메뉴 건너뛰기




Volumn 111, Issue 1, 2014, Pages 125-130

Production and stabilization of the trimeric influenza hemagglutinin stem domain for potentially broadly protective influenza vaccines

Author keywords

[No Author keywords available]

Indexed keywords

HEMAGGLUTININ; INFLUENZA VACCINE; MONOMER; NEUTRALIZING ANTIBODY; POLIDOCANOL; POLYPEPTIDE;

EID: 84891912497     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1308701110     Document Type: Article
Times cited : (172)

References (31)
  • 1
    • 77956379133 scopus 로고    scopus 로고
    • Design of an HA2-based Escherichia coli expressed influenza immunogen that protects mice from pathogenic challenge
    • Bommakanti G, et al. (2010) Design of an HA2-based Escherichia coli expressed influenza immunogen that protects mice from pathogenic challenge. Proc Natl Acad Sci USA 107(31): 13701-13706.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.31 , pp. 13701-13706
    • Bommakanti, G.1
  • 2
    • 79953309492 scopus 로고    scopus 로고
    • Cell-based flu vaccines ready for US prime time
    • Extance A (2011) Cell-based flu vaccines ready for US prime time. Nat Rev Drug Discov 10(4): 246-247.
    • (2011) Nat Rev Drug Discov , vol.10 , Issue.4 , pp. 246-247
    • Extance, A.1
  • 3
    • 84883223706 scopus 로고    scopus 로고
    • Recombinant trivalent influenza vaccine (flublok(-)): A review of its use in the prevention of seasonal influenza in adults
    • Yang LPH (2013) Recombinant trivalent influenza vaccine (flublok(-)): A review of its use in the prevention of seasonal influenza in adults. Drugs 73(12): 1357-1366.
    • (2013) Drugs , vol.73 , Issue.12 , pp. 1357-1366
    • Yang, L.P.H.1
  • 4
    • 45149130345 scopus 로고    scopus 로고
    • Vaccine preparedness-are we ready for the next influenza pandemic?
    • Wright PF (2008) Vaccine preparedness-are we ready for the next influenza pandemic? N Engl J Med 358(24): 2540-2543.
    • (2008) N Engl J Med , vol.358 , Issue.24 , pp. 2540-2543
    • Wright, P.F.1
  • 5
    • 0036337409 scopus 로고    scopus 로고
    • Cleavage of influenza a virus hemagglutinin in human respiratory epithelium is cell associated and sensitive to exogenous antiproteases
    • Zhirnov OP, Ikizler MR, Wright PF (2002) Cleavage of influenza a virus hemagglutinin in human respiratory epithelium is cell associated and sensitive to exogenous antiproteases. J Virol 76(17): 8682-8689.
    • (2002) J Virol , vol.76 , Issue.17 , pp. 8682-8689
    • Zhirnov, O.P.1    Ikizler, M.R.2    Wright, P.F.3
  • 6
    • 70449099712 scopus 로고    scopus 로고
    • Attacking the flu: Neutralizing antibodies may lead to 'universal' vaccine
    • Chen GL, Subbarao K (2009) Attacking the flu: Neutralizing antibodies may lead to 'universal' vaccine. Nat Med 15(11): 1251-1252.
    • (2009) Nat Med , vol.15 , Issue.11 , pp. 1251-1252
    • Chen, G.L.1    Subbarao, K.2
  • 7
    • 77952533063 scopus 로고    scopus 로고
    • High frequency of cross-reacting antibodies against 2009 pandemic influenza A(H1N1) virus among the elderly in Finland
    • Ikonen N, et al. (2010) High frequency of cross-reacting antibodies against 2009 pandemic influenza A(H1N1) virus among the elderly in Finland. Euro Surveill 15(5): 16-23.
    • (2010) Euro Surveill , vol.15 , Issue.5 , pp. 16-23
    • Ikonen, N.1
  • 8
    • 0029022681 scopus 로고
    • Low-pH induced conformational changes in viral fusion proteins: Implications for the fusion mechanism
    • Gaudin Y, Ruigrok RWH, Brunner J (1995) Low-pH induced conformational changes in viral fusion proteins: Implications for the fusion mechanism. J Gen Virol 76(Pt 7): 1541-1556.
    • (1995) J Gen Virol , vol.76 , Issue.PART 7 , pp. 1541-1556
    • Gaudin, Y.1    Ruigrok, R.W.H.2    Brunner, J.3
  • 9
    • 79952140653 scopus 로고    scopus 로고
    • Influenza virus vaccine based on the conserved hemagglutinin stalk domain
    • Steel J, et al. (2010) Influenza virus vaccine based on the conserved hemagglutinin stalk domain. MBio 1(1): E00018-E10.
    • (2010) MBio , vol.1 , Issue.1
    • Steel, J.1
  • 10
    • 78649953803 scopus 로고    scopus 로고
    • Vaccination with a synthetic peptide from the influenza virus hemagglutinin provides protection against distinct viral subtypes
    • Wang TT, et al. (2010) Vaccination with a synthetic peptide from the influenza virus hemagglutinin provides protection against distinct viral subtypes. Proc Natl Acad Sci USA 107(44): 18979-18984.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.44 , pp. 18979-18984
    • Wang, T.T.1
  • 11
    • 84861872090 scopus 로고    scopus 로고
    • Pandemic H1N1 influenza vaccine induces a recall response in humans that favors broadly cross-reactive memory B cells
    • Li GM, et al. (2012) Pandemic H1N1 influenza vaccine induces a recall response in humans that favors broadly cross-reactive memory B cells. Proc Natl Acad Sci USA 109(23): 9047-9052.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.23 , pp. 9047-9052
    • Li, G.M.1
  • 12
    • 64849114224 scopus 로고    scopus 로고
    • Antibody recognition of a highly conserved influenza virus epitope
    • Ekiert DC, et al. (2009) Antibody recognition of a highly conserved influenza virus epitope. Science 324(5924): 246-251.
    • (2009) Science , vol.324 , Issue.5924 , pp. 246-251
    • Ekiert, D.C.1
  • 13
    • 77956119219 scopus 로고    scopus 로고
    • Induction of broadly neutralizing H1N1 influenza antibodies by vaccination
    • Wei CJ, et al. (2010) Induction of broadly neutralizing H1N1 influenza antibodies by vaccination. Science 329(5995): 1060-1064.
    • (2010) Science , vol.329 , Issue.5995 , pp. 1060-1064
    • Wei, C.J.1
  • 14
    • 2442629758 scopus 로고    scopus 로고
    • Full-length influenza hemagglutinin HA(2) refolds into the trimeric low-pH-induced conformation
    • Swalley SE, et al. (2004) Full-length influenza hemagglutinin HA(2) refolds into the trimeric low-pH-induced conformation. Biochemistry-Us 43(19): 5902-5911.
    • (2004) Biochemistry-Us , vol.43 , Issue.19 , pp. 5902-5911
    • Swalley, S.E.1
  • 15
    • 50049096697 scopus 로고    scopus 로고
    • Isotopically labeled expression in E. Coli, purification, and refolding of the full ectodomain of the influenza virus membrane fusion protein
    • Curtis-Fisk J, Spencer RM, Weliky DP (2008) Isotopically labeled expression in E. coli, purification, and refolding of the full ectodomain of the influenza virus membrane fusion protein. Protein Expr Purif 61(2): 212-219.
    • (2008) Protein Expr Purif , vol.61 , Issue.2 , pp. 212-219
    • Curtis-Fisk, J.1    Spencer, R.M.2    Weliky, D.P.3
  • 16
    • 70349781658 scopus 로고    scopus 로고
    • Preparation, characterization, and immunogenicity in mice of a recombinant influenza H5 hemagglutinin vaccine against the avian H5N1 A/Vietnam/ 1203/2004 influenza virus
    • Biesova Z, et al. (2009) Preparation, characterization, and immunogenicity in mice of a recombinant influenza H5 hemagglutinin vaccine against the avian H5N1 A/Vietnam/ 1203/2004 influenza virus. Vaccine 27(44): 6234-6238.
    • (2009) Vaccine , vol.27 , Issue.44 , pp. 6234-6238
    • Biesova, Z.1
  • 17
    • 84875236527 scopus 로고    scopus 로고
    • Structure and accessibility of HA trimers on intact 2009 H1N1 pandemic influenza virus to stem region-specific neutralizing antibodies
    • Harris AK, et al. (2013) Structure and accessibility of HA trimers on intact 2009 H1N1 pandemic influenza virus to stem region-specific neutralizing antibodies. Proc Natl Acad Sci USA 110(12): 4592-4597.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.12 , pp. 4592-4597
    • Harris, A.K.1
  • 18
    • 0031570687 scopus 로고    scopus 로고
    • Structure of bacteriophage T4 fibritin: A segmented coiled coil and the role of the C-terminal domain
    • Tao YZ, Strelkov SV, Mesyanzhinov VV, Rossmann MG (1997) Structure of bacteriophage T4 fibritin: A segmented coiled coil and the role of the C-terminal domain. Structure 5(6): 789-798.
    • (1997) Structure , vol.5 , Issue.6 , pp. 789-798
    • Tao, Y.Z.1    Strelkov, S.V.2    Mesyanzhinov, V.V.3    Rossmann, M.G.4
  • 19
    • 1642352884 scopus 로고    scopus 로고
    • Structure of the uncleaved human H1 hemagglutinin from the extinct 1918 influenza virus
    • Stevens J, et al. (2004) Structure of the uncleaved human H1 hemagglutinin from the extinct 1918 influenza virus. Science 303(5665): 1866-1870.
    • (2004) Science , vol.303 , Issue.5665 , pp. 1866-1870
    • Stevens, J.1
  • 20
    • 0025335792 scopus 로고
    • Refined crystal structure of type III chloramphenicol acetyltransferase at 1.75 A resolution
    • Leslie AGW (1990) Refined crystal structure of type III chloramphenicol acetyltransferase at 1.75 A resolution. J Mol Biol 213(1): 167-186.
    • (1990) J Mol Biol , vol.213 , Issue.1 , pp. 167-186
    • Leslie, A.G.W.1
  • 21
    • 84864953230 scopus 로고    scopus 로고
    • Cell-free protein synthesis: Applications come of age
    • Carlson ED, Gan R, Hodgman CE, Jewett MC (2012) Cell-free protein synthesis: Applications come of age. Biotechnol Adv 30(5): 1185-1194.
    • (2012) Biotechnol Adv , vol.30 , Issue.5 , pp. 1185-1194
    • Carlson, E.D.1    Gan, R.2    Hodgman, C.E.3    Jewett, M.C.4
  • 22
    • 84863249248 scopus 로고    scopus 로고
    • Aglycosylated antibodies and antibody fragments produced in a scalable in vitro transcription-translation system
    • Yin G, et al. (2012) Aglycosylated antibodies and antibody fragments produced in a scalable in vitro transcription-translation system. MAbs 4(2).
    • (2012) MAbs , vol.4 , Issue.2
    • Yin, G.1
  • 23
    • 79956158054 scopus 로고    scopus 로고
    • Microscale to manufacturing scale-up of cell-free cytokine production - A new approach for shortening protein production development timelines
    • Zawada JF, et al. (2011) Microscale to manufacturing scale-up of cell-free cytokine production-a new approach for shortening protein production development timelines. Biotechnol Bioeng 108(7): 1570-1578.
    • (2011) Biotechnol Bioeng , vol.108 , Issue.7 , pp. 1570-1578
    • Zawada, J.F.1
  • 24
    • 38449099301 scopus 로고    scopus 로고
    • Development of cell-free protein synthesis platforms for disulfide bonded proteins
    • Goerke AR, Swartz JR (2008) Development of cell-free protein synthesis platforms for disulfide bonded proteins. Biotechnol Bioeng 99(2): 351-367.
    • (2008) Biotechnol Bioeng , vol.99 , Issue.2 , pp. 351-367
    • Goerke, A.R.1    Swartz, J.R.2
  • 25
    • 0030046574 scopus 로고    scopus 로고
    • In vitro folding of inclusion body proteins
    • Rudolph R, Lilie H (1996) In vitro folding of inclusion body proteins. FASEB J 10(1): 49-56.
    • (1996) FASEB J , vol.10 , Issue.1 , pp. 49-56
    • Rudolph, R.1    Lilie, H.2
  • 26
    • 0032190686 scopus 로고    scopus 로고
    • Advances in refolding of proteins produced in E. Coli
    • Lilie H, Schwarz E, Rudolph R (1998) Advances in refolding of proteins produced in E. coli. Curr Opin Biotechnol 9(5): 497-501.
    • (1998) Curr Opin Biotechnol , vol.9 , Issue.5 , pp. 497-501
    • Lilie, H.1    Schwarz, E.2    Rudolph, R.3
  • 27
    • 0041018174 scopus 로고
    • Single-step solubilization and folding of Igf-1 aggregates from Escherichia-coli
    • Chang JY, Swartz JR (1993) Single-step solubilization and folding of Igf-1 aggregates from Escherichia-coli. ACS Symp Ser 526: 178-188.
    • (1993) ACS Symp ser , vol.526 , pp. 178-188
    • Chang, J.Y.1    Swartz, J.R.2
  • 28
    • 0032619552 scopus 로고    scopus 로고
    • Protein identification and analysis tools in the ExPASy server
    • Wilkins MR, et al. (1999) Protein identification and analysis tools in the ExPASy server. Methods Mol Biol 112: 531-552.
    • (1999) Methods Mol Biol , vol.112 , pp. 531-552
    • Wilkins, M.R.1
  • 29
    • 84875551472 scopus 로고    scopus 로고
    • Broadly neutralizing antiviral antibodies
    • Corti D, Lanzavecchia A (2013) Broadly neutralizing antiviral antibodies. Annu Rev Immunol 31: 705-742.
    • (2013) Annu Rev Immunol , vol.31 , pp. 705-742
    • Corti, D.1    Lanzavecchia, A.2
  • 30
    • 1542720448 scopus 로고    scopus 로고
    • Mimicking the Escherichia coli cytoplasmic environment activates long-lived and efficient cell-free protein synthesis
    • Jewett MC, Swartz JR (2004) Mimicking the Escherichia coli cytoplasmic environment activates long-lived and efficient cell-free protein synthesis. Biotechnol Bioeng 86(1): 19-26.
    • (2004) Biotechnol Bioeng , vol.86 , Issue.1 , pp. 19-26
    • Jewett, M.C.1    Swartz, J.R.2
  • 31
    • 84879601253 scopus 로고    scopus 로고
    • Escherichia coli-based cell free production of flagellin and ordered flagellin display on virus-like particles
    • Lu Y, Welsh JP, Chan W, Swartz JR (2013) Escherichia coli-based cell free production of flagellin and ordered flagellin display on virus-like particles. Biotechnol Bioeng 110(8): 2073-2085.
    • (2013) Biotechnol Bioeng , vol.110 , Issue.8 , pp. 2073-2085
    • Lu, Y.1    Welsh, J.P.2    Chan, W.3    Swartz, J.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.