메뉴 건너뛰기




Volumn 319, Issue 3, 2004, Pages 746-752

Suppression of SARS-CoV entry by peptides corresponding to heptad regions on spike glycoprotein

Author keywords

Entry inhibitor; Peptides; Pseudotyped virus; SARS CoV; Spike protein

Indexed keywords

GLYCOPROTEIN; PEPTIDE DERIVATIVE; PROTEIN INHIBITOR;

EID: 2942594156     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.05.046     Document Type: Article
Times cited : (101)

References (34)
  • 8
    • 0141814730 scopus 로고    scopus 로고
    • The entry of entry inhibitors: A fusion of science and medicine
    • Moore J.P., Doms R.W. The entry of entry inhibitors: a fusion of science and medicine. Proc. Natl. Acad. Sci. USA. 100:2003;10598-10602
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 10598-10602
    • Moore, J.P.1    Doms, R.W.2
  • 9
    • 0034924823 scopus 로고    scopus 로고
    • Mechanisms of viral membrane fusion and its inhibition
    • Eckert D.M., Kim P.S. Mechanisms of viral membrane fusion and its inhibition. Annu. Rev. Biochem. 70:2001;777-810
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 777-810
    • Eckert, D.M.1    Kim, P.S.2
  • 11
    • 0033783032 scopus 로고    scopus 로고
    • Receptor binding and membrane fusion in virus entry: The influenza hemagglutinin
    • Skehel J.J., Wiley D.C. Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin. Annu. Rev. Biochem. 69:2000;531-569
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 531-569
    • Skehel, J.J.1    Wiley, D.C.2
  • 12
    • 0034120341 scopus 로고    scopus 로고
    • Membrane fusion mediated by coiled coils: A hypothesis
    • Bentz J. Membrane fusion mediated by coiled coils: a hypothesis. Biophys. J. 78:2000;886-900
    • (2000) Biophys. J. , vol.78 , pp. 886-900
    • Bentz, J.1
  • 13
    • 0032935886 scopus 로고    scopus 로고
    • The paramyxovirus fusion protein forms an extremely stable core trimer: Structural parallels to influenza virus haemagglutinin and HIV-1 gp41
    • Lamb R.A., Joshi S.B., Dutch R.E. The paramyxovirus fusion protein forms an extremely stable core trimer: structural parallels to influenza virus haemagglutinin and HIV-1 gp41. Mol. Membr. Biol. 16:1999;11-19
    • (1999) Mol. Membr. Biol. , vol.16 , pp. 11-19
    • Lamb, R.A.1    Joshi, S.B.2    Dutch, R.E.3
  • 14
    • 0036534449 scopus 로고    scopus 로고
    • New insights into the mechanism of virus-induced membrane fusion
    • Peisajovich S.G., Shai Y. New insights into the mechanism of virus-induced membrane fusion. Trends Biochem. Sci. 27:2002;183-190
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 183-190
    • Peisajovich, S.G.1    Shai, Y.2
  • 15
    • 0033771310 scopus 로고    scopus 로고
    • Functional importance of the coiled-coil of the Ebola virus glycoprotein
    • Watanabe S., Takada A., Watanabe T., Ito H., Kida H., Kawaoka Y. Functional importance of the coiled-coil of the Ebola virus glycoprotein. J. Virol. 74:2000;10194-10201
    • (2000) J. Virol. , vol.74 , pp. 10194-10201
    • Watanabe, S.1    Takada, A.2    Watanabe, T.3    Ito, H.4    Kida, H.5    Kawaoka, Y.6
  • 16
    • 0042208243 scopus 로고    scopus 로고
    • The coronavirus spike protein is a class I virus fusion protein: Structural and functional characterization of the fusion core complex
    • Bosch B.J., van der Zee R., de Haan C.A., Rottier P.J. The coronavirus spike protein is a class I virus fusion protein: structural and functional characterization of the fusion core complex. J. Virol. 77:2003;8801-8811
    • (2003) J. Virol. , vol.77 , pp. 8801-8811
    • Bosch, B.J.1    Van Der Zee, R.2    De Haan, C.A.3    Rottier, P.J.4
  • 17
    • 0035793406 scopus 로고    scopus 로고
    • Protein design of an HIV-1 entry inhibitor
    • Root M.J., Kay M.S., 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
    • 0034027019 scopus 로고    scopus 로고
    • Inhibition of HIV-1 infection by an intramolecular antisense peptide to T20 in gp160
    • Imai M., Okada N., Okada H. Inhibition of HIV-1 infection by an intramolecular antisense peptide to T20 in gp160. Microbiol. Immunol. 44:2000;205-212
    • (2000) Microbiol. Immunol. , vol.44 , pp. 205-212
    • Imai, M.1    Okada, N.2    Okada, H.3
  • 20
    • 0942298133 scopus 로고    scopus 로고
    • A 193-amino acid fragment of the SARS coronavirus S protein efficiently binds angiotensin-converting enzyme 2
    • Wong S.K., Li W., Moore M.J., Choe H., Farzan M. A 193-amino acid fragment of the SARS coronavirus S protein efficiently binds angiotensin-converting enzyme 2. J. Biol. Chem. 279:2004;3197-3201
    • (2004) J. Biol. Chem. , vol.279 , pp. 3197-3201
    • Wong, S.K.1    Li, W.2    Moore, M.J.3    Choe, H.4    Farzan, M.5
  • 22
    • 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., 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
  • 23
    • 3042845376 scopus 로고    scopus 로고
    • Cloaked similarity between HIV-1 and SARS-CoV suggests an anti-SARS strategy
    • Kliger Y., Levanon E.Y. Cloaked similarity between HIV-1 and SARS-CoV suggests an anti-SARS strategy. BMC Microbiol. 3:2003;20
    • (2003) BMC Microbiol. , vol.3 , pp. 20
    • Kliger, Y.1    Levanon, E.Y.2
  • 25
    • 0033618320 scopus 로고    scopus 로고
    • LearnCoil-VMF: Computational evidence for coiled-coil-like motifs in many viral membrane-fusion proteins
    • Singh M., Berger B., 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
  • 26
    • 1642488368 scopus 로고    scopus 로고
    • Characterization of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) spike glycoprotein-mediated viral entry
    • Simmons G., Reeves J.D., Rennekamp A.J., Amberg S.M., Piefer A.J., Bates P. Characterization of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) spike glycoprotein-mediated viral entry. Proc. Natl. Acad. Sci. USA. 2004
    • (2004) Proc. Natl. Acad. Sci. USA
    • Simmons, G.1    Reeves, J.D.2    Rennekamp, A.J.3    Amberg, S.M.4    Piefer, A.J.5    Bates, P.6
  • 28
    • 2942554766 scopus 로고    scopus 로고
    • Identification of an antigenic determinant on the S2 domain of the SARS-CoV spike glycoprotein capable of inducing neutralizing antibodies
    • in press
    • Hong Zhang, Guangwen Wang, Jian Li, Yuchun Nie, Xuanling Shi, Gewei Lian, Wei Wang, Xiaolei Yin, Yang Zhao, Xiuxia Qu, M. Ding, H. Deng, Identification of an antigenic determinant on the S2 domain of the SARS-CoV spike glycoprotein capable of inducing neutralizing antibodies, J. Virol. (2004) in press
    • (2004) J. Virol.
    • Zhang, H.1    Wang, G.2    Li, J.3    Nie, Y.4    Shi, X.5    Lian, G.6    Wang, W.7    Yin, X.8    Zhao, Y.9    Qu, X.10    Ding, M.11    Deng, H.12
  • 29
    • 0027531682 scopus 로고
    • A new approach for measurement of cytotoxicity using colorimetric assay
    • Hussain R.F., Nouri A.M., Oliver R.T. A new approach for measurement of cytotoxicity using colorimetric assay. J. Immunol. Methods. 160:1993;89-96
    • (1993) J. Immunol. Methods , vol.160 , pp. 89-96
    • Hussain, R.F.1    Nouri, A.M.2    Oliver, R.T.3
  • 30
    • 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., Shugars D.C., Greenwell T.K., McDanal C.B., Matthews T.J. 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. USA. 91:1994;9770-9774
    • (1994) Proc. Natl. Acad. Sci. USA , 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
  • 31
    • 0028834461 scopus 로고
    • A trimeric structural domain of the HIV-1 transmembrane glycoprotein
    • Lu M., Blacklow S.C., Kim P.S. A trimeric structural domain of the HIV-1 transmembrane glycoprotein. Nat. Struct. Biol. 2:1995;1075-1082
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 1075-1082
    • Lu, M.1    Blacklow, S.C.2    Kim, P.S.3
  • 32
    • 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., 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
  • 34
    • 0038671938 scopus 로고    scopus 로고
    • The hydrophobic pocket contributes to the structural stability of the N-terminal coiled coil of HIV gp41 but is not required for six-helix bundle formation
    • Dwyer J.J., Hasan A., Wilson K.L., White J.M., Matthews T.J., Delmedico M.K. The hydrophobic pocket contributes to the structural stability of the N-terminal coiled coil of HIV gp41 but is not required for six-helix bundle formation. Biochemistry. 42:2003;4945-4953
    • (2003) Biochemistry , vol.42 , pp. 4945-4953
    • Dwyer, J.J.1    Hasan, A.2    Wilson, K.L.3    White, J.M.4    Matthews, T.J.5    Delmedico, M.K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.