission.Am. J. Trop. Med. Hyg. 85:946-951.
    • (2011) Am. J. Trop. Med. Hyg. , vol.85 , pp. 946-951
    • Halpin, K.1
  • 33
    • 0027934571 scopus 로고
    • Crystal structure of an isoleucinezipper trimer
    • Harbury PB, Kim PS, Alber T. 1994. Crystal structure of an isoleucinezipper trimer. Nature 371:80-83.
    • (1994) Nature , vol.371 , pp. 80-83
    • Harbury, P.B.1    Kim, P.S.2    Alber, T.3
  • 34
    • 0034608231 scopus 로고    scopus 로고
    • Molecular characterization of Nipah virus, a newly emergent paramyxovirus
    • Harcourt BH, et al. 2000. Molecular characterization of Nipah virus, a newly emergent paramyxovirus. Virology 271:334-349.
    • (2000) Virology , vol.271 , pp. 334-349
    • Harcourt, B.H.1
  • 35
    • 50549098494 scopus 로고    scopus 로고
    • Evidence of henipavirus infection in West African fruit bats
    • Hayman DT, et al. 2008. Evidence of henipavirus infection in West African fruit bats. PLoS One 3:e2739. doi:10.1371/journal.pone.0002739.
    • (2008) PLoS One , vol.3
    • Hayman, D.T.1
  • 36
    • 78149430469 scopus 로고    scopus 로고
    • Cluster of Nipah virus infection, Kushtia District,Bangladesh, 2007
    • doi:10.1371/journal. pone.0013570
    • Homaira N, et al. 2010. Cluster of Nipah virus infection, Kushtia District,Bangladesh, 2007. PLoS One 5:e13570. doi:10.1371/journal. pone.0013570.Chan et al.11470
    • (2010) PLoS One , vol.5
    • Homaira, N.1
  • 37
    • 9744233639 scopus 로고    scopus 로고
    • Nipah virus encephalitis reemergence, Bangladesh
    • Hsu VP, et al. 2004. Nipah virus encephalitis reemergence, Bangladesh.Emerg. Infect. Dis. 10:2082-2087.
    • (2004) Emerg. Infect. Dis. , vol.10 , pp. 2082-2087
    • Hsu, V.P.1
  • 38
    • 0019756004 scopus 로고
    • Analysis of data from the analytical ultracentrifuge by nonlinear least-squares techniques
    • Johnson ML, Correia JJ, Yphantis DA, Halvorson HR. 1981. Analysis of data from the analytical ultracentrifuge by nonlinear least-squares techniques.Biophys. J. 36:575-588.
    • (1981) Biophys. J. , vol.36 , pp. 575-588
    • Johnson, M.L.1    Correia, J.J.2    Yphantis, D.A.3    Halvorson, H.R.4
  • 39
    • 0027199871 scopus 로고
    • GPI- and transmembraneanchored influenza hemagglutinin differ in structure and receptor binding activity
    • Kemble GW, Henis YI, White JM. 1993. GPI- and transmembraneanchored influenza hemagglutinin differ in structure and receptor binding activity. J. Cell Biol. 122:1253-1265.
    • (1993) J. Cell Biol. , vol.122 , pp. 1253-1265
    • Kemble, G.W.1    Henis, Y.I.2    White, J.M.3
  • 40
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J, Doolittle RF. 1982. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157:105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 41
    • 34547601896 scopus 로고    scopus 로고
    • Paramyxoviridae: the viruses and their replication
    • Lippincott Williams & Wilkins, Philadelphia, PA
    • Lamb RA, Parks GD. 2007. Paramyxoviridae: the viruses and their replication,p 1449-1496. In Knipe DM, et al. (ed), Fields virology, 5 ed, vol 1.Lippincott Williams & Wilkins, Philadelphia, PA.
    • (2007) In Knipe DM, et al. (ed), Fields virology, 5 ed. , vol.1 , pp. 1449-1496
    • Lamb, R.A.1    Parks, G.D.2
  • 42
    • 29144460894 scopus 로고    scopus 로고
    • Paramyxovirus membranefusion: lessons from the F andHNatomic structures
    • Lamb RA, Paterson RG, Jardetzky TS. 2006. Paramyxovirus membranefusion: lessons from the F andHNatomic structures. Virology 344:30-37.
    • (2006) Virology , vol.344 , pp. 30-37
    • Lamb, R.A.1    Paterson, R.G.2    Jardetzky, T.S.3
  • 44
    • 79960918320 scopus 로고    scopus 로고
    • Modes of paramyxovirus fusion: a henipavirus perspective
    • Lee B, Ataman ZA. 2011. Modes of paramyxovirus fusion: a henipavirus perspective. Trends Microbiol. 19:389-399.
    • (2011) Trends Microbiol , vol.19 , pp. 389-399
    • Lee, B.1    Ataman, Z.A.2
  • 45
    • 57049185810 scopus 로고    scopus 로고
    • Antibodies to Nipah or Nipah-like viruses in bats, China
    • Li Y, et al. 2008. Antibodies to Nipah or Nipah-like viruses in bats, China.Emerg. Infect. Dis. 14:1974-1976.
    • (2008) Emerg. Infect. Dis. , vol.14 , pp. 1974-1976
    • Li, Y.1
  • 46
    • 68049105299 scopus 로고    scopus 로고
    • Recurrent zoonotic transmission of Nipah virus into humans, Bangladesh, 2001-2007
    • Luby SP, et al. 2009. Recurrent zoonotic transmission of Nipah virus into humans, Bangladesh, 2001-2007. Emerg. Infect. Dis. 15:1229-1235.
    • (2009) Emerg. Infect. Dis. , vol.15 , pp. 1229-1235
    • Luby, S.P.1
  • 47
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: semiautomated software for high-resolution single-particle reconstructions
    • Ludtke SJ, Baldwin PR, Chiu W. 1999. EMAN: semiautomated software for high-resolution single-particle reconstructions. J. Struct. Biol. 128:82-97.
    • (1999) J. Struct. Biol. , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 48
    • 33744828666 scopus 로고    scopus 로고
    • Sequence elements of the fusion peptide of human respiratory syncytial virus fusion protein required for activity
    • Martin D, Calder LJ, Garcia-Barreno B, Skehel JJ, Melero JA. 2006.Sequence elements of the fusion peptide of human respiratory syncytial virus fusion protein required for activity. J. Gen. Virol. 87:1649-1658.
    • (2006) J. Gen. Virol. , vol.87 , pp. 1649-1658
    • Martin, D.1    Calder, L.J.2    Garcia-Barreno, B.3    Skehel, J.J.4    Melero, J.A.5
  • 49
    • 30344467852 scopus 로고    scopus 로고
    • Addition of N-glycans in the stalk of the Newcastle disease virus HN protein blocks its interaction with the F protein and prevents fusion
    • Melanson VR, Iorio RM. 2006. Addition of N-glycans in the stalk of the Newcastle disease virus HN protein blocks its interaction with the F protein and prevents fusion. J. Virol. 80:623- 633.
    • (2006) J. Virol. , vol.80 , pp. 623-633
    • Melanson, V.R.1    Iorio, R.M.2
  • 50
    • 8644256749 scopus 로고    scopus 로고
    • Amino acid substitutions in the F-specific domain in the stalk of the Newcastle disease virus HN protein modulate fusion and interfere with its interaction with the F protein
    • Melanson VR, Iorio RM. 2004. Amino acid substitutions in the F-specific domain in the stalk of the Newcastle disease virus HN protein modulate fusion and interfere with its interaction with the F protein. J. Virol. 78:13053-13061.
    • (2004) J. Virol. , vol.78 , pp. 13053-13061
    • Melanson, V.R.1    Iorio, R.M.2
  • 51
    • 26444565765 scopus 로고    scopus 로고
    • Endocytosis plays a critical role in proteolytic processing of the Hendra virus fusion protein
    • Meulendyke KA, Wurth MA, McCann RO, Dutch RE. 2005. Endocytosis plays a critical role in proteolytic processing of the Hendra virus fusion protein. J. Virol. 79:12643-12649.
    • (2005) J. Virol. , vol.79 , pp. 12643-12649
    • Meulendyke, K.A.1    Wurth, M.A.2    McCann, R.O.3    Dutch, R.E.4
  • 52
    • 0034715228 scopus 로고    scopus 로고
    • The cleavage activation and sites of glycosylation in the fusion protein of Hendra virus
    • Michalski WP, Crameri G, Wang L, Shiell BJ, Eaton B. 2000. The cleavage activation and sites of glycosylation in the fusion protein of Hendra virus. Virus Res. 69:83-93.
    • (2000) Virus Res. , vol.69 , pp. 83-93
    • Michalski, W.P.1    Crameri, G.2    Wang, L.3    Shiell, B.J.4    Eaton, B.5
  • 53
    • 2942647917 scopus 로고    scopus 로고
    • Influence of N-glycans on processing and biological activity of the Nipah virus fusion protein
    • Moll M, Kaufmann A, Maisner A. 2004. Influence of N-glycans on processing and biological activity of the Nipah virus fusion protein. J.Virol. 78:7274-7278.54. Murray K, et al. 1995. A morbillivirus that caused fatal disease in horses and humans. Science 268:94-97.
    • (2004) J.Virol. , vol.78 , pp. 7274-7278
    • Moll, M.1    Kaufmann, A.2    Maisner, A.3
  • 54
    • 0028943779 scopus 로고
    • A morbillivirus that caused fatal disease in horses and humans
    • Murray K, et al. 1995. A morbillivirus that caused fatal disease in horses and humans. Science 268:94-97
    • (1995) Science , vol.268 , pp. 94-97
    • Murray, K.1
  • 55
    • 2342662152 scopus 로고    scopus 로고
    • Negative staining and image classification-powerful tools in modern electron microscopy
    • Ohi M, Li Y, Cheng Y, Walz T. 2004. Negative staining and image classification-powerful tools in modern electron microscopy. Biol.Proced. Online 6:23-34.
    • (2004) Biol.Proced. Online , vol.6 , pp. 23-34
    • Ohi, M.1    Li, Y.2    Cheng, Y.3    Walz, T.4
  • 56
    • 33644822934 scopus 로고    scopus 로고
    • A mature and fusogenic form of the Nipah virus fusion protein requires proteolytic processing by cathepsin L
    • Pager CT, Craft WW, Jr, Patch J, Dutch RE. 2006. A mature and fusogenic form of the Nipah virus fusion protein requires proteolytic processing by cathepsin L. Virology 346:251-257.
    • (2006) Virology , vol.346 , pp. 251-257
    • Pager, C.T.1    Craft, W.W.2    Jr Patch, J.3    Dutch, R.E.4
  • 57
    • 26444552119 scopus 로고    scopus 로고
    • Cathepsin L is involved in proteolytic processing of the Hendra virus fusion protein
    • Pager CT, Dutch RE. 2005. Cathepsin L is involved in proteolytic processing of the Hendra virus fusion protein. J. Virol. 79:12714-12720.
    • (2005) J. Virol. , vol.79 , pp. 12714-12720
    • Pager, C.T.1    Dutch, R.E.2
  • 59
    • 79959835596 scopus 로고    scopus 로고
    • Structural and mechanistic studies of measles virus illuminate paramyxovirus entry
    • doi:10.1371/journal.ppat.1002058
    • Plemper RK, Brindley MA, Iorio RM. 2011. Structural and mechanistic studies of measles virus illuminate paramyxovirus entry. PLoS Pathog.7:e1002058. doi:10.1371/journal.ppat.1002058.
    • (2011) PLoS Pathog. , vol.7
    • Plemper, R.K.1    Brindley, M.A.2    Iorio, R.M.3
  • 60
    • 0036238643 scopus 로고    scopus 로고
    • Strength of envelope protein interaction modulates cytopathicity of measles virus
    • Plemper RK, Hammond AL, Gerlier D, Fielding AK, Cattaneo R. 2002. Strength of envelope protein interaction modulates cytopathicity of measles virus. J. Virol. 76:5051-5061.
    • (2002) J. Virol. , vol.76 , pp. 5051-5061
    • Plemper, R.K.1    Hammond, A.L.2    Gerlier, D.3    Fielding, A.K.4    Cattaneo, R.5
  • 61
    • 21144440209 scopus 로고    scopus 로고
    • Nipah virus in Lyle's flying foxes, Cambodia
    • Reynes JM, et al. 2005. Nipah virus in Lyle's flying foxes, Cambodia.Emerg. Infect. Dis. 11:1042-1047.
    • (2005) Emerg. Infect. Dis. , vol.11 , pp. 1042-1047
    • Reynes, J.M.1
  • 62
    • 71949123985 scopus 로고    scopus 로고
    • Viral entry mechanisms: the increasing diversity of paramyxovirus entry
    • Smith EC, Popa A, Chang A, Masante C, Dutch RE. 2009. Viral entry mechanisms: the increasing diversity of paramyxovirus entry. FEBS J. 276: 7217-7227.
    • (2009) FEBS J. , vol.276 , pp. 7217-7227
    • Smith, E.C.1    Popa, A.2    Chang, A.3    Masante, C.4    Dutch, R.E.5
  • 63
    • 80053222800 scopus 로고    scopus 로고
    • Identifying Hendra virus diversity in pteropid bats
    • doi:10.1371/journal.pone.0025275
    • Smith I, et al. 2011. Identifying Hendra virus diversity in pteropid bats.PLoS One 6:e25275. doi:10.1371/journal.pone.0025275.
    • (2011) PLoS One , vol.6
    • Smith, I.1
  • 64
    • 84857682692 scopus 로고    scopus 로고
    • Henipavirus mediated membrane fusion, virus entry and targeted therapeutics
    • Steffen DL, Xu K, Nikolov DB, Broder CC. 2012. Henipavirus mediated membrane fusion, virus entry and targeted therapeutics. Viruses 4:280-308.
    • (2012) Viruses , vol.4 , pp. 280-308
    • Steffen, D.L.1    Xu, K.2    Nikolov, D.B.3    Broder, C.C.4
  • 65
    • 77953021928 scopus 로고    scopus 로고
    • Structure of the Newcastle disease virus F protein in the post-fusion conformation
    • Swanson K, et al. 2010. Structure of the Newcastle disease virus F protein in the post-fusion conformation. Virology 402:372-379.
    • (2010) Virology , vol.402 , pp. 372-379
    • Swanson, K.1
  • 66
    • 33746798064 scopus 로고    scopus 로고
    • Isolation and characterization of monoclonal antibodies which neutralize human metapneumovirus in vitro and in vivo
    • Ulbrandt ND, et al. 2006. Isolation and characterization of monoclonal antibodies which neutralize human metapneumovirus in vitro and in vivo. J. Virol. 80:7799-7806.
    • (2006) J. Virol. , vol.80 , pp. 7799-7806
    • Ulbrandt, N.D.1
  • 67
    • 77950581527 scopus 로고    scopus 로고
    • A longitudinal study of the prevalence of Nipah virus in Pteropus lylei bats in Thailand: evidence for seasonal preference in disease transmission
    • Wacharapluesadee S, et al. 2010. A longitudinal study of the prevalence of Nipah virus in Pteropus lylei bats in Thailand: evidence for seasonal preference in disease transmission. Vector Borne Zoonotic Dis. 10:183-190.
    • (2010) Vector Borne Zoonotic Dis. , vol.10 , pp. 183-190
    • Wacharapluesadee, S.1
  • 68
    • 84861315738 scopus 로고    scopus 로고
    • Structure of the human metapneumovirus fusion protein with neutralizing antibody identifies a pneumovirus antigenic site
    • Wen X, et al. 2012. Structure of the human metapneumovirus fusion protein with neutralizing antibody identifies a pneumovirus antigenic site.Nat. Struct. Mol. Biol. 19:461- 463.
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 461-463
    • Wen, X.1
  • 69
    • 84857443530 scopus 로고    scopus 로고
    • Ephrin-B2 and ephrin-B3 as functional henipavirus receptors
    • Xu K, Broder CC, Nikolov DB. 2012. Ephrin-B2 and ephrin-B3 as functional henipavirus receptors. Semin. Cell Dev. Biol. 23:116-123.
    • (2012) Semin. Cell Dev. Biol. , vol.23 , pp. 116-123
    • Xu, K.1    Broder, C.C.2    Nikolov, D.B.3
  • 70
    • 0034087050 scopus 로고    scopus 로고
    • Characterization of stable,soluble trimers containing complete ectodomains of human immunodeficiency virus type 1 envelope glycoproteins
    • Yang X, Farzan M, Wyatt R, Sodroski J. 2000. Characterization of stable,soluble trimers containing complete ectodomains of human immunodeficiency virus type 1 envelope glycoproteins. J. Virol. 74:5716-5725.
    • (2000) J. Virol. , vol.74 , pp. 5716-5725
    • Yang, X.1    Farzan, M.2    Wyatt, R.3    Sodroski, J.4
  • 71
    • 0034004321 scopus 로고    scopus 로고
    • Modifications that stabilize human immunodeficiency virus envelope glycoprotein trimers in solution
    • Yang X, et al. 2000. Modifications that stabilize human immunodeficiency virus envelope glycoprotein trimers in solution. J. Virol. 74:4746-4754.
    • (2000) J. Virol. , vol.74 , pp. 4746-4754
    • Yang, X.1
  • 73
    • 30144436116 scopus 로고    scopus 로고
    • Structure of the parainfluenza virus 5 F protein in its metastable, prefusion conformation
    • Yin HS, Wen X, Paterson RG, Lamb RA, Jardetzky TS. 2006. Structure of the parainfluenza virus 5 F protein in its metastable, prefusion conformation.Nature 439:38-44.
    • (2006) Nature , vol.439 , pp. 38-44
    • Yin, H.S.1    Wen, X.2    Paterson, R.G.3    Lamb, R.A.4    Jardetzky, T.S.5


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