메뉴 건너뛰기




Volumn 85, Issue 24, 2011, Pages 12867-12880

Spring-loaded model revisited: Paramyxovirus fusion requires engagement of a receptor binding protein beyond initial triggering of the fusion protein

Author keywords

[No Author keywords available]

Indexed keywords

HEMAGGLUTININ NEURAMINIDASE; HYBRID PROTEIN; UNCLASSIFIED DRUG;

EID: 84855270854     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.05873-11     Document Type: Article
Times cited : (46)

References (82)
  • 1
    • 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, H. C., V. Aspericueta, L. R. Robinson, K. E. Aanensen, and B. Lee. 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
  • 2
    • 33646447520 scopus 로고    scopus 로고
    • N-glycans on Nipah virus fusion protein protect against neutralization but reduce membrane fusion and viral entry
    • Aguilar, H. C., 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
  • 3
    • 33645996373 scopus 로고    scopus 로고
    • Expanded tropism and altered activation of a retroviral glycoprotein resistant to an entry inhibitor peptide
    • Amberg, S. M., R. C. Netter, G. Simmons, and P. Bates. 2006. Expanded tropism and altered activation of a retroviral glycoprotein resistant to an entry inhibitor peptide. J. Virol. 80:353-359.
    • (2006) J. Virol. , vol.80 , pp. 353-359
    • Amberg, S.M.1    Netter, R.C.2    Simmons, G.3    Bates, P.4
  • 4
    • 36749035394 scopus 로고    scopus 로고
    • Bimolecular complementation reveals that glycoproteins gB and gH/gL of herpes simplex virus interact with each other during cell fusion
    • Atanasiu, D., et al. 2007. Bimolecular complementation reveals that glycoproteins gB and gH/gL of herpes simplex virus interact with each other during cell fusion. Proc. Natl. Acad. Sci. U. S. A. 104:18718-18723.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 18718-18723
    • Atanasiu, D.1
  • 5
    • 0033106334 scopus 로고    scopus 로고
    • Structural basis for paramyxovirus-mediated membrane fusion
    • Baker, K. A., R. E. Dutch, R. A. Lamb, and T. S. Jardetzky. 1999. Structural basis for paramyxovirus-mediated membrane fusion. Mol. Cell 3:309-319.
    • (1999) Mol. Cell , vol.3 , pp. 309-319
    • Baker, K.A.1    Dutch, R.E.2    Lamb, R.A.3    Jardetzky, T.S.4
  • 6
    • 55549116002 scopus 로고    scopus 로고
    • Residues in the stalk domain of the Hendra virus g glycoprotein modulate conformational changes associated with receptor binding
    • Bishop, K. A., 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
  • 7
    • 0031460632 scopus 로고    scopus 로고
    • Influenza hemagglutinin is spring-loaded by a metastable native conformation
    • Carr, C. M., C. Chaudhry, and P. S. Kim. 1997. Influenza hemagglutinin is spring-loaded by a metastable native conformation. Proc. Natl. Acad. Sci. U. S. A. 94:14306-14313.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 14306-14313
    • Carr, C.M.1    Chaudhry, C.2    Kim, P.S.3
  • 8
    • 0027253445 scopus 로고
    • A spring-loaded mechanism for the conformational change of influenza hemagglutinin
    • Carr, C. M., and P. S. Kim. 1993. A spring-loaded mechanism for the conformational change of influenza hemagglutinin. Cell 73:823-832.
    • (1993) Cell , vol.73 , pp. 823-832
    • Carr, C.M.1    Kim, P.S.2
  • 9
    • 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., R. F. Epand, P. L. Collins, R. M. Epand, and M. E. Peeples. 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
  • 10
    • 70350277403 scopus 로고    scopus 로고
    • Bimolecular complementation of paramyxovirus fusion and hemagglutinin-neuraminidase proteins enhances fusion: implications for the mechanism of fusion triggering
    • Connolly, S. A., G. P. Leser, T. S. Jardetzky, and R. A. Lamb. 2009. Bimolecular complementation of paramyxovirus fusion and hemagglutinin-neuraminidase 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
  • 11
    • 33845212315 scopus 로고    scopus 로고
    • Refolding of a paramyxovirus F protein from prefusion to postfusion conformations observed by liposome binding and electron microscopy
    • Connolly, S. A., G. P. Leser, H. S. Yin, T. S. Jardetzky, and R. A. Lamb. 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
  • 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, E. A., and R. M. Iorio. 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
    • 14744272823 scopus 로고    scopus 로고
    • Receptor-induced conformational changes in the SU subunit of the avian sarcoma/leukosis virus A envelope protein: implications for fusion activation
    • Delos, S. E., J. A. Godby, and J. M. White. 2005. Receptor-induced conformational changes in the SU subunit of the avian sarcoma/leukosis virus A envelope protein: implications for fusion activation. J. Virol. 79:3488-3499.
    • (2005) J. Virol. , vol.79 , pp. 3488-3499
    • Delos, S.E.1    Godby, J.A.2    White, J.M.3
  • 14
    • 77954683314 scopus 로고    scopus 로고
    • Entry and fusion of emerging paramyxoviruses
    • Dutch, R. E. 2010. Entry and fusion of emerging paramyxoviruses. PLoS Pathog. 6:e1000881.
    • (2010) PLoS Pathog. , vol.6
    • Dutch, R.E.1
  • 16
    • 0034924823 scopus 로고    scopus 로고
    • Mechanisms of viral membrane fusion and its inhibition
    • Eckert, D. M., and P. S. Kim. 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
  • 17
    • 64849114224 scopus 로고    scopus 로고
    • Antibody recognition of a highly conserved influenza virus epitope
    • Ekiert, D. C., et al. 2009. Antibody recognition of a highly conserved influenza virus epitope. Science 324:246-251.
    • (2009) Science , vol.324 , pp. 246-251
    • Ekiert, D.C.1
  • 18
    • 80055078313 scopus 로고    scopus 로고
    • Premature activation of the paramyxovirus fusion protein before target cell attachment: corruption of the viral fusion machinery
    • [Epub ahead of print.] doi:10.1074/jbc.M111.256248
    • Farzan, S., et al. 2011. Premature activation of the paramyxovirus fusion protein before target cell attachment: corruption of the viral fusion machinery. J. Biol. Chem. [Epub ahead of print.] doi:10.1074/jbc.M111.256248.
    • (2011) J. Biol. Chem.
    • Farzan, S.1
  • 19
    • 0037569181 scopus 로고    scopus 로고
    • Enfuvirtide, a new drug for HIV infection
    • Fletcher, C. V. 2003. Enfuvirtide, a new drug for HIV infection. Lancet 361:1577-1578.
    • (2003) Lancet , vol.361 , pp. 1577-1578
    • Fletcher, C.V.1
  • 20
    • 0029914834 scopus 로고    scopus 로고
    • Mutations at two conserved acidic amino acids in the glycoprotein of vesicular stomatitis virus affect pH-dependent conformational changes and reduce the pH threshold for membrane fusion
    • Fredericksen, B. L., and M. A. Whitt. 1996. Mutations at two conserved acidic amino acids in the glycoprotein of vesicular stomatitis virus affect pH-dependent conformational changes and reduce the pH threshold for membrane fusion. Virology 217:49-57.
    • (1996) Virology , vol.217 , pp. 49-57
    • Fredericksen, B.L.1    Whitt, M.A.2
  • 21
    • 0028871747 scopus 로고
    • Receptor-induced conformational changes in the subgroup A avian leukosis and sarcoma virus envelope glycoprotein
    • Gilbert, J. M., L. D. Hernandez, J. W. Balliet, P. Bates, and J. M. White. 1995. Receptor-induced conformational changes in the subgroup A avian leukosis and sarcoma virus envelope glycoprotein. J. Virol. 69:7410-7415.
    • (1995) J. Virol. , vol.69 , pp. 7410-7415
    • Gilbert, J.M.1    Hernandez, L.D.2    Balliet, J.W.3    Bates, P.4    White, J.M.5
  • 22
    • 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., N. Poltoratskaia, E. Leikina, J. Zimmerberg, and A. Moscona. 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
  • 24
    • 0030753409 scopus 로고    scopus 로고
    • Structure-based identification of an inducer of the low-pH conformational change in the influenza virus hemagglutinin: irreversible inhibition of infectivity
    • Hoffman, L. R., I. D. Kuntz, and J. M. White. 1997. Structure-based identification of an inducer of the low-pH conformational change in the influenza virus hemagglutinin: irreversible inhibition of infectivity. J. Virol. 71:8808-8820.
    • (1997) J. Virol. , vol.71 , pp. 8808-8820
    • Hoffman, L.R.1    Kuntz, I.D.2    White, J.M.3
  • 25
    • 0034469766 scopus 로고    scopus 로고
    • Mechanism of interference mediated by human parainfluenza virus type 3 infection
    • Horga, M. A., et al. 2000. Mechanism of interference mediated by human parainfluenza virus type 3 infection. J. Virol. 74:11792-11799.
    • (2000) J. Virol. , vol.74 , pp. 11792-11799
    • Horga, M.A.1
  • 26
    • 0036241055 scopus 로고    scopus 로고
    • Visualization of interactions among bZIP and Rel family proteins in living cells using bimolecular fluorescence complementation
    • Hu, C. D., Y. Chinenov, and T. K. Kerppola. 2002. Visualization of interactions among bZIP and Rel family proteins in living cells using bimolecular fluorescence complementation. Mol. Cell 9:789-798.
    • (2002) Mol. Cell , vol.9 , pp. 789-798
    • Hu, C.D.1    Chinenov, Y.2    Kerppola, T.K.3
  • 27
    • 0037995710 scopus 로고    scopus 로고
    • Simultaneous visualization of multiple protein interactions in living cells using multicolor fluorescence complementation analysis
    • Hu, C. D., and T. K. Kerppola. 2003. Simultaneous visualization of multiple protein interactions in living cells using multicolor fluorescence complementation analysis. Nat. Biotechnol. 21:539-545.
    • (2003) Nat. Biotechnol. , vol.21 , pp. 539-545
    • Hu, C.D.1    Kerppola, T.K.2
  • 28
    • 65249085618 scopus 로고    scopus 로고
    • Addition of a cholesterol group to an HIV-1 peptide fusion inhibitor dramatically increases its antiviral potency
    • Ingallinella, P., et al. 2009. Addition of a cholesterol group to an HIV-1 peptide fusion inhibitor dramatically increases its antiviral potency. Proc. Natl. Acad. Sci. U. S. A. 106:5801-5806.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 5801-5806
    • Ingallinella, P.1
  • 29
    • 70350089241 scopus 로고    scopus 로고
    • Glycoprotein interactions in paramyxovirus fusion
    • Iorio, R. M., V. R. Melanson, and P. J. Mahon. 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
  • 30
    • 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
    • 9044234408 scopus 로고    scopus 로고
    • Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion
    • Lambert, D. M., et al. 1996. Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion. Proc. Natl. Acad. Sci. U. S. A. 93:2186-2191.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 2186-2191
    • Lambert, D.M.1
  • 32
    • 79960918320 scopus 로고    scopus 로고
    • Modes of paramyxovirus fusion: a henipavirus perspective
    • Lee, B., and Z. A. Ataman. 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
  • 33
    • 11144220563 scopus 로고    scopus 로고
    • Decreased dependence on receptor recognition for the fusion promotion activity of L289A-mutated Newcastle disease virus fusion protein correlates with a monoclonal antibody-detected conformational change
    • Li, J., V. R. Melanson, A. M. Mirza, and R. M. Iorio. 2005. Decreased dependence on receptor recognition for the fusion promotion activity of L289A-mutated Newcastle disease virus fusion protein correlates with a monoclonal antibody-detected conformational change. J. Virol. 79:1180-1190.
    • (2005) J. Virol. , vol.79 , pp. 1180-1190
    • Li, J.1    Melanson, V.R.2    Mirza, A.M.3    Iorio, R.M.4
  • 34
    • 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., E. Quinlan, A. Mirza, and R. M. Iorio. 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
  • 35
    • 77956857860 scopus 로고    scopus 로고
    • Bimolecular fluorescence complementation analysis of eukaryotic fusion products
    • Lin, H. P., C. Vincenz, K. W. Eliceiri, T. K. Kerppola, and B. M. Ogle. 2010. Bimolecular fluorescence complementation analysis of eukaryotic fusion products. Biol. Cell 102:525-537.
    • (2010) Biol. Cell , vol.102 , pp. 525-537
    • Lin, H.P.1    Vincenz, C.2    Eliceiri, K.W.3    Kerppola, T.K.4    Ogle, B.M.5
  • 36
    • 0028834461 scopus 로고
    • A trimeric structural domain of the HIV-1 transmembrane glycoprotein
    • Lu, M., S. C. Blacklow, and P. S. Kim. 1995. A trimeric structural domain of the HIV-1 transmembrane glycoprotein. Nat. Struct. Biol. 2:1075-1082.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 1075-1082
    • Lu, M.1    Blacklow, S.C.2    Kim, P.S.3
  • 37
    • 41149136590 scopus 로고    scopus 로고
    • Electron cryomicroscopy reveals different F1+F2 protein states in intact parainfluenza virions
    • Ludwig, K., et al. 2008. Electron cryomicroscopy reveals different F1+F2 protein states in intact parainfluenza virions. J. Virol. 82:3775-3781.
    • (2008) J. Virol. , vol.82 , pp. 3775-3781
    • Ludwig, K.1
  • 38
    • 80655142480 scopus 로고    scopus 로고
    • Role of the two sialic acid binding sites on the NDV HN protein in triggering the interaction with the F protein required for the promotion of fusion
    • [Epub ahead of print.] doi:10.1128/JVI.05679-11
    • Mahon, P. J., A. M. Mirza, and R. M. Iorio. 2011. Role of the two sialic acid binding sites on the NDV HN protein in triggering the interaction with the F protein required for the promotion of fusion. J. Virol. [Epub ahead of print.] doi:10.1128/JVI.05679-11.
    • (2011) J. Virol.
    • Mahon, P.J.1    Mirza, A.M.2    Iorio, R.M.3
  • 39
    • 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
  • 40
    • 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, A. M., 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
  • 41
    • 0029914507 scopus 로고    scopus 로고
    • Alpha complementation of LacZ in mammalian cells
    • Moosmann, P., and S. Rusconi. 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
  • 42
    • 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. Investig. 115:1688-1698.
    • (2005) J. Clin. Investig. , vol.115 , pp. 1688-1698
    • Moscona, A.1
  • 43
    • 0034979362 scopus 로고    scopus 로고
    • A single amino acid alteration in the human parainfluenza virus type 3 HN confers resistance to both binding inhibition and neuraminidase inhibition by the antiviral agent 4-GU-DANA (zanamivir)
    • Murrell, M., O. Greengard, M. Porotto, N. Poltoratskaia, and A. Moscona. 2001. A single amino acid alteration in the human parainfluenza virus type 3 HN confers resistance to both binding inhibition and neuraminidase inhibition by the antiviral agent 4-GU-DANA (zanamivir). J. Virol. 75:6310-6320.
    • (2001) J. Virol. , vol.75 , pp. 6310-6320
    • Murrell, M.1    Greengard, O.2    Porotto, M.3    Poltoratskaia, N.4    Moscona, A.5
  • 44
    • 0037213302 scopus 로고    scopus 로고
    • Mutations in human parainfluenza virus type 3 hemagglutinin-neuraminidase causing increased receptor binding activity and resistance to the transition state sialic acid analog 4-GU-DANA (zanamivir)
    • Murrell, M., M. Porotto, T. Weber, O. Greengard, and A. Moscona. 2003. Mutations in human parainfluenza virus type 3 hemagglutinin-neuraminidase 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
  • 45
    • 79551621397 scopus 로고    scopus 로고
    • The heads of the measles virus attachment protein move to transmit the fusion-triggering signal
    • Navaratnarajah, C. K., 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
  • 46
    • 10044241596 scopus 로고    scopus 로고
    • Heptad repeat 2-based peptides inhibit avian sarcoma and leukosis virus subgroup a infection and identify a fusion intermediate
    • Netter, R. C., et al. 2004. Heptad repeat 2-based peptides inhibit avian sarcoma and leukosis virus subgroup a infection and identify a fusion intermediate. J. Virol. 78:13430-13439.
    • (2004) J. Virol. , vol.78 , pp. 13430-13439
    • Netter, R.C.1
  • 47
    • 0015216932 scopus 로고
    • The mechanism by which cycloheximide and related glutarimide antibiotics in-hibit peptide synthesis on reticulocyte ribosomes
    • Obrig, T. G., W. J. Culp, W. L. McKeehan, and B. Hardesty. 1971. The mechanism by which cycloheximide and related glutarimide antibiotics in-hibit peptide synthesis on reticulocyte ribosomes. J. Biol. Chem. 246:174-181.
    • (1971) J. Biol. Chem. , vol.246 , pp. 174-181
    • Obrig, T.G.1    Culp, W.J.2    McKeehan, W.L.3    Hardesty, B.4
  • 48
    • 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
  • 49
    • 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, L. M., M. Porotto, O. Greengard, and A. Moscona. 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
  • 50
    • 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
  • 51
    • 34648830863 scopus 로고    scopus 로고
    • Molecular determinants of antiviral potency of paramyxovirus entry inhibitors
    • Porotto, M., et al. 2007. Molecular determinants of antiviral potency of paramyxovirus entry inhibitors. J. Virol. 81:10567-10574.
    • (2007) J. Virol. , vol.81 , pp. 10567-10574
    • Porotto, M.1
  • 52
    • 33748948794 scopus 로고    scopus 로고
    • Inhibition of Hendra virus membrane fusion
    • Porotto, M., et al. 2006. Inhibition of Hendra virus membrane fusion. J. Virol. 80:9837-9849.
    • (2006) J. Virol. , vol.80 , pp. 9837-9849
    • Porotto, M.1
  • 53
    • 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
  • 54
    • 33947363286 scopus 로고    scopus 로고
    • A second receptor binding site on the human parainfluenza 3 hemagglutinin-neuraminidase contributes to activation of the fusion mechanism
    • Porotto, M., M. Fornabaio, G. Kellogg, and A. Moscona. 2007. A second receptor binding site on the human parainfluenza 3 hemagglutinin-neuraminidase 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
  • 55
    • 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., O. Greengard, N. Poltoratskaia, M.-A. Horga, and A. Moscona. 2001. Human parainfluenza virus type 3 HN-receptor interaction: the effect of 4-GU-DANA on a neuraminidase-deficient variant. J. Virol. 76:7481-7488.
    • (2001) J. Virol. , vol.76 , pp. 7481-7488
    • Porotto, M.1    Greengard, O.2    Poltoratskaia, N.3    Horga, M.-A.4    Moscona, A.5
  • 56
    • 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., M. Murrell, O. Greengard, L. Doctor, and A. Moscona. 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
  • 57
    • 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
  • 58
    • 0037333844 scopus 로고    scopus 로고
    • Triggering of human parainfluenza virus 3 fusion protein (F) by the hemagglutinin-neuraminidase (HN): an HN mutation diminishing the rate of F activation and fusion
    • Porotto, M., M. Murrell, O. Greengard, and A. Moscona. 2003. Triggering of human parainfluenza virus 3 fusion protein (F) by the hemagglutinin-neuraminidase (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
  • 59
    • 78449243403 scopus 로고    scopus 로고
    • Inhibition of Nipah virus infection in vivo: targeting an early stage of paramyxovirus fusion activation during viral entry
    • Porotto, M., et al. 2010. Inhibition of Nipah virus infection in vivo: targeting an early stage of paramyxovirus fusion activation during viral entry. PLoS Pathog. 6:e1001168.
    • (2010) PLoS Pathog. , vol.6
    • Porotto, M.1
  • 60
    • 67449092278 scopus 로고    scopus 로고
    • Kinetic dependence of paramyxovirus entry inhibition
    • Porotto, M., et al. 2009. Kinetic dependence of paramyxovirus entry inhibition. J. Virol. 83:6947-6951.
    • (2009) J. Virol. , vol.83 , pp. 6947-6951
    • Porotto, M.1
  • 61
    • 77953313232 scopus 로고    scopus 로고
    • Viral entry inhibitors targeted to the membrane site of action
    • Porotto, M., et al. 2010. Viral entry inhibitors targeted to the membrane site of action. J. Virol. 84:6760-6768.
    • (2010) J. Virol. , vol.84 , pp. 6760-6768
    • Porotto, M.1
  • 62
    • 0028864218 scopus 로고
    • A synthetic peptide corresponding to a conserved heptad repeat domain is a potent inhibitor of Sendai virus-cell fusion: an emerging similarity with functional domains of other viruses
    • Rapaport, D., M. Ovadia, and Y. Shai. 1995. A synthetic peptide corresponding to a conserved heptad repeat domain is a potent inhibitor of Sendai virus-cell fusion: an emerging similarity with functional domains of other viruses. EMBO J. 14:5524-5531.
    • (1995) EMBO J. , vol.14 , pp. 5524-5531
    • Rapaport, D.1    Ovadia, M.2    Shai, Y.3
  • 63
    • 0035421959 scopus 로고    scopus 로고
    • Membrane fusion machines of paramyxoviruses: capture of intermediates of fusion
    • Russell, C. J., T. S. Jardetzky, and R. A. Lamb. 2001. Membrane fusion machines of paramyxoviruses: capture of intermediates of fusion. EMBO J. 20:4024-4034.
    • (2001) EMBO J. , vol.20 , pp. 4024-4034
    • Russell, C.J.1    Jardetzky, T.S.2    Lamb, R.A.3
  • 64
    • 0242298583 scopus 로고    scopus 로고
    • A dual-functional paramyxovirus F protein regulatory switch segment: activation and membrane fusion
    • Russell, C. J., K. L. Kantor, T. S. Jardetzky, and R. A. Lamb. 2003. A dual-functional paramyxovirus F protein regulatory switch segment: activation and membrane fusion. J. Cell Biol. 163:363-374.
    • (2003) J. Cell Biol. , vol.163 , pp. 363-374
    • Russell, C.J.1    Kantor, K.L.2    Jardetzky, T.S.3    Lamb, R.A.4
  • 66
    • 37749019200 scopus 로고    scopus 로고
    • Viral and developmental cell fusion mechanisms: conservation and divergence
    • Sapir, A., O. Avinoam, B. Podbilewicz, and L. V. Chernomordik. 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
  • 67
    • 0025866185 scopus 로고
    • Conformational changes induced in the human immunodeficiency virus envelope glycoprotein by soluble CD4 binding
    • Sattentau, Q. J., and J. P. Moore. 1991. Conformational changes induced in the human immunodeficiency virus envelope glycoprotein by soluble CD4 binding. J. Exp. Med. 174:407-415.
    • (1991) J. Exp. Med. , vol.174 , pp. 407-415
    • Sattentau, Q.J.1    Moore, J.P.2
  • 68
    • 33644861986 scopus 로고    scopus 로고
    • Identification of new fluorescent protein fragments for bimolecular fluorescence complementation analysis under physiological conditions
    • Shyu, Y. J., H. Liu, X. Deng, and C. D. Hu. 2006. Identification of new fluorescent protein fragments for bimolecular fluorescence complementation analysis under physiological conditions. Biotechniques 40:61-66.
    • (2006) Biotechniques , vol.40 , pp. 61-66
    • Shyu, Y.J.1    Liu, H.2    Deng, X.3    Hu, C.D.4
  • 69
    • 0020035202 scopus 로고
    • Changes in the conformation of influenza virus hemagglutinin at the pH optimum of virus-mediated membrane fusion
    • Skehel, J. J., et al. 1982. Changes in the conformation of influenza virus hemagglutinin at the pH optimum of virus-mediated membrane fusion. Proc. Natl. Acad. Sci. U. S. A. 79:968-972.
    • (1982) Proc. Natl. Acad. Sci. U. S. A. , vol.79 , pp. 968-972
    • Skehel, J.J.1
  • 70
    • 71949123985 scopus 로고    scopus 로고
    • Viral entry mechanisms: the increasing diversity of paramyxovirus entry
    • Smith, E. C., A. Popa, A. Chang, C. Masante, and R. E. Dutch. 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
  • 71
    • 62049083943 scopus 로고    scopus 로고
    • Structural and functional bases for broad-spectrum neutralization of avian and human influenza A viruses
    • Sui, J., et al. 2009. Structural and functional bases for broad-spectrum neutralization of avian and human influenza A viruses. Nat. Struct. Mol. Biol. 16:265-273.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 265-273
    • Sui, J.1
  • 72
    • 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
  • 74
    • 0034713246 scopus 로고    scopus 로고
    • Temperature dependence of fusion by Sendai virus
    • Wharton, S. A., J. J. Skehel, and D. C. Wiley. 2000. Temperature dependence of fusion by Sendai virus. Virology 271:71-78.
    • (2000) Virology , vol.271 , pp. 71-78
    • Wharton, S.A.1    Skehel, J.J.2    Wiley, D.C.3
  • 75
    • 45849108331 scopus 로고    scopus 로고
    • Structures and mechanisms of viral membrane fusion proteins: multiple variations on a common theme
    • White, J. M., S. E. Delos, M. Brecher, and K. Schornberg. 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
  • 76
    • 0023574003 scopus 로고
    • Anti-peptide antibodies detect steps in a protein conformational change: low-pH activation of the influenza virus hemagglutinin
    • White, J. M., and I. A. Wilson. 1987. Anti-peptide antibodies detect steps in a protein conformational change: low-pH activation of the influenza virus hemagglutinin. J. Cell Biol. 105:2887-2896.
    • (1987) J. Cell Biol. , vol.105 , pp. 2887-2896
    • White, J.M.1    Wilson, I.A.2
  • 77
    • 0027959493 scopus 로고
    • Peptides corresponding to a predictive alpha-helical domain of human immunodeficiency virus type 1 gp41 are potent inhibitors of virus infection
    • Wild, C. T., D. C. Shugars, T. K. Greenwell, C. B. McDanal, and T. J. Matthews. 1994. Peptides corresponding to a predictive alpha-helical domain of human immunodeficiency virus type 1 gp41 are potent inhibitors of virus infection. Proc. Natl. Acad. Sci. U. S. A. 91:9770-9774.
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 9770-9774
    • Wild, C.T.1    Shugars, D.C.2    Greenwell, T.K.3    McDanal, C.B.4    Matthews, T.J.5
  • 78
    • 79955373167 scopus 로고    scopus 로고
    • Structural characterization of an early fusion intermediate of influenza virus hemagglutinin
    • Xu, R., and I. A. Wilson. 2011. Structural characterization of an early fusion intermediate of influenza virus hemagglutinin. J. Virol. 85:5172-5182.
    • (2011) J. Virol. , vol.85 , pp. 5172-5182
    • Xu, R.1    Wilson, I.A.2
  • 79
    • 0030245704 scopus 로고    scopus 로고
    • Peptides corresponding to the heptad repeat sequence of human parainfluenza virus fusion protein are potent inhibitors of virus infection
    • Yao, Q., and R. W. Compans. 1996. Peptides corresponding to the heptad repeat sequence of human parainfluenza virus fusion protein are potent inhibitors of virus infection. Virology 223:103-112.
    • (1996) Virology , vol.223 , pp. 103-112
    • Yao, Q.1    Compans, R.W.2
  • 81
    • 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
  • 82
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.