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Volumn 345, Issue 3, 2006, Pages 1108-1115

Characterization of HCoV-229E fusion core: Implications for structure basis of coronavirus membrane fusion

Author keywords

Fusion core; Heptad repeat regions; Human coronavirus 229E; Type I membrane fusion; Virus fusion

Indexed keywords

CORE PROTEIN; HETERODIMER; HYBRID PROTEIN; MEMBRANE PROTEIN; POLYPEPTIDE; PROTEIN SPIKE; UNCLASSIFIED DRUG; VIRUS FUSION PROTEIN;

EID: 33646827147     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.04.141     Document Type: Article
Times cited : (11)

References (39)
  • 1
    • 20444365774 scopus 로고    scopus 로고
    • Human coronavirus NL63 infection and other coronavirus infections in children hospitalized with acute respiratory disease in Hong Kong, China
    • Chiu S.S., Chan K.H., Chu K.W., Kwan S.W., Guan Y., Poon L.L., and Peiris J.S. Human coronavirus NL63 infection and other coronavirus infections in children hospitalized with acute respiratory disease in Hong Kong, China. Clin. Infect. Dis. 40 (2005) 1721-1729
    • (2005) Clin. Infect. Dis. , vol.40 , pp. 1721-1729
    • Chiu, S.S.1    Chan, K.H.2    Chu, K.W.3    Kwan, S.W.4    Guan, Y.5    Poon, L.L.6    Peiris, J.S.7
  • 2
    • 0034086980 scopus 로고    scopus 로고
    • The core of the respiratory syncytial virus fusion protein is a trimeric coiled coil
    • Matthews J.M., Young T.F., Tucker S.P., and Mackay J.P. The core of the respiratory syncytial virus fusion protein is a trimeric coiled coil. J. Virol. 74 (2000) 5911-5920
    • (2000) J. Virol. , vol.74 , pp. 5911-5920
    • Matthews, J.M.1    Young, T.F.2    Tucker, S.P.3    Mackay, J.P.4
  • 4
    • 27744531541 scopus 로고    scopus 로고
    • Development of one-step, real-time, quantitative reverse transcriptase PCR assays for absolute quantitation of human coronaviruses OC43 and 229E
    • Vijgen L., Keyaerts E., Moes E., Maes P., Duson G., and Van Ranst M. Development of one-step, real-time, quantitative reverse transcriptase PCR assays for absolute quantitation of human coronaviruses OC43 and 229E. J. Clin. Microbiol. 43 (2005) 5452-5456
    • (2005) J. Clin. Microbiol. , vol.43 , pp. 5452-5456
    • Vijgen, L.1    Keyaerts, E.2    Moes, E.3    Maes, P.4    Duson, G.5    Van Ranst, M.6
  • 8
    • 12144287276 scopus 로고    scopus 로고
    • Interaction between heptad repeat 1 and 2 regions in spike protein of SARS-associated coronavirus: implications for virus fusogenic mechanism and identification of fusion inhibitors
    • Liu S., Xiao G., Chen Y., He Y., Niu J., Escalante C.R., Xiong H., Farmar J., Debnath A.K., Tien P., and Jiang S. Interaction between heptad repeat 1 and 2 regions in spike protein of SARS-associated coronavirus: implications for virus fusogenic mechanism and identification of fusion inhibitors. Lancet 363 (2004) 938-947
    • (2004) Lancet , vol.363 , pp. 938-947
    • Liu, S.1    Xiao, G.2    Chen, Y.3    He, Y.4    Niu, J.5    Escalante, C.R.6    Xiong, H.7    Farmar, J.8    Debnath, A.K.9    Tien, P.10    Jiang, S.11
  • 9
    • 27844511949 scopus 로고    scopus 로고
    • Design and characterization of human respiratory syncytial virus entry inhibitors
    • Ni L., Zhao L., Qian Y., Zhu J., Jin Z., Chen Y.W., Tien P., and Gao G.F. Design and characterization of human respiratory syncytial virus entry inhibitors. Antivir. Ther. 10 (2005) 833-840
    • (2005) Antivir. Ther. , vol.10 , pp. 833-840
    • Ni, L.1    Zhao, L.2    Qian, Y.3    Zhu, J.4    Jin, Z.5    Chen, Y.W.6    Tien, P.7    Gao, G.F.8
  • 10
    • 0345701489 scopus 로고    scopus 로고
    • Both heptad repeats of human respiratory syncytial virus fusion protein are potent inhibitors of viral fusion
    • Wang E., Sun X., Qian Y., Zhao L., Tien P., and Gao G.F. Both heptad repeats of human respiratory syncytial virus fusion protein are potent inhibitors of viral fusion. Biochem. Biophys. Res. Commun. 302 (2003) 469-475
    • (2003) Biochem. Biophys. Res. Commun. , vol.302 , pp. 469-475
    • Wang, E.1    Sun, X.2    Qian, Y.3    Zhao, L.4    Tien, P.5    Gao, G.F.6
  • 11
    • 8344260757 scopus 로고    scopus 로고
    • Characterization of the heptad repeat regions, HR1 and HR2, and design of a fusion core structure model of the spike protein from severe acute respiratory syndrome (SARS) coronavirus
    • Xu Y., Zhu J., Liu Y., Lou Z., Yuan F., Liu Y., Cole D.K., Ni L., Su N., Qin L., Li X., Bai Z., Bell J.I., Pang H., Tien P., Gao G.F., and Rao Z. Characterization of the heptad repeat regions, HR1 and HR2, and design of a fusion core structure model of the spike protein from severe acute respiratory syndrome (SARS) coronavirus. Biochemistry 43 (2004) 14064-14071
    • (2004) Biochemistry , vol.43 , pp. 14064-14071
    • Xu, Y.1    Zhu, J.2    Liu, Y.3    Lou, Z.4    Yuan, F.5    Liu, Y.6    Cole, D.K.7    Ni, L.8    Su, N.9    Qin, L.10    Li, X.11    Bai, Z.12    Bell, J.I.13    Pang, H.14    Tien, P.15    Gao, G.F.16    Rao, Z.17
  • 12
    • 27144551308 scopus 로고    scopus 로고
    • Biochemical and biophysical characterization of the transmissible gastroenteritis coronavirus fusion core
    • Ma G., Feng Y., Gao F., Wang J., Liu C., and Li Y. Biochemical and biophysical characterization of the transmissible gastroenteritis coronavirus fusion core. Biochem. Biophys. Res. Commun. 337 (2005) 1301-1307
    • (2005) Biochem. Biophys. Res. Commun. , vol.337 , pp. 1301-1307
    • Ma, G.1    Feng, Y.2    Gao, F.3    Wang, J.4    Liu, C.5    Li, Y.6
  • 13
    • 0032214714 scopus 로고    scopus 로고
    • Crystal structure of the Ebola virus membrane fusion subunit, GP2, from the envelope glycoprotein ectodomain
    • Weissenhorn W., Carfi A., Lee K.H., Skehel J.J., and Wiley D.C. Crystal structure of the Ebola virus membrane fusion subunit, GP2, from the envelope glycoprotein ectodomain. Mol. Cell. 2 (1998) 605-616
    • (1998) Mol. Cell. , vol.2 , pp. 605-616
    • Weissenhorn, W.1    Carfi, A.2    Lee, K.H.3    Skehel, J.J.4    Wiley, D.C.5
  • 14
    • 0027253445 scopus 로고
    • A spring-loaded mechanism for the conformational change of influenza hemagglutinin
    • Carr C.M., and Kim P.S. A spring-loaded mechanism for the conformational change of influenza hemagglutinin. Cell 73 (1993) 823-832
    • (1993) Cell , vol.73 , pp. 823-832
    • Carr, C.M.1    Kim, P.S.2
  • 15
    • 0032577550 scopus 로고    scopus 로고
    • HIV entry and its inhibition
    • Chan D.C., and Kim P.S. HIV entry and its inhibition. Cell 93 (1998) 681-684
    • (1998) Cell , vol.93 , pp. 681-684
    • Chan, D.C.1    Kim, P.S.2
  • 16
    • 0036500549 scopus 로고    scopus 로고
    • H5 avian and H9 swine influenza virus haemagglutinin structures: possible origin of influenza subtypes
    • Ha Y., Stevens D.J., Skehel J.J., and Wiley D.C. H5 avian and H9 swine influenza virus haemagglutinin structures: possible origin of influenza subtypes. EMBO J. 21 (2002) 865-875
    • (2002) EMBO J. , vol.21 , pp. 865-875
    • Ha, Y.1    Stevens, D.J.2    Skehel, J.J.3    Wiley, D.C.4
  • 17
    • 0034708369 scopus 로고    scopus 로고
    • Development of HIV entry inhibitors targeted to the coiled-coil regions of gp41
    • Jiang S., and Debnath A.K. Development of HIV entry inhibitors targeted to the coiled-coil regions of gp41. Biochem. Biophys. Res. Commun. 269 (2000) 641-646
    • (2000) Biochem. Biophys. Res. Commun. , vol.269 , pp. 641-646
    • Jiang, S.1    Debnath, A.K.2
  • 18
    • 0035793406 scopus 로고    scopus 로고
    • Protein design of an HIV-1 entry inhibitor
    • Root M.J., Kay M.S., and Kim P.S. Protein design of an HIV-1 entry inhibitor. Science 291 (2001) 884-888
    • (2001) Science , vol.291 , pp. 884-888
    • Root, M.J.1    Kay, M.S.2    Kim, P.S.3
  • 19
    • 0036715404 scopus 로고    scopus 로고
    • HIV-1 entry and entry inhibitors as therapeutic agents
    • Starr-Spires L.D., and Collman R.G. HIV-1 entry and entry inhibitors as therapeutic agents. Clin. Lab. Med. 22 (2002) 681-701
    • (2002) Clin. Lab. Med. , vol.22 , pp. 681-701
    • Starr-Spires, L.D.1    Collman, R.G.2
  • 20
    • 1342265790 scopus 로고    scopus 로고
    • HIV-1 gp41: mediator of fusion and target for inhibition
    • Weiss C.D. HIV-1 gp41: mediator of fusion and target for inhibition. AIDS Rev. 5 (2003) 214-221
    • (2003) AIDS Rev. , vol.5 , pp. 214-221
    • Weiss, C.D.1
  • 21
    • 0033214895 scopus 로고    scopus 로고
    • Inhibiting HIV-1 entry: discovery of D-peptide inhibitors that target the gp41 coiled-coil pocket
    • Eckert D.M., Malashkevich V.N., Hong L.H., Carr P.A., and Kim P.S. Inhibiting HIV-1 entry: discovery of D-peptide inhibitors that target the gp41 coiled-coil pocket. Cell 99 (1999) 103-115
    • (1999) Cell , vol.99 , pp. 103-115
    • Eckert, D.M.1    Malashkevich, V.N.2    Hong, L.H.3    Carr, P.A.4    Kim, P.S.5
  • 22
    • 5344258285 scopus 로고    scopus 로고
    • Construct design, biophysical, and biochemical characterization of the fusion core from mouse hepatitis virus (a coronavirus) spike protein
    • Xu Y., Cole D.K., Lou Z., Liu Y., Qin L., Li X., Bai Z., Yuan F., Rao Z., and Gao G.F. Construct design, biophysical, and biochemical characterization of the fusion core from mouse hepatitis virus (a coronavirus) spike protein. Protein Expr. Purif. 38 (2004) 116-122
    • (2004) Protein Expr. Purif. , vol.38 , pp. 116-122
    • Xu, Y.1    Cole, D.K.2    Lou, Z.3    Liu, Y.4    Qin, L.5    Li, X.6    Bai, Z.7    Yuan, F.8    Rao, Z.9    Gao, G.F.10
  • 23
    • 0036190641 scopus 로고    scopus 로고
    • Six-helix bundle assembly and characterization of heptad repeat regions from the F protein of Newcastle disease virus
    • Yu M., Wang E., Liu Y., Cao D., Jin N., Zhang C.W., Bartlam M., Rao Z., Tien P., and Gao G.F. Six-helix bundle assembly and characterization of heptad repeat regions from the F protein of Newcastle disease virus. J. Gen. Virol. 83 (2002) 623-629
    • (2002) J. Gen. Virol. , vol.83 , pp. 623-629
    • Yu, M.1    Wang, E.2    Liu, Y.3    Cao, D.4    Jin, N.5    Zhang, C.W.6    Bartlam, M.7    Rao, Z.8    Tien, P.9    Gao, G.F.10
  • 25
    • 4544381403 scopus 로고    scopus 로고
    • HIV fusion and its inhibition in antiretroviral therapy
    • Greenberg M., Cammack N., Salgo M., and Smiley L. HIV fusion and its inhibition in antiretroviral therapy. Rev. Med. Virol. 14 (2004) 321-337
    • (2004) Rev. Med. Virol. , vol.14 , pp. 321-337
    • Greenberg, M.1    Cammack, N.2    Salgo, M.3    Smiley, L.4
  • 26
    • 2342466810 scopus 로고    scopus 로고
    • CD4-induced T-20 binding to human immunodeficiency virus type 1 gp120 blocks interaction with the CXCR4 coreceptor
    • Yuan W., Craig S., Si Z., Farzan M., and Sodroski J. CD4-induced T-20 binding to human immunodeficiency virus type 1 gp120 blocks interaction with the CXCR4 coreceptor. J. Virol. 78 (2004) 5448-5457
    • (2004) J. Virol. , vol.78 , pp. 5448-5457
    • Yuan, W.1    Craig, S.2    Si, Z.3    Farzan, M.4    Sodroski, J.5
  • 27
    • 0025117784 scopus 로고
    • The structure of a membrane fusion mutant of the influenza virus haemagglutinin
    • Weis W.I., Cusack S.C., Brown J.H., Daniels R.S., Skehel J.J., and Wiley D.C. The structure of a membrane fusion mutant of the influenza virus haemagglutinin. EMBO J. 9 (1990) 17-24
    • (1990) EMBO J. , vol.9 , pp. 17-24
    • Weis, W.I.1    Cusack, S.C.2    Brown, J.H.3    Daniels, R.S.4    Skehel, J.J.5    Wiley, D.C.6
  • 28
    • 0034687711 scopus 로고    scopus 로고
    • Structural characterization of the human respiratory syncytial virus fusion protein core
    • Zhao X., Singh M., Malashkevich V.N., and Kim P.S. Structural characterization of the human respiratory syncytial virus fusion protein core. Proc. Natl. Acad. Sci. USA 97 (2000) 14172-14177
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 14172-14177
    • Zhao, X.1    Singh, M.2    Malashkevich, V.N.3    Kim, P.S.4
  • 29
    • 3142663245 scopus 로고    scopus 로고
    • Structural basis for coronavirus-mediated membrane fusion. Crystal structure of mouse hepatitis virus spike protein fusion core
    • Xu Y., Liu Y., Lou Z., Qin L., Li X., Bai Z., Pang H., Tien P., Gao G.F., and Rao Z. Structural basis for coronavirus-mediated membrane fusion. Crystal structure of mouse hepatitis virus spike protein fusion core. J. Biol. Chem. 279 (2004) 30514-30522
    • (2004) J. Biol. Chem. , vol.279 , pp. 30514-30522
    • Xu, Y.1    Liu, Y.2    Lou, Z.3    Qin, L.4    Li, X.5    Bai, Z.6    Pang, H.7    Tien, P.8    Gao, G.F.9    Rao, Z.10
  • 31
    • 0038116337 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray diffraction analysis of post-fusion six-helix bundle core structure from Newcastle disease virus F protein
    • Li P.Y., Zhu J.Q., Wu B.L., Gao F., Tien P., Rao Z., and Gao G.F. Crystallization and preliminary X-ray diffraction analysis of post-fusion six-helix bundle core structure from Newcastle disease virus F protein. Acta Crystallogr. D. Biol. Crystallogr. 59 (2003) 1296-1298
    • (2003) Acta Crystallogr. D. Biol. Crystallogr. , vol.59 , pp. 1296-1298
    • Li, P.Y.1    Zhu, J.Q.2    Wu, B.L.3    Gao, F.4    Tien, P.5    Rao, Z.6    Gao, G.F.7
  • 32
    • 27744533984 scopus 로고    scopus 로고
    • Design and characterization of viral polypeptide inhibitors targeting Newcastle disease virus fusion
    • Zhu J., Jiang X., Liu Y., Tien P., and Gao G.F. Design and characterization of viral polypeptide inhibitors targeting Newcastle disease virus fusion. J. Mol. Biol. 354 (2005) 601-613
    • (2005) J. Mol. Biol. , vol.354 , pp. 601-613
    • Zhu, J.1    Jiang, X.2    Liu, Y.3    Tien, P.4    Gao, G.F.5
  • 33
    • 15544386225 scopus 로고    scopus 로고
    • Filling the hole: evidence of a small molecule binding to the fusion core pocket in human respiratory syncytial virus
    • Gao G.F. Filling the hole: evidence of a small molecule binding to the fusion core pocket in human respiratory syncytial virus. Expert Opin. Investig. Drugs 14 (2005) 195-197
    • (2005) Expert Opin. Investig. Drugs , vol.14 , pp. 195-197
    • Gao, G.F.1
  • 34
    • 1642540249 scopus 로고    scopus 로고
    • Conformational change and protein-protein interactions of the fusion protein of Semliki Forest virus
    • Gibbons D.L., Vaney M.C., Roussel A., Vigouroux A., Reilly B., Lepault J., Kielian M., and Rey F.A. Conformational change and protein-protein interactions of the fusion protein of Semliki Forest virus. Nature 427 (2004) 320-325
    • (2004) Nature , vol.427 , pp. 320-325
    • Gibbons, D.L.1    Vaney, M.C.2    Roussel, A.3    Vigouroux, A.4    Reilly, B.5    Lepault, J.6    Kielian, M.7    Rey, F.A.8
  • 35
    • 1642499388 scopus 로고    scopus 로고
    • Structure of the dengue virus envelope protein after membrane fusion
    • Modis Y., Ogata S., Clements D., and Harrison S.C. Structure of the dengue virus envelope protein after membrane fusion. Nature 427 (2004) 313-319
    • (2004) Nature , vol.427 , pp. 313-319
    • Modis, Y.1    Ogata, S.2    Clements, D.3    Harrison, S.C.4
  • 36
    • 10344234242 scopus 로고    scopus 로고
    • Crystal structure of severe acute respiratory syndrome coronavirus spike protein fusion core
    • Xu Y., Lou Z., Liu Y., Pang H., Tien P., Gao G.F., and Rao Z. Crystal structure of severe acute respiratory syndrome coronavirus spike protein fusion core. J. Biol. Chem. 279 (2004) 49414-49419
    • (2004) J. Biol. Chem. , vol.279 , pp. 49414-49419
    • Xu, Y.1    Lou, Z.2    Liu, Y.3    Pang, H.4    Tien, P.5    Gao, G.F.6    Rao, Z.7
  • 37
    • 0032483021 scopus 로고    scopus 로고
    • Crystal structure of the simian immunodeficiency virus (SIV) gp41 core: conserved helical interactions underlie the broad inhibitory activity of gp41 peptides
    • Malashkevich V.N., Chan D.C., Chutkowski C.T., and Kim P.S. Crystal structure of the simian immunodeficiency virus (SIV) gp41 core: conserved helical interactions underlie the broad inhibitory activity of gp41 peptides. Proc. Natl. Acad. Sci. USA 95 (1998) 9134-9139
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 9134-9139
    • Malashkevich, V.N.1    Chan, D.C.2    Chutkowski, C.T.3    Kim, P.S.4
  • 38
    • 21644470919 scopus 로고    scopus 로고
    • Crystallization and preliminary crystallographic analysis of the heptad-repeat complex of SARS coronavirus spike protein
    • Xu Y., Su N., Qin L., Bai Z., Gao G.F., and Rao Z. Crystallization and preliminary crystallographic analysis of the heptad-repeat complex of SARS coronavirus spike protein. Acta Crystallogr. D. Biol. Crystallogr. 60 (2004) 2377-2379
    • (2004) Acta Crystallogr. D. Biol. Crystallogr. , vol.60 , pp. 2377-2379
    • Xu, Y.1    Su, N.2    Qin, L.3    Bai, Z.4    Gao, G.F.5    Rao, Z.6
  • 39
    • 0033618320 scopus 로고    scopus 로고
    • LearnCoil-VMF: computational evidence for coiled-coil-like motifs in many viral membrane-fusion proteins
    • Singh M., Berger B., and Kim P.S. LearnCoil-VMF: computational evidence for coiled-coil-like motifs in many viral membrane-fusion proteins. J. Mol. Biol. 290 (1999) 1031-1041
    • (1999) J. Mol. Biol. , vol.290 , pp. 1031-1041
    • Singh, M.1    Berger, B.2    Kim, P.S.3


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