메뉴 건너뛰기




Volumn 82, Issue 22, 2008, Pages 11398-11409

Residues in the stalk domain of the Hendra virus G glycoprotein modulate conformational changes associated with receptor binding

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; ISOLEUCINE; MONOCLONAL ANTIBODY; VIRUS GLYCOPROTEIN; ATTACHMENT PROTEIN G; EPHRIN B2; EPHRIN B3; VIRUS ANTIBODY; VIRUS ENVELOPE PROTEIN;

EID: 55549116002     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.02654-07     Document Type: Article
Times cited : (68)

References (53)
  • 4
    • 18744388130 scopus 로고    scopus 로고
    • Person-to-person transmission of Nipah virus during outbreak in Faridpur District, 2004. Health
    • Anonymous
    • Anonymous. 2004. Person-to-person transmission of Nipah virus during outbreak in Faridpur District, 2004. Health Sci. Bull. 2:5-9.
    • (2004) Sci. Bull , vol.2 , pp. 5-9
  • 7
    • 65249163447 scopus 로고    scopus 로고
    • Paramyxovirus entry
    • S. Pöhlmann and G. Simmons ed, in press. Landes Bioscience, Austin, TX
    • Bossart, K. N., and C. C. Broder. Paramyxovirus entry. In S. Pöhlmann and G. Simmons (ed.), Viral entry into host cells, in press. Landes Bioscience, Austin, TX.
    • Viral entry into host cells
    • Bossart, K.N.1    Broder, C.C.2
  • 8
    • 4043123101 scopus 로고    scopus 로고
    • Viral glycoprotein- mediated cell fusion assays using vaccinia virus vectors
    • Bossart, K. N., and C. C. Broder. 2004. Viral glycoprotein- mediated cell fusion assays using vaccinia virus vectors. Methods Mol. Biol. 269:309-332.
    • (2004) Methods Mol. Biol , vol.269 , pp. 309-332
    • Bossart, K.N.1    Broder, C.C.2
  • 10
    • 8644247468 scopus 로고    scopus 로고
    • Biological significance of the second receptor binding site of Newcastle disease virus hemagglutinin-neuraminidase protein
    • Bousse, T. L., G. Taylor, S. Krishnamurthy, A. Portner, S. K. Samal, and T. Takimoto. 2004. Biological significance of the second receptor binding site of Newcastle disease virus hemagglutinin-neuraminidase protein. J. Virol. 78: 13351-13355.
    • (2004) J. Virol , vol.78 , pp. 13351-13355
    • Bousse, T.L.1    Taylor, G.2    Krishnamurthy, S.3    Portner, A.4    Samal, S.K.5    Takimoto, T.6
  • 12
    • 0029360471 scopus 로고    scopus 로고
    • Carroll, M. W., and B. Moss. 1995. E. coli beta-glucuronidase (GUS) as a marker for recombinant vaccinia viruses. BioTechniques 19:352-356.
    • Carroll, M. W., and B. Moss. 1995. E. coli beta-glucuronidase (GUS) as a marker for recombinant vaccinia viruses. BioTechniques 19:352-356.
  • 14
    • 0037375269 scopus 로고    scopus 로고
    • Nipah virus outbreak in Malaysia
    • Chua, K. B. 2003. Nipah virus outbreak in Malaysia. J. Clin. Virol. 26:265-275.
    • (2003) J. Clin. Virol , vol.26 , pp. 265-275
    • Chua, K.B.1
  • 15
    • 35348888403 scopus 로고    scopus 로고
    • Mutations in the stalk of the measles virus hemagglutinin protein decrease fusion but do not interfere with virus-specific interaction with the homologous fusion protein
    • Corey, E. A., and R. M. Iorio. 2007. Mutations in the stalk of the measles virus hemagglutinin protein decrease fusion but do not interfere with virus-specific interaction with the homologous fusion protein. J. Virol. 81:9900-9910.
    • (2007) J. Virol , vol.81 , pp. 9900-9910
    • Corey, E.A.1    Iorio, R.M.2
  • 16
    • 0033762350 scopus 로고    scopus 로고
    • Crystal structure of the multifunctional paramyxovirus hemagglutinin- neuraminidase
    • Crennell, S., T. Takimoto, A. Portner, and G. Taylor. 2000. Crystal structure of the multifunctional paramyxovirus hemagglutinin- neuraminidase. Nat. Struct. Biol. 7:1068-1074.
    • (2000) Nat. Struct. Biol , vol.7 , pp. 1068-1074
    • Crennell, S.1    Takimoto, T.2    Portner, A.3    Taylor, G.4
  • 17
    • 0031303377 scopus 로고    scopus 로고
    • Functional chimeric HN glycoproteins derived from Newcastle disease virus and human parainfluenza virus-3
    • Deng, R., A. M. Mirza, P. J. Mahon, and R. M. Iorio. 1997. Functional chimeric HN glycoproteins derived from Newcastle disease virus and human parainfluenza virus-3. Arch. Virol. Suppl. 13:115-130.
    • (1997) Arch. Virol. Suppl , vol.13 , pp. 115-130
    • Deng, R.1    Mirza, A.M.2    Mahon, P.J.3    Iorio, R.M.4
  • 18
    • 0029006480 scopus 로고
    • Localization of a domain on the paramyxovirus attachment protein required for the promotion of cellular fusion by its homologous fusion protein spike
    • Deng, R., Z. Wang, A. M. Mirza, and R. M. Iorio. 1995. Localization of a domain on the paramyxovirus attachment protein required for the promotion of cellular fusion by its homologous fusion protein spike. Virology 209:457-469.
    • (1995) Virology , vol.209 , pp. 457-469
    • Deng, R.1    Wang, Z.2    Mirza, A.M.3    Iorio, R.M.4
  • 20
    • 0034171207 scopus 로고    scopus 로고
    • A fatal case of Hendra virus infection in a horse in north Queensland: Clinical and epidemiological features
    • Field, H. E., P. C. Barratt, R. J. Hughes, J. Shield, and N. D. Sullivan. 2000. A fatal case of Hendra virus infection in a horse in north Queensland: clinical and epidemiological features. Aust. Vet. J. 78:279-280.
    • (2000) Aust. Vet. J , vol.78 , pp. 279-280
    • Field, H.E.1    Barratt, P.C.2    Hughes, R.J.3    Shield, J.4    Sullivan, N.D.5
  • 21
    • 34748832866 scopus 로고    scopus 로고
    • Henipaviruses: Emerging paramyxoviruses associated with fruit bats
    • Field, H. E., J. S. Mackenzie, and P. Daszak. 2007. Henipaviruses: emerging paramyxoviruses associated with fruit bats. Curr. Top. Microbiol. Immunol. 315:133-159.
    • (2007) Curr. Top. Microbiol. Immunol , vol.315 , pp. 133-159
    • Field, H.E.1    Mackenzie, J.S.2    Daszak, P.3
  • 22
    • 0141454790 scopus 로고    scopus 로고
    • Interacting domains of the HN and F proteins of Newcastle disease virus
    • Gravel, K. A., and T. G. Morrison. 2003. Interacting domains of the HN and F proteins of Newcastle disease virus. J. Virol. 77:11040- 11049.
    • (2003) J. Virol , vol.77 , pp. 11040-11049
    • Gravel, K.A.1    Morrison, T.G.2
  • 23
    • 33746214691 scopus 로고    scopus 로고
    • Evidence of a potential receptor-binding site on the Nipah virus G protein (NiV-G): Identification of globular head residues with a role in fusion promotion and their localization on an NiV-G structural model
    • Guillaume, V., H. Aslan, M. Ainouze, M. Guerbois, T. F. Wild, R. Buckland, and J. P. Langedijk. 2006. Evidence of a potential receptor-binding site on the Nipah virus G protein (NiV-G): identification of globular head residues with a role in fusion promotion and their localization on an NiV-G structural model. J. Virol. 80:7546-7554.
    • (2006) J. Virol , vol.80 , pp. 7546-7554
    • Guillaume, V.1    Aslan, H.2    Ainouze, M.3    Guerbois, M.4    Wild, T.F.5    Buckland, R.6    Langedijk, J.P.7
  • 27
    • 41549166734 scopus 로고    scopus 로고
    • Paramyxoviruses: Different receptors-different mechanisms of fusion
    • Iorio, R. M., and P. J. Mahon. 2008. Paramyxoviruses: different receptors-different mechanisms of fusion. Trends Microbiol. 16:135-137.
    • (2008) Trends Microbiol , vol.16 , pp. 135-137
    • Iorio, R.M.1    Mahon, P.J.2
  • 28
    • 56349144861 scopus 로고    scopus 로고
    • Lamb, R. A., and G. D. Parks. 2007. Paramyxoviridae: the viruses and their replication, p. 1449-1496. In D. M. Knipe and P. M. Howley (ed.), Fields virology, 5th ed., 1. Lippincott Williams & Wilkins, Philadelphia, PA.
    • Lamb, R. A., and G. D. Parks. 2007. Paramyxoviridae: the viruses and their replication, p. 1449-1496. In D. M. Knipe and P. M. Howley (ed.), Fields virology, 5th ed., vol. 1. Lippincott Williams & Wilkins, Philadelphia, PA.
  • 29
    • 29144460894 scopus 로고    scopus 로고
    • Paramyxovirus membrane fusion: Lessons from the F and HN atomic structures
    • Lamb, R. A., R. G. Paterson, and T. S. Jardetzky. 2006. Paramyxovirus membrane fusion: lessons from the F and HN atomic structures. Virology 344:30-37.
    • (2006) Virology , vol.344 , pp. 30-37
    • Lamb, R.A.1    Paterson, R.G.2    Jardetzky, T.S.3
  • 31
    • 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, V. R., and R. M. Iorio. 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
  • 32
    • 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, V. R., and R. M. Iorio. 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
  • 33
    • 56349148469 scopus 로고    scopus 로고
    • Hendra virus findings in Queensland, Australia
    • Paris, France
    • Murray, G. 2006. Hendra virus findings in Queensland, Australia, Vol. 19, no.26. World Organisation for Animal Health (OIE), Paris, France.
    • (2006) World Organisation for Animal Health (OIE) , vol.19 , Issue.26
    • Murray, G.1
  • 36
    • 0028129959 scopus 로고
    • Fusogenic mechanisms of enveloped-virus glycoproteins analyzed by a novel recombinant vaccinia virus-based assay quantitating cell fusion-dependent reporter gene activation
    • Nussbaum, O., C. C. Broder, and E. A. Berger. 1994. Fusogenic mechanisms of enveloped-virus glycoproteins analyzed by a novel recombinant vaccinia virus-based assay quantitating cell fusion-dependent reporter gene activation. J. Virol. 68:5411-5422.
    • (1994) J. Virol , vol.68 , pp. 5411-5422
    • Nussbaum, O.1    Broder, C.C.2    Berger, E.A.3
  • 37
    • 0033934723 scopus 로고    scopus 로고
    • Characterization of a region of the measles virus hemagglutinin sufficient for its dimerization
    • Plemper, R. K., A. L. Hammond, and R. Cattaneo. 2000. Characterization of a region of the measles virus hemagglutinin sufficient for its dimerization. J. Virol. 74:6485-6493.
    • (2000) J. Virol , vol.74 , pp. 6485-6493
    • Plemper, R.K.1    Hammond, A.L.2    Cattaneo, R.3
  • 38
    • 0036238643 scopus 로고    scopus 로고
    • Strength of envelope protein interaction modulates cytopathicity of measles virus
    • Plemper, R. K., A. L. Hammond, D. Gerlier, A. K. Fielding, and R. Cattaneo. 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
  • 39
    • 0030761711 scopus 로고    scopus 로고
    • Detection of an interaction between the HN and F proteins in Newcastle disease virus-infected cells
    • Stone-Hulslander, J., and T. G. Morrison. 1997. Detection of an interaction between the HN and F proteins in Newcastle disease virus-infected cells. J. Virol. 71:6287-6295.
    • (1997) J. Virol , vol.71 , pp. 6287-6295
    • Stone-Hulslander, J.1    Morrison, T.G.2
  • 40
    • 0032899490 scopus 로고    scopus 로고
    • Mutational analysis of heptad repeats in the membrane-proximal region of Newcastle disease virus HN protein
    • Stone-Hulslander, J., and T. G. Morrison. 1999. Mutational analysis of heptad repeats in the membrane-proximal region of Newcastle disease virus HN protein. J. Virol. 73:3630-3637.
    • (1999) J. Virol , vol.73 , pp. 3630-3637
    • Stone-Hulslander, J.1    Morrison, T.G.2
  • 41
    • 0036891868 scopus 로고    scopus 로고
    • Role of the hemagglutinin-neuraminidase protein in the mechanism of paramyxovirus-cell membrane fusion
    • Takimoto, T., G. L. Taylor, H. C. Connaris, S. J. Crennell, and A. Portner. 2002. Role of the hemagglutinin-neuraminidase protein in the mechanism of paramyxovirus-cell membrane fusion. J. Virol. 76:13028- 13033.
    • (2002) J. Virol , vol.76 , pp. 13028-13033
    • Takimoto, T.1    Taylor, G.L.2    Connaris, H.C.3    Crennell, S.J.4    Portner, A.5
  • 42
    • 0029836433 scopus 로고    scopus 로고
    • Functional interaction of paramyxovirus glycoproteins: Identification of a domain in Sendai virus HN which promotes cell fusion
    • Tanabayashi, K., and R. W. Compans. 1996. Functional interaction of paramyxovirus glycoproteins: identification of a domain in Sendai virus HN which promotes cell fusion. J. Virol. 70:6112-6118.
    • (1996) J. Virol , vol.70 , pp. 6112-6118
    • Tanabayashi, K.1    Compans, R.W.2
  • 43
    • 0028850294 scopus 로고
    • Identification of regions on the hemagglutinin- neuraminidase protein of human parainfluenza virus type 2 important for promoting cell fusion
    • Tsurudome, M., M. Kawano, T. Yuasa, N. Tabata, M. Nishio, H. Komada, and Y. Ito. 1995. Identification of regions on the hemagglutinin- neuraminidase protein of human parainfluenza virus type 2 important for promoting cell fusion. Virology 213:190-203.
    • (1995) Virology , vol.213 , pp. 190-203
    • Tsurudome, M.1    Kawano, M.2    Yuasa, T.3    Tabata, N.4    Nishio, M.5    Komada, H.6    Ito, Y.7
  • 44
    • 0032989659 scopus 로고    scopus 로고
    • Amino acid substitutions in a conserved region in the stalk of the Newcastle disease virus HN glycoprotein spike impair its neuraminidase activity in the globular domain
    • Wang, Z., and R. M. Iorio. 1999. Amino acid substitutions in a conserved region in the stalk of the Newcastle disease virus HN glycoprotein spike impair its neuraminidase activity in the globular domain. J. Gen. Virol. 80:749-753.
    • (1999) J. Gen. Virol , vol.80 , pp. 749-753
    • Wang, Z.1    Iorio, R.M.2
  • 45
    • 1642430785 scopus 로고    scopus 로고
    • An oligosaccharide at the C-terminus of the F-specific domain in the stalk of the human parainfluenza virus 3 hemagglutinin-neuraminidase modulates fusion
    • Wang, Z., A. M. Mirza, J. Li, P. J. Mahon, and R. M. Iorio. 2004. An oligosaccharide at the C-terminus of the F-specific domain in the stalk of the human parainfluenza virus 3 hemagglutinin-neuraminidase modulates fusion. Virus Res. 99:177-185.
    • (2004) Virus Res , vol.99 , pp. 177-185
    • Wang, Z.1    Mirza, A.M.2    Li, J.3    Mahon, P.J.4    Iorio, R.M.5
  • 46
    • 26244454780 scopus 로고    scopus 로고
    • Location of, immunogenicity of and relationships between neutralization epitopes on the attachment protein (G) of Hendra virus
    • White, J. R., V. Boyd, G. S. Crameri, C. J. Duch, R. K. van Laar, L. F. Wang, and B. T. Eaton. 2005. Location of, immunogenicity of and relationships between neutralization epitopes on the attachment protein (G) of Hendra virus. J. Gen. Virol. 86:2839-2848.
    • (2005) J. Gen. Virol , vol.86 , pp. 2839-2848
    • White, J.R.1    Boyd, V.2    Crameri, G.S.3    Duch, C.J.4    van Laar, R.K.5    Wang, L.F.6    Eaton, B.T.7
  • 47
    • 48249113696 scopus 로고    scopus 로고
    • Host cell recognition by the henipaviruses: Crystal structures of the Nipah G attachment glycoprotein and its complex with ephrin-B3
    • Xu, K., K. R. Rajashankar, Y. P. Chan, J. P. Himanen, C. C. Broder, and D. B. Nikolov. 2008. Host cell recognition by the henipaviruses: crystal structures of the Nipah G attachment glycoprotein and its complex with ephrin-B3. Proc. Natl. Acad. Sci. USA 105:9953-9958.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 9953-9958
    • Xu, K.1    Rajashankar, K.R.2    Chan, Y.P.3    Himanen, J.P.4    Broder, C.C.5    Nikolov, D.B.6
  • 48
    • 21544470513 scopus 로고    scopus 로고
    • Structure of the uncleaved ectodomain of the paramyxovirus (hPIV3) fusion protein
    • Yin, H. S., R. G. Paterson, X. Wen, R. A. Lamb, and T. S. Jardetzky. 2005. Structure of the uncleaved ectodomain of the paramyxovirus (hPIV3) fusion protein. Proc. Natl. Acad. Sci. USA 102:9288-9293.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 9288-9293
    • Yin, H.S.1    Paterson, R.G.2    Wen, X.3    Lamb, R.A.4    Jardetzky, T.S.5
  • 49
    • 30144436116 scopus 로고    scopus 로고
    • Structure of the parainfluenza virus 5 F protein in its metastable, prefusion conformation
    • Yin, H. S., X. Wen, R. G. Paterson, R. A. Lamb, and T. S. Jardetzky. 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
  • 50
    • 0032567043 scopus 로고    scopus 로고
    • The attachment protein of Hendra virus has high structural similarity but limited primary sequence homology compared with viruses in the genus Paramyxovirus
    • Yu, M., E. Hansson, J. P. Langedijk, B. T. Eaton, and L. F. Wang. 1998. The attachment protein of Hendra virus has high structural similarity but limited primary sequence homology compared with viruses in the genus Paramyxovirus. Virology 251:227-233.
    • (1998) Virology , vol.251 , pp. 227-233
    • Yu, M.1    Hansson, E.2    Langedijk, J.P.3    Eaton, B.T.4    Wang, L.F.5
  • 51
    • 18944375873 scopus 로고    scopus 로고
    • Structural studies of the parainfluenza virus 5 hemagglutinin-neuraminidase tetramer in complex with its receptor, sialyllactose
    • Yuan, P., T. B. Thompson, B. A. Wurzburg, R. G. Paterson, R. A. Lamb, and T. S. Jardetzky. 2005. Structural studies of the parainfluenza virus 5 hemagglutinin-neuraminidase tetramer in complex with its receptor, sialyllactose. Structure (Cambridge) 13:803-815.
    • (2005) Structure (Cambridge) , vol.13 , pp. 803-815
    • Yuan, P.1    Thompson, T.B.2    Wurzburg, B.A.3    Paterson, R.G.4    Lamb, R.A.5    Jardetzky, T.S.6
  • 52
    • 1842614339 scopus 로고    scopus 로고
    • Second sialic acid binding site in Newcastle disease virus hemagglutinin-neuraminidase: Implications for fusion
    • Zaitsev, V., M. von Itzstein, D. Groves, M. Kiefel, T. Takimoto, A. Portner, and G. Taylor. 2004. Second sialic acid binding site in Newcastle disease virus hemagglutinin-neuraminidase: implications for fusion. J. Virol. 78: 3733-3741.
    • (2004) J. Virol , vol.78 , pp. 3733-3741
    • Zaitsev, V.1    von Itzstein, M.2    Groves, D.3    Kiefel, M.4    Takimoto, T.5    Portner, A.6    Taylor, G.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.