메뉴 건너뛰기




Volumn 89, Issue 14, 2015, Pages 7417-7420

Design and structure of an engineered disulfide-stabilized influenza virus hemagglutinin trimer

Author keywords

[No Author keywords available]

Indexed keywords

ANTIGEN; VIRUS GLYCOPROTEIN; VIRUS HEMAGGLUTININ; DISULFIDE; INFLUENZA VIRUS HEMAGGLUTININ; PROTEIN BINDING; VIRUS ANTIBODY; VIRUS ANTIGEN;

EID: 84931049237     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.00808-15     Document Type: Article
Times cited : (30)

References (31)
  • 1
    • 84875551472 scopus 로고    scopus 로고
    • Broadly neutralizing antiviral antibodies
    • Corti D, Lanzavecchia A. 2013. Broadly neutralizing antiviral antibodies. Annu Rev Immunol 31:705-742. http://dx.doi.org/10.1146/annurev-immunol-032712-095916.
    • (2013) Annu Rev Immunol , vol.31 , pp. 705-742
    • Corti, D.1    Lanzavecchia, A.2
  • 2
    • 84921847141 scopus 로고    scopus 로고
    • Structural characterization of viral epitopes recognized by broadly cross-reactive antibodies
    • Lee PS, Wilson IA. 2015. Structural characterization of viral epitopes recognized by broadly cross-reactive antibodies. Curr Top Microbiol Immunol 386:323-341. http://dx.doi.org/10.1007/82_2014_413.
    • (2015) Curr Top Microbiol Immunol , vol.386 , pp. 323-341
    • Lee, P.S.1    Wilson, I.A.2
  • 3
    • 0019890491 scopus 로고
    • Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution
    • Wilson IA, Skehel JJ, Wiley DC. 1981. Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution. Nature 289: 366-373. http://dx.doi.org/10.1038/289366a0.
    • (1981) Nature , vol.289 , pp. 366-373
    • Wilson, I.A.1    Skehel, J.J.2    Wiley, D.C.3
  • 4
    • 84873403163 scopus 로고    scopus 로고
    • Structure and receptor binding properties of a pandemic H1N1 virus hemagglutinin
    • Yang H, Carney P, Stevens J. 2010. Structure and receptor binding properties of a pandemic H1N1 virus hemagglutinin. PLoS Curr 2:RRN1152. http://dx.doi.org/10.1371/currents.RRN1152.
    • (2010) PLoS Curr , vol.2
    • Yang, H.1    Carney, P.2    Stevens, J.3
  • 5
    • 77957816428 scopus 로고    scopus 로고
    • Crystal structure of the swine-origin A (H1N1)-2009 influenza A virus hemagglutinin (HA) reveals similar antigenicity to that of the 1918 pandemic virus
    • Zhang W, Qi J, Shi Y, Li Q, Gao F, Sun Y, Lu X, Lu Q, Vavricka CJ, Liu D, Yan J, Gao GF. 2010. Crystal structure of the swine-origin A (H1N1)-2009 influenza A virus hemagglutinin (HA) reveals similar antigenicity to that of the 1918 pandemic virus. Protein Cell 1:459-467. http://dx.doi.org/10.1007/s13238-010-0059-1.
    • (2010) Protein Cell , vol.1 , pp. 459-467
    • Zhang, W.1    Qi, J.2    Shi, Y.3    Li, Q.4    Gao, F.5    Sun, Y.6    Lu, X.7    Lu, Q.8    Vavricka, C.J.9    Liu, D.10    Yan, J.11    Gao, G.F.12
  • 6
    • 84856875534 scopus 로고    scopus 로고
    • Structural characterization of the hemagglutinin receptor specificity from the 2009 H1N1 influenza pandemic
    • Xu R, McBride R, Nycholat CM, Paulson JC, Wilson IA. 2012. Structural characterization of the hemagglutinin receptor specificity from the 2009 H1N1 influenza pandemic. J Virol 86:982-990. http://dx.doi.org/10.1128/JVI.06322-11.
    • (2012) J Virol , vol.86 , pp. 982-990
    • Xu, R.1    McBride, R.2    Nycholat, C.M.3    Paulson, J.C.4    Wilson, I.A.5
  • 7
    • 79952702297 scopus 로고    scopus 로고
    • Antigenic stability of H1N1 pandemic vaccines correlates with vaccine strain
    • Farnsworth A, Cyr TD, Li C, Wang J, Li X. 2011. Antigenic stability of H1N1 pandemic vaccines correlates with vaccine strain. Vaccine 29:1529-1533. http://dx.doi.org/10.1016/j.vaccine.2010.12.120.
    • (2011) Vaccine , vol.29 , pp. 1529-1533
    • Farnsworth, A.1    Cyr, T.D.2    Li, C.3    Wang, J.4    Li, X.5
  • 10
    • 34547770260 scopus 로고    scopus 로고
    • Reversible inhibition of the fusion activity of measles virus F protein by an engineered intersubunit disulfide bridge
    • Lee JK, Prussia A, Snyder JP, Plemper RK. 2007. Reversible inhibition of the fusion activity of measles virus F protein by an engineered intersubunit disulfide bridge. J Virol 81:8821-8826. http://dx.doi.org/10.1128/JVI.00754-07.
    • (2007) J Virol , vol.81 , pp. 8821-8826
    • Lee, J.K.1    Prussia, A.2    Snyder, J.P.3    Plemper, R.K.4
  • 12
    • 0024818499 scopus 로고
    • Stereochemical modeling of disulfide bridges. Criteria for introduction into proteins by site-directed mutagenesis
    • Sowdhamini R, Srinivasan N, Shoichet B, Santi DV, Ramakrishnan C, Balaram P. 1989. Stereochemical modeling of disulfide bridges. Criteria for introduction into proteins by site-directed mutagenesis. Protein Eng 3:95-103.
    • (1989) Protein Eng , vol.3 , pp. 95-103
    • Sowdhamini, R.1    Srinivasan, N.2    Shoichet, B.3    Santi, D.V.4    Ramakrishnan, C.5    Balaram, P.6
  • 18
    • 84911404794 scopus 로고    scopus 로고
    • Receptor mimicry by antibody F045-092 facilitates universal binding to the H3 subtype of influenza virus
    • Lee PS, Ohshima N, Stanfield RL, Yu W, Iba Y, Okuno Y, Kurosawa Y, Wilson IA. 2014. Receptor mimicry by antibody F045-092 facilitates universal binding to the H3 subtype of influenza virus. Nat Commun 5:3614. http://dx.doi.org/10.1093/emboj/21.5.865.
    • (2014) Nat Commun , vol.5 , pp. 3614
    • Lee, P.S.1    Ohshima, N.2    Stanfield, R.L.3    Yu, W.4    Iba, Y.5    Okuno, Y.6    Kurosawa, Y.7    Wilson, I.A.8
  • 19
    • 0036500549 scopus 로고    scopus 로고
    • H5 avian and H9 swine influenza virus haemagglutinin structures: possible origin of influenza subtypes
    • Ha Y, Stevens DJ, Skehel JJ, Wiley DC. 2002. H5 avian and H9 swine influenza virus haemagglutinin structures: possible origin of influenza subtypes. EMBO J 21:865-875. http://dx.doi.org/10.1093/emboj/21.5.865.
    • (2002) EMBO J , vol.21 , pp. 865-875
    • Ha, Y.1    Stevens, D.J.2    Skehel, J.J.3    Wiley, D.C.4
  • 20
    • 3142574848 scopus 로고    scopus 로고
    • H1 and H7 influenza haemagglutinin structures extend a structural classification of haemagglutinin subtypes
    • Russell RJ, Gamblin SJ, Haire LF, Stevens DJ, Xiao B, Ha Y, Skehel JJ. 2004. H1 and H7 influenza haemagglutinin structures extend a structural classification of haemagglutinin subtypes. Virology 325:287-296. http://dx.doi.org/10.1016/j.virol.2004.04.040.
    • (2004) Virology , vol.325 , pp. 287-296
    • Russell, R.J.1    Gamblin, S.J.2    Haire, L.F.3    Stevens, D.J.4    Xiao, B.5    Ha, Y.6    Skehel, J.J.7
  • 21
    • 0026560161 scopus 로고
    • Introduction of intersubunit disulfide bonds in the membrane-distal region of the influenza hemagglutinin abolishes membrane fusion activity
    • Godley L, Pfeifer J, Steinhauer D, Ely B, Shaw G, Kaufmann R, Suchanek E, Pabo C, Skehel JJ, Wiley DC, Wharton S. 1992. Introduction of intersubunit disulfide bonds in the membrane-distal region of the influenza hemagglutinin abolishes membrane fusion activity. Cell 68:635-645. http://dx.doi.org/10.1016/0092-8674(92)90140-8.
    • (1992) Cell , vol.68 , pp. 635-645
    • Godley, L.1    Pfeifer, J.2    Steinhauer, D.3    Ely, B.4    Shaw, G.5    Kaufmann, R.6    Suchanek, E.7    Pabo, C.8    Skehel, J.J.9    Wiley, D.C.10    Wharton, S.11
  • 22
    • 0028023726 scopus 로고
    • Structure of influenza haemagglutinin at the pH of membrane fusion
    • Bullough PA, Hughson FM, Skehel JJ, Wiley DC. 1994. Structure of influenza haemagglutinin at the pH of membrane fusion. Nature 371:37-43. http://dx.doi.org/10.1038/371037a0.
    • (1994) Nature , vol.371 , pp. 37-43
    • Bullough, P.A.1    Hughson, F.M.2    Skehel, J.J.3    Wiley, D.C.4
  • 23
    • 79955373167 scopus 로고    scopus 로고
    • Structural characterization of an early fusion intermediate of influenza virus hemagglutinin
    • Xu R, Wilson IA. 2011. Structural characterization of an early fusion intermediate of influenza virus hemagglutinin. J Virol 85:5172-5182. http://dx.doi.org/10.1128/JVI.02430-10.
    • (2011) J Virol , vol.85 , pp. 5172-5182
    • Xu, R.1    Wilson, I.A.2
  • 27
    • 84870656355 scopus 로고    scopus 로고
    • Design of Escherichia coli-expressed stalk domain immunogens of H1N1 hemagglutinin that protect mice from lethal challenge
    • Bommakanti G, Lu X, Citron MP, Najar TA, Heidecker GJ, Ter Meulen J, Varadarajan R, Liang X. 2012. Design of Escherichia coli-expressed stalk domain immunogens of H1N1 hemagglutinin that protect mice from lethal challenge. J Virol 86:13434-13444. http://dx.doi.org/10.1128/JVI.01429-12.
    • (2012) J Virol , vol.86 , pp. 13434-13444
    • Bommakanti, G.1    Lu, X.2    Citron, M.P.3    Najar, T.A.4    Heidecker, G.J.5    Ter Meulen, J.6    Varadarajan, R.7    Liang, X.8
  • 28
    • 84885953445 scopus 로고    scopus 로고
    • Influenza virus hemagglutinin stalk-based antibodies and vaccines
    • Krammer F, Palese P. 2013. Influenza virus hemagglutinin stalk-based antibodies and vaccines. Curr Opin Virol 3:521-530. http://dx.doi.org/10.1016/j.coviro.2013.07.007.
    • (2013) Curr Opin Virol , vol.3 , pp. 521-530
    • Krammer, F.1    Palese, P.2
  • 29
    • 84891912497 scopus 로고    scopus 로고
    • Production and stabilization of the trimeric influenza hemagglutinin stem domain for potentially broadly protective influenza vaccines
    • Lu Y, Welsh JP, Swartz JR. 2014. Production and stabilization of the trimeric influenza hemagglutinin stem domain for potentially broadly protective influenza vaccines. Proc Natl Acad Sci USA 111:125-130. http://dx.doi.org/10.1073/pnas.1308701110.
    • (2014) Proc Natl Acad Sci USA , vol.111 , pp. 125-130
    • Lu, Y.1    Welsh, J.P.2    Swartz, J.R.3
  • 31
    • 0029558245 scopus 로고
    • A soluble domain of the membrane-anchoring chain of influenza virus hemagglutinin (HA2) folds in Escherichia coli into the low-pH-induced conformation
    • Chen J, Wharton SA, Weissenhorn W, Calder LJ, Hughson FM, Skehel JJ, Wiley DC. 1995. A soluble domain of the membrane-anchoring chain of influenza virus hemagglutinin (HA2) folds in Escherichia coli into the low-pH-induced conformation. Proc Natl Acad Sci USA 92:12205-12209. http://dx.doi.org/10.1073/pnas.92.26.12205.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 12205-12209
    • Chen, J.1    Wharton, S.A.2    Weissenhorn, W.3    Calder, L.J.4    Hughson, F.M.5    Skehel, J.J.6    Wiley, D.C.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.