메뉴 건너뛰기




Volumn 78, Issue 24, 2004, Pages 13911-13919

Inhibition of parainfluenza virus type 3 and newcastle disease virus hemagglutinin-neuraminidase receptor binding: Effect of receptor avidity and steric hindrance at the inhibitor binding sites

Author keywords

[No Author keywords available]

Indexed keywords

HN PROTEIN; SIALIDASE INHIBITOR; ZANAMIVIR;

EID: 10044296412     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.78.24.13911-13919.2004     Document Type: Article
Times cited : (56)

References (25)
  • 2
    • 0029585928 scopus 로고
    • Generation and characterization of an influenza virus neuraminidase variant with decreased sensitivity to the neuraminidase-specific inhibitor 4-guanidino-Neu5Ac2en
    • Blick, T., T. Tiong, A. Sahasrabudhe, J. Varghese, P. Colman, G. Hart, R. Bethell, and J. McKimm-Breschkin. 1995. Generation and characterization of an influenza virus neuraminidase variant with decreased sensitivity to the neuraminidase-specific inhibitor 4-guanidino-Neu5Ac2en. Virology 214:475-484.
    • (1995) Virology , vol.214 , pp. 475-484
    • Blick, T.1    Tiong, T.2    Sahasrabudhe, A.3    Varghese, J.4    Colman, P.5    Hart, G.6    Bethell, R.7    McKimm-Breschkin, J.8
  • 3
    • 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., T. Takimoto, R. Russell, S. Crennell, I. Moustafa, A. Portner, and G. Taylor. 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    Takimoto, T.2    Russell, R.3    Crennell, S.4    Moustafa, I.5    Portner, A.6    Taylor, G.7
  • 4
    • 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
  • 5
    • 0036667731 scopus 로고    scopus 로고
    • Rotamer libraries in the 21st century
    • Dunbrack, R. 2002. Rotamer libraries in the 21st century. Curr. Opin. Struct. Biol. 12:431-440.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 431-440
    • Dunbrack, R.1
  • 6
    • 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
  • 7
    • 0003074858 scopus 로고
    • A super position. CCP4/ESF-EACBM News
    • Kleywegt, G., and T. Jones. 1994. A super position. CCP4/ESF-EACBM News. Protein Crystallogr. 31:9-14.
    • (1994) Protein Crystallogr. , vol.31 , pp. 9-14
    • Kleywegt, G.1    Jones, T.2
  • 8
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. 1991. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24:946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 9
    • 0001178028 scopus 로고    scopus 로고
    • Paramyxoviridae: The viruses and their replication
    • B. Fields, D. Knipe, and P. Howley (ed.). Lippincott-Raven, Philadelphia, Pa.
    • Lamb, R., and D. Kolakofsky. 1996. Paramyxoviridae: the viruses and their replication, p. 577-604. In B. Fields, D. Knipe, and P. Howley (ed.), Fields virology. Lippincott-Raven, Philadelphia, Pa.
    • (1996) Fields Virology , pp. 577-604
    • Lamb, R.1    Kolakofsky, D.2
  • 11
    • 0343851577 scopus 로고    scopus 로고
    • The use of a quantitative fusion assay to evaluate HN-receptor interaction for human parainfluenza virus type 3
    • Levin Perlman, S., M. Jordan, R. Brossmer, O. Greengard, and A. Moscona. 1999. The use of a quantitative fusion assay to evaluate HN-receptor interaction for human parainfluenza virus type 3. Virology 265:57-65.
    • (1999) Virology , vol.265 , pp. 57-65
    • Levin Perlman, S.1    Jordan, M.2    Brossmer, R.3    Greengard, O.4    Moscona, A.5
  • 12
    • 0033897803 scopus 로고    scopus 로고
    • Resistance of influenza viruses to neuraminidase inhibitors - A review
    • McKimm-Breschkin. 2000. Resistance of influenza viruses to neuraminidase inhibitors-a review. Antiviral Res. 47:1-17.
    • (2000) Antiviral Res. , vol.47 , pp. 1-17
    • McKimm-Breschkin1
  • 13
    • 0015959249 scopus 로고
    • Inhibition of neuraminidase activity by derivatives of 2-deoxy-2,3-dehydro-AT-acetyl-neuraminic acid
    • Meindl, P., G. Bodo, P. Palese, J. Schulman, and H. Tuppy. 1974. Inhibition of neuraminidase activity by derivatives of 2-deoxy-2,3-dehydro-AT- acetyl-neuraminic acid. Virology 58:457-463.
    • (1974) Virology , vol.58 , pp. 457-463
    • Meindl, P.1    Bodo, G.2    Palese, P.3    Schulman, J.4    Tuppy, H.5
  • 14
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merritt, E., and D. Bacon. 1997. Raster3D: photorealistic molecular graphics. Methods Enzymol. 277:505-524.
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.1    Bacon, D.2
  • 15
    • 0027381637 scopus 로고
    • Relative affinity of the human parainfluenza virus 3 hemagglutinin- neuraminidase for sialic acid correlates with virus-induced fusion activity
    • Moscona, A., and R. W. Peluso. 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
  • 16
    • 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
  • 17
    • 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., M. Porotto, T. Weber, O. Greengard, and A. Moscona. 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
  • 18
    • 0017151109 scopus 로고
    • Inhibition of influenza virus replication in tissue culture by 2-deoxy-2,3-dehydro-N-trifluoroacetylneuraminic acid (FANA): Mechanism of action
    • Palese, P., and R. W. Compans. 1976. Inhibition of influenza virus replication in tissue culture by 2-deoxy-2,3-dehydro-N-trifluoroacetylneuraminic acid (FANA): mechanism of action. J. Gen. Virol. 33:159-163.
    • (1976) J. Gen. Virol. , vol.33 , pp. 159-163
    • Palese, P.1    Compans, R.W.2
  • 19
    • 0016244226 scopus 로고
    • Inhibition of influenza and parainfluenza virus replication in tissue culture by 2-deoxy-2,3-dehydro-N-trifluoroacelylneuraminic cid (FANA)
    • Palese, P., J. L. Schulman, G. Bodo, and P. Meindl. 1974. Inhibition of influenza and parainfluenza virus replication in tissue culture by 2-deoxy-2,3-dehydro-N-trifluoroacelylneuraminic cid (FANA). Virology 59:490-498.
    • (1974) Virology , vol.59 , pp. 490-498
    • Palese, P.1    Schulman, J.L.2    Bodo, G.3    Meindl, P.4
  • 20
    • 0037223757 scopus 로고    scopus 로고
    • Newcastle disease virus (NDV)-based assay demonstrates interferon-antagonist activity for the NDV V protein and the Nipah virus V, W, and C proteins
    • Park, M. S., M. L. Shaw, J. Munoz-Jordan, J. F. Cros, T. Nakaya, N. Bouvier, P. Palese, A. Garcia-Sastre, and C. F. Basler. 2003. Newcastle disease virus (NDV)-based assay demonstrates interferon-antagonist activity for the NDV V protein and the Nipah virus V, W, and C proteins. J. Virol. 77:1501-1511.
    • (2003) J. Virol. , vol.77 , pp. 1501-1511
    • Park, M.S.1    Shaw, M.L.2    Munoz-Jordan, J.3    Cros, J.F.4    Nakaya, T.5    Bouvier, N.6    Palese, P.7    Garcia-Sastre, A.8    Basler, C.F.9
  • 21
    • 0038661342 scopus 로고    scopus 로고
    • Structural features of paramyxovirus F protein required for fusion initiation
    • Plemper, R. K., A. S. Lakdawala, K. M. Gernert, J. P. Snyder, and R. W. Compans. 2003. Structural features of paramyxovirus F protein required for fusion initiation. Biochemistry 42:6645-6655.
    • (2003) Biochemistry , vol.42 , pp. 6645-6655
    • Plemper, R.K.1    Lakdawala, A.S.2    Gernert, K.M.3    Snyder, J.P.4    Compans, R.W.5
  • 22
    • 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
  • 23
    • 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
  • 25
    • 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.