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Volumn 86, Issue 10, 2012, Pages 5730-5741

The second receptor binding site of the globular head of the newcastle disease virus hemagglutinin-neuraminidase activates the stalk of multiple paramyxovirus receptor binding proteins to trigger fusion

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; HN PROTEIN; HUMAN PARAINFLUENZA VIRUS 3 RECEPTOR BINDING PROTEIN; HYBRID PROTEIN; NIPAH VIRUS RECEPTOR BINDING PROTEIN; UNCLASSIFIED DRUG; VIRUS RECEPTOR; ZANAMIVIR;

EID: 84861303416     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.06793-11     Document Type: Article
Times cited : (53)

References (69)
  • 2
    • 77954976612 scopus 로고    scopus 로고
    • A quantitative and kinetic fusion protein-triggering assay can discern distinct steps in the Nipah virus membrane fusion cascade
    • Aguilar HC, Aspericueta V, Robinson LR, Aanensen KE, Lee B. 2010. A quantitative and kinetic fusion protein-triggering assay can discern distinct steps in the Nipah virus membrane fusion cascade. J. Virol. 84:8033-8041.
    • (2010) J. Virol. , vol.84 , pp. 8033-8041
    • Aguilar, H.C.1    Aspericueta, V.2    Robinson, L.R.3    Aanensen, K.E.4    Lee, B.5
  • 3
    • 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
    • 50149118372 scopus 로고    scopus 로고
    • Loss of the N-linked glycan at residue 173 of human parainfluenza virus type 1 hemagglutinin-neuraminidase exposes a second receptor-binding site
    • Alymova IV, et al. 2008. Loss of the N-linked glycan at residue 173 of human parainfluenza virus type 1 hemagglutinin-neuraminidase exposes a second receptor-binding site. J. Virol. 82:8400-8410.
    • (2008) J. Virol. , vol.82 , pp. 8400-8410
    • Alymova, I.V.1
  • 5
    • 55549116002 scopus 로고    scopus 로고
    • Residues in the stalk domain of the hendra virus G glycoprotein modulate conformational changes associated with receptor binding
    • Bishop KA, et al. 2008. Residues in the stalk domain of the hendra virus G glycoprotein modulate conformational changes associated with receptor binding. J. Virol. 82:11398-11409.
    • (2008) J. Virol. , vol.82 , pp. 11398-11409
    • Bishop, K.A.1
  • 6
    • 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
  • 7
    • 84855845971 scopus 로고    scopus 로고
    • Structure and mutagenesis of the parainfluenza virus 5 hemagglutinin-neuraminidase stalk domain reveals a four-helix bundle and the role of the stalk in fusion promotion
    • Bose S, et al. 2011. Structure and mutagenesis of the parainfluenza virus 5 hemagglutinin-neuraminidase stalk domain reveals a four-helix bundle and the role of the stalk in fusion promotion. J. Virol. 85:12855-12866.
    • (2011) J. Virol. , vol.85 , pp. 12855-12866
    • Bose, S.1
  • 8
    • 33748513031 scopus 로고    scopus 로고
    • Mutation at residue 523 creates a second receptor binding site on human parainfluenza virus type 1 hemagglutininneuraminidase protein
    • Bousse T, Takimoto T. 2006. Mutation at residue 523 creates a second receptor binding site on human parainfluenza virus type 1 hemagglutininneuraminidase protein. J. Virol. 80:9009-9016.
    • (2006) J. Virol. , vol.80 , pp. 9009-9016
    • Bousse, T.1    Takimoto, T.2
  • 9
    • 8644247468 scopus 로고    scopus 로고
    • Biological significance of the second receptor binding site of Newcastle disease virus hemagglutinin-neuraminidase protein
    • Bousse TL, et al. 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
  • 10
    • 79952820810 scopus 로고    scopus 로고
    • Soluble respiratory syncytial virus fusion protein in the fully cleaved, pretriggered state is triggered by exposure to low-molarity buffer
    • Chaiwatpongsakorn S, Epand RF, Collins PL, Epand RM, Peeples ME. 2011. Soluble respiratory syncytial virus fusion protein in the fully cleaved, pretriggered state is triggered by exposure to low-molarity buffer. J. Virol. 85:3968-3977.
    • (2011) J. Virol. , vol.85 , pp. 3968-3977
    • Chaiwatpongsakorn, S.1    Epand, R.F.2    Collins, P.L.3    Epand, R.M.4    Peeples, M.E.5
  • 11
    • 0036148172 scopus 로고    scopus 로고
    • Probing the sialic acid binding site of the hemagglutinin-neuraminidase of Newcastle disease virus: identification of key amino acids involved in cell binding, catalysis, and fusion
    • Connaris H, et al. 2002. Probing the sialic acid binding site of the hemagglutinin-neuraminidase of Newcastle disease virus: identification of key amino acids involved in cell binding, catalysis, and fusion. J. Virol. 76: 1816-1824.
    • (2002) J. Virol. , vol.76 , pp. 1816-1824
    • Connaris, H.1
  • 12
    • 35348888403 scopus 로고    scopus 로고
    • Mutations in the stalk of the measles virus hemagglutinin protein decrease fusion but do not interfere with virusspecific interaction with the homologous fusion protein
    • Corey EA, Iorio RM. 2007. Mutations in the stalk of the measles virus hemagglutinin protein decrease fusion but do not interfere with virusspecific 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
  • 13
    • 0038279845 scopus 로고    scopus 로고
    • Fusion deficiency induced by mutations at the dimer interface in the Newcastle disease virus hemagglutinin-neuraminidase is due to a temperaturedependent defect in receptor binding
    • Corey EA, Mirza AM, Levandowsky E, Iorio RM. 2003. Fusion deficiency induced by mutations at the dimer interface in the Newcastle disease virus hemagglutinin-neuraminidase is due to a temperaturedependent defect in receptor binding. J. Virol. 77:6913-6922.
    • (2003) J. Virol. , vol.77 , pp. 6913-6922
    • Corey, E.A.1    Mirza, A.M.2    Levandowsky, E.3    Iorio, R.M.4
  • 14
    • 0033762350 scopus 로고    scopus 로고
    • Crystal structure of the multifunctional paramyxovirus hemagglutinin-neuraminidase
    • Crennell S, Takimoto T, Portner A, Taylor G. 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
  • 15
    • 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, Wang Z, Mirza A, Iorio R. 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.3    Iorio, R.4
  • 16
    • 77954683314 scopus 로고    scopus 로고
    • Entry and fusion of emerging paramyxoviruses
    • Dutch RE. 2010. Entry and fusion of emerging paramyxoviruses. PLoS Pathog. 6:e1000881.
    • (2010) PLoS Pathog , vol.6
    • Dutch, R.E.1
  • 17
    • 0034924823 scopus 로고    scopus 로고
    • Mechanisms of viral membrane fusion and its inhibition
    • Eckert DM, Kim PS. 2001. Mechanisms of viral membrane fusion and its inhibition. Annu. Rev. Biochem. 70:777-810.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 777-810
    • Eckert, D.M.1    Kim, P.S.2
  • 19
    • 80055078313 scopus 로고    scopus 로고
    • Premature activation of the paramyxovirus fusion protein before target cell attachment with corruption of the viral fusion machinery
    • Farzan SF, et al. 2011. Premature activation of the paramyxovirus fusion protein before target cell attachment with corruption of the viral fusion machinery. J. Biol. Chem. 286:37945-37954.
    • (2011) J. Biol. Chem. , vol.286 , pp. 37945-37954
    • Farzan, S.F.1
  • 20
    • 0034469926 scopus 로고    scopus 로고
    • The anti-influenza virus agent 4-GU-DANA (Zanamivir) inhibits cell fusion mediated by human parainfluenza virus and influenza virus HA
    • Greengard O, Poltoratskaia N, Leikina E, Zimmerberg J, Moscona A. 2000. The anti-influenza virus agent 4-GU-DANA (Zanamivir) inhibits cell fusion mediated by human parainfluenza virus and influenza virus HA. J. Virol. 74:11108-11114.
    • (2000) J. Virol. , vol.74 , pp. 11108-11114
    • Greengard, O.1    Poltoratskaia, N.2    Leikina, E.3    Zimmerberg, J.4    Moscona, A.5
  • 22
    • 79551638780 scopus 로고    scopus 로고
    • Structure of the measles virus hemagglutinin bound to its cellular receptor SLAM
    • Hashiguchi T, et al. 2011. Structure of the measles virus hemagglutinin bound to its cellular receptor SLAM. Nat. Struct. Mol. Biol. 18:135-141.
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 135-141
    • Hashiguchi, T.1
  • 23
    • 0035132884 scopus 로고    scopus 로고
    • Structural and functional relationship between the receptor recognition and neuraminidase activities of the Newcastle disease virus hemagglutinin-neuraminidase protein: receptor recognition is dependent on neuraminidase activity
    • Iorio RM, et al. 2001. Structural and functional relationship between the receptor recognition and neuraminidase activities of the Newcastle disease virus hemagglutinin-neuraminidase protein: receptor recognition is dependent on neuraminidase activity. J. Virol. 75:1918-1927.
    • (2001) J. Virol. , vol.75 , pp. 1918-1927
    • Iorio, R.M.1
  • 24
    • 41549166734 scopus 로고    scopus 로고
    • Paramyxoviruses: different receptors- different mechanisms of fusion
    • Iorio RM, Mahon PJ. 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
  • 25
    • 70350089241 scopus 로고    scopus 로고
    • Glycoprotein interactions in paramyxovirus fusion
    • Iorio RM, Melanson VR, Mahon PJ. 2009. Glycoprotein interactions in paramyxovirus fusion. Future Virol. 4:335-351.
    • (2009) Future Virol , vol.4 , pp. 335-351
    • Iorio, R.M.1    Melanson, V.R.2    Mahon, P.J.3
  • 26
    • 29144460894 scopus 로고    scopus 로고
    • Paramyxovirus membrane fusion: lessons from the F andHNatomic structures
    • Lamb RA, Paterson RG, Jardetzky TS. 2006. Paramyxovirus membrane fusion: 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
  • 27
    • 0033925033 scopus 로고    scopus 로고
    • Determination of polymorphonuclear neutrophil adhesion receptors. Effect of pre-analytic factors
    • (In French.)
    • Latger-Cannard V, et al. 2000. Determination of polymorphonuclear neutrophil adhesion receptors. Effect of pre-analytic factors. J. Mal. Vasc. 25:181-186. (In French.)
    • (2000) J. Mal. Vasc. , vol.25 , pp. 181-186
    • Latger-Cannard, V.1
  • 28
    • 0034095863 scopus 로고    scopus 로고
    • Use of standard for quantitation of adhesion of polynuclear neutrophils by flow cytometry
    • (In French.)
    • Latger-Cannard V, et al. 2000. Use of standard for quantitation of adhesion of polynuclear neutrophils by flow cytometry. Ann. Biol. Clin. (Paris) 58:337-343. (In French.)
    • (2000) Ann. Biol. Clin. (Paris) , vol.58 , pp. 337-343
    • Latger-Cannard, V.1
  • 29
    • 0346654073 scopus 로고    scopus 로고
    • Structure of the haemagglutininneuraminidase from human parainfluenza virus type III
    • Lawrence MC, et al. 2004. Structure of the haemagglutininneuraminidase from human parainfluenza virus type III. J. Mol. Biol. 335:1343-1357.
    • (2004) J. Mol. Biol. , vol.335 , pp. 1343-1357
    • Lawrence, M.C.1
  • 30
    • 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
  • 31
    • 82755163036 scopus 로고    scopus 로고
    • Capturing a fusion intermediate of influenza hemagglutinin with a cholesterol-conjugated peptide: a new antiviral strategy for influenza virus
    • Lee KK, et al. 2011. Capturing a fusion intermediate of influenza hemagglutinin with a cholesterol-conjugated peptide: a new antiviral strategy for influenza virus. J. Biol. Chem. 286:42141-42149.
    • (2011) J. Biol. Chem. , vol.286 , pp. 42141-42149
    • Lee, K.K.1
  • 32
    • 2342512265 scopus 로고    scopus 로고
    • Mutated form of the Newcastle disease virus hemagglutinin-neuraminidase interacts with the homologous fusion protein despite deficiencies in both receptor recognition and fusion promotion
    • Li J, Quinlan E, Mirza A, Iorio RM. 2004. Mutated form of the Newcastle disease virus hemagglutinin-neuraminidase interacts with the homologous fusion protein despite deficiencies in both receptor recognition and fusion promotion. J. Virol. 78:5299-5310.
    • (2004) J. Virol. , vol.78 , pp. 5299-5310
    • Li, J.1    Quinlan, E.2    Mirza, A.3    Iorio, R.M.4
  • 33
    • 80655142480 scopus 로고    scopus 로고
    • Role of the two sialic acid binding sites on the Newcastle disease virus HN protein in triggering the interaction with the F protein required for the promotion of fusion
    • Mahon PJ, Mirza AM, Iorio RM. 2011. Role of the two sialic acid binding sites on the Newcastle disease virus HN protein in triggering the interaction with the F protein required for the promotion of fusion. J. Virol. 85:12079-12082.
    • (2011) J. Virol. , vol.85 , pp. 12079-12082
    • Mahon, P.J.1    Mirza, A.M.2    Iorio, R.M.3
  • 34
    • 79955975776 scopus 로고    scopus 로고
    • Triggering of the Newcastle disease virus fusion protein by a chimeric attachment protein that binds to Nipah virus receptors
    • Mirza AM, et al. 2011. Triggering of the Newcastle disease virus fusion protein by a chimeric attachment protein that binds to Nipah virus receptors. J. Biol. Chem. 286:17851-17860.
    • (2011) J. Biol. Chem. , vol.286 , pp. 17851-17860
    • Mirza, A.M.1
  • 35
    • 77649103933 scopus 로고    scopus 로고
    • N-linked glycan at residue 523 of human parainfluenza virus type 3 hemagglutinin-neuraminidase masks a second receptor-binding site
    • Mishin VP, et al. 2010. N-linked glycan at residue 523 of human parainfluenza virus type 3 hemagglutinin-neuraminidase masks a second receptor-binding site. J. Virol. 84:3094-3100.
    • (2010) J. Virol. , vol.84 , pp. 3094-3100
    • Mishin, V.P.1
  • 36
    • 0029914507 scopus 로고    scopus 로고
    • Alpha complementation of LacZ in mammalian cells
    • Moosmann P, Rusconi S. 1996. Alpha complementation of LacZ in mammalian cells. Nucleic Acids Res. 24:1171-1172.
    • (1996) Nucleic Acids Res , vol.24 , pp. 1171-1172
    • Moosmann, P.1    Rusconi, S.2
  • 37
    • 22144445629 scopus 로고    scopus 로고
    • Entry of parainfluenza virus into cells as a target for interrupting childhood respiratory disease
    • Moscona A. 2005. Entry of parainfluenza virus into cells as a target for interrupting childhood respiratory disease. J. Clin. Invest. 115:1688-1698.
    • (2005) J. Clin. Invest. , vol.115 , pp. 1688-1698
    • Moscona, A.1
  • 38
    • 0025734272 scopus 로고
    • Properties of the human parainfluenza virus type 3 RNA polymerase/replicase in vitro: consensus with other negativestranded RNA viruses
    • Moscona A, Peluso R. 1991. Properties of the human parainfluenza virus type 3 RNA polymerase/replicase in vitro: consensus with other negativestranded RNA viruses. J. Virol. 65:4470-4474.
    • (1991) J. Virol. , vol.65 , pp. 4470-4474
    • Moscona, A.1    Peluso, R.2
  • 39
    • 0026726805 scopus 로고
    • Fusion properties of cells infected with human parainfluenza virus type 3: receptor requirements for viral spread and virus-mediated membrane fusion
    • Moscona A, Peluso RW. 1992. Fusion properties of cells infected with human parainfluenza virus type 3: receptor requirements for viral spread and virus-mediated membrane fusion. J. Virol. 66:6280-6287.
    • (1992) J. Virol. , vol.66 , pp. 6280-6287
    • Moscona, A.1    Peluso, R.W.2
  • 40
    • 0027381637 scopus 로고
    • Relative affinity of the human parainfluenza virus 3 hemagglutinin-neuraminidase for sialic acid correlates with virus-induced fusion activity
    • Moscona A, Peluso RW. 1993. Relative affinity of the human parainfluenza virus 3 hemagglutinin-neuraminidase for sialic acid correlates with virus-induced fusion activity. J. Virol. 67:6463-6468.
    • (1993) J. Virol. , vol.67 , pp. 6463-6468
    • Moscona, A.1    Peluso, R.W.2
  • 41
    • 0037213302 scopus 로고    scopus 로고
    • Mutations in human parainfluenza virus type 3 HN causing increased receptor binding activity and resistance to the transition state sialic acid analog 4-GU-DANA (zanamivir)
    • Murrell M, Porotto M, Weber T, Greengard O, Moscona A. 2003. Mutations in human parainfluenza virus type 3 HN causing increased receptor binding activity and resistance to the transition state sialic acid analog 4-GU-DANA (zanamivir). J. Virol. 77:309-317.
    • (2003) J. Virol. , vol.77 , pp. 309-317
    • Murrell, M.1    Porotto, M.2    Weber, T.3    Greengard, O.4    Moscona, A.5
  • 42
    • 79551621397 scopus 로고    scopus 로고
    • The heads of the measles virus attachment protein move to transmit the fusion-triggering signal
    • Navaratnarajah CK, et al. 2011. The heads of the measles virus attachment protein move to transmit the fusion-triggering signal. Nat. Struct. Mol. Biol. 18:128-134.
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 128-134
    • Navaratnarajah, C.K.1
  • 43
    • 22944445501 scopus 로고    scopus 로고
    • EphrinB2 is the entry receptor for Nipah virus, an emergent deadly paramyxovirus
    • Negrete OA, et al. 2005. EphrinB2 is the entry receptor for Nipah virus, an emergent deadly paramyxovirus. Nature 436:401-405.
    • (2005) Nature , vol.436 , pp. 401-405
    • Negrete, O.A.1
  • 44
    • 80052315535 scopus 로고    scopus 로고
    • Tumor cell marker PVRL4 (nectin 4) is an epithelial cell receptor for measles virus
    • Noyce RS, et al. 2011. Tumor cell marker PVRL4 (nectin 4) is an epithelial cell receptor for measles virus. PLoS Pathog. 7:e1002240.
    • (2011) PLoS Pathog , vol.7
    • Noyce, R.S.1
  • 45
    • 70349747076 scopus 로고    scopus 로고
    • Probing the spatial organization of measles virus fusion complexes
    • Paal T, et al. 2009. Probing the spatial organization of measles virus fusion complexes. J. Virol. 83:10480-10493.
    • (2009) J. Virol. , vol.83 , pp. 10480-10493
    • Paal, T.1
  • 46
    • 67449093027 scopus 로고    scopus 로고
    • Human parainfluenza virus infection of the airway epithelium: the viral hemagglutinin-neuraminidase regulates fusion protein activation and modulates infectivity
    • Palermo L, et al. 2009. Human parainfluenza virus infection of the airway epithelium: the viral hemagglutinin-neuraminidase regulates fusion protein activation and modulates infectivity. J. Virol. 83:6900-6908.
    • (2009) J. Virol. , vol.83 , pp. 6900-6908
    • Palermo, L.1
  • 47
    • 34548169552 scopus 로고    scopus 로고
    • Fusion promotion by a paramyxovirus hemagglutinin-neuraminidase protein: pH modulation of receptor avidity of binding sites I and II
    • Palermo LM, Porotto M, Greengard O, Moscona A. 2007. Fusion promotion by a paramyxovirus hemagglutinin-neuraminidase protein: pH modulation of receptor avidity of binding sites I and II. J. Virol. 81: 9152-9161.
    • (2007) J. Virol. , vol.81 , pp. 9152-9161
    • Palermo, L.M.1    Porotto, M.2    Greengard, O.3    Moscona, A.4
  • 48
    • 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
  • 49
    • 84855270854 scopus 로고    scopus 로고
    • Spring-loaded model revisited: Paramyxovirus fusion requires engagement of a receptor binding protein beyond initial triggering of the fusion protein
    • Porotto M, et al. 2011. Spring-loaded model revisited: Paramyxovirus fusion requires engagement of a receptor binding protein beyond initial triggering of the fusion protein. J. Virol. 85:12867-12880.
    • (2011) J. Virol. , vol.85 , pp. 12867-12880
    • Porotto, M.1
  • 50
    • 31144439130 scopus 로고    scopus 로고
    • Paramyxovirus receptor-binding molecules: engagement of one site on the hemagglutinin-neuraminidase protein modulates activity at the second site
    • Porotto M, et al. 2006. Paramyxovirus receptor-binding molecules: engagement of one site on the hemagglutinin-neuraminidase protein modulates activity at the second site. J. Virol. 80:1204-1213.
    • (2006) J. Virol. , vol.80 , pp. 1204-1213
    • Porotto, M.1
  • 51
    • 33947363286 scopus 로고    scopus 로고
    • A second receptor binding site on the human parainfluenza 3 hemagglutininneuraminidase contributes to activation of the fusion mechanism
    • Porotto M, Fornabaio M, Kellogg G, Moscona A. 2007. A second receptor binding site on the human parainfluenza 3 hemagglutininneuraminidase contributes to activation of the fusion mechanism. J. Virol. 81:3216-3228.
    • (2007) J. Virol. , vol.81 , pp. 3216-3228
    • Porotto, M.1    Fornabaio, M.2    Kellogg, G.3    Moscona, A.4
  • 52
    • 0034909749 scopus 로고    scopus 로고
    • Human parainfluenza virus type 3 HN-receptor interaction: the effect of 4-GU-DANA on a neuraminidase-deficient variant
    • Porotto M, Greengard O, Poltoratskaia N, Horga M-A, Moscona A. 2001. Human parainfluenza virus type 3 HN-receptor interaction: the effect of 4-GU-DANA on a neuraminidase-deficient variant. J. Virol. 75: 7481-7488.
    • (2001) J. Virol. , vol.75 , pp. 7481-7488
    • Porotto, M.1    Greengard, O.2    Poltoratskaia, N.3    Horga, M.-A.4    Moscona, A.5
  • 53
    • 13444270795 scopus 로고    scopus 로고
    • Influence of the human parainfluenza virus 3 attachment protein's neuraminidase activity on its capacity to activate the fusion protein
    • Porotto M, Murrell M, Greengard O, Doctor L, Moscona A. 2005. Influence of the human parainfluenza virus 3 attachment protein's neuraminidase activity on its capacity to activate the fusion protein. J. Virol. 79:2383-2392.
    • (2005) J. Virol. , vol.79 , pp. 2383-2392
    • Porotto, M.1    Murrell, M.2    Greengard, O.3    Doctor, L.4    Moscona, A.5
  • 54
    • 10044296412 scopus 로고    scopus 로고
    • Inhibition of parainfluenza type 3 and Newcastle disease virus hemagglutinin-neuraminidase receptor binding: effect of receptor avidity and steric hindrance at the inhibitor binding sites
    • Porotto M, et al. 2004. Inhibition of parainfluenza type 3 and Newcastle disease virus hemagglutinin-neuraminidase receptor binding: effect of receptor avidity and steric hindrance at the inhibitor binding sites. J. Virol. 78:13911-13919.
    • (2004) J. Virol. , vol.78 , pp. 13911-13919
    • Porotto, M.1
  • 55
    • 0037333844 scopus 로고    scopus 로고
    • Triggering of human parainfluenza virus 3 fusion protein(F) by the hemagglutininneuraminidase (HN): an HN mutation diminishing the rate of F activation and fusion
    • Porotto M, Murrell M, Greengard O, Moscona A. 2003. Triggering of human parainfluenza virus 3 fusion protein(F) by the hemagglutininneuraminidase (HN): an HN mutation diminishing the rate of F activation and fusion. J. Virol. 77:3647-3654.
    • (2003) J. Virol. , vol.77 , pp. 3647-3654
    • Porotto, M.1    Murrell, M.2    Greengard, O.3    Moscona, A.4
  • 56
    • 84855272388 scopus 로고    scopus 로고
    • Mechanism of fusion triggering by human parainfluenza virus type III: communication between the viral glycoproteins during entry
    • Porotto M, Palmer SG, Palermo LM, Moscona A. 2012. Mechanism of fusion triggering by human parainfluenza virus type III: communication between the viral glycoproteins during entry. J. Biol. Chem. 287:778-793.
    • (2012) J. Biol. Chem. , vol.287 , pp. 778-793
    • Porotto, M.1    Palmer, S.G.2    Palermo, L.M.3    Moscona, A.4
  • 58
    • 33645453800 scopus 로고    scopus 로고
    • Structural analysis of a designed inhibitor complexed with the hemagglutinin-neuraminidase of Newcastle disease virus
    • Ryan C, et al. 2006. Structural analysis of a designed inhibitor complexed with the hemagglutinin-neuraminidase of Newcastle disease virus. Glycoconj. J. 23:135-141.
    • (2006) Glycoconj. J. , vol.23 , pp. 135-141
    • Ryan, C.1
  • 59
    • 37749019200 scopus 로고    scopus 로고
    • Viral and developmental cell fusion mechanisms: conservation and divergence
    • Sapir A, Avinoam O, Podbilewicz B, Chernomordik LV. 2008. Viral and developmental cell fusion mechanisms: conservation and divergence. Dev. Cell 14:11-21.
    • (2008) Dev. Cell , vol.14 , pp. 11-21
    • Sapir, A.1    Avinoam, O.2    Podbilewicz, B.3    Chernomordik, L.V.4
  • 60
    • 77957196709 scopus 로고    scopus 로고
    • Side chain packing below the fusion peptide strongly modulates triggering of the Hendra virus F protein
    • Smith EC, Dutch RE. 2010. Side chain packing below the fusion peptide strongly modulates triggering of the Hendra virus F protein. J. Virol. 84: 10928-10932.
    • (2010) J. Virol. , vol.84 , pp. 10928-10932
    • Smith, E.C.1    Dutch, R.E.2
  • 61
    • 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
  • 62
    • 0032722076 scopus 로고    scopus 로고
    • Standardisation of a procedure for quantifying surface antigens by indirect immunofluorescence
    • Smith KB, Ellis SA. 1999. Standardisation of a procedure for quantifying surface antigens by indirect immunofluorescence. J. Immunol. Methods 228:29-36.
    • (1999) J. Immunol. Methods , vol.228 , pp. 29-36
    • Smith, K.B.1    Ellis, S.A.2
  • 63
    • 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, Mirza AM, Li J, Mahon PJ, Iorio RM. 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
  • 65
    • 45849108331 scopus 로고    scopus 로고
    • Structures and mechanisms of viral membrane fusion proteins: multiple variations on a common theme
    • White JM, Delos SE, Brecher M, Schornberg K. 2008. Structures and mechanisms of viral membrane fusion proteins: multiple variations on a common theme. Crit. Rev. Biochem. Mol. Biol. 43:189-219.
    • (2008) Crit. Rev. Biochem. Mol. Biol. , vol.43 , pp. 189-219
    • White, J.M.1    Delos, S.E.2    Brecher, M.3    Schornberg, K.4
  • 67
    • 80052564183 scopus 로고    scopus 로고
    • Structure of the Newcastle disease virus hemagglutinin-neuraminidase (HN) ectodomain reveals a four-helix bundle stalk
    • Yuan P, et al. 2011. Structure of the Newcastle disease virus hemagglutinin-neuraminidase (HN) ectodomain reveals a four-helix bundle stalk. Proc. Natl. Acad. Sci. U. S. A. 108:14920-14925.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 14920-14925
    • Yuan, P.1
  • 68
    • 18944375873 scopus 로고    scopus 로고
    • Structural studies of the parainfluenza virus 5 hemagglutinin-neuraminidase tetramer in complex with its receptor, sialyllactose
    • Yuan P, et al. 2005. Structural studies of the parainfluenza virus 5 hemagglutinin-neuraminidase tetramer in complex with its receptor, sialyllactose. Structure 13:803-815.
    • (2005) Structure , vol.13 , pp. 803-815
    • Yuan, P.1
  • 69
    • 1842614339 scopus 로고    scopus 로고
    • Second sialic acid binding site in Newcastle disease virus hemagglutinin-neuraminidase: implications for fusion
    • Zaitsev V, et al. 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


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