메뉴 건너뛰기




Volumn 29, Issue 8, 2011, Pages 1529-1533

Antigenic stability of H1N1 pandemic vaccines correlates with vaccine strain

Author keywords

H1N1 2009; Influenza; Vaccine stability

Indexed keywords

HEMAGGLUTININ; INFLUENZA VACCINE;

EID: 79952702297     PISSN: 0264410X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.vaccine.2010.12.120     Document Type: Article
Times cited : (34)

References (18)
  • 3
    • 85030583733 scopus 로고    scopus 로고
    • Health Canada
    • Information update, Ottawa
    • Health Canada. New expiry date for unused adjuvanted H1N1 vaccine. Information update, vol. 2010, Ottawa. http://www.hc-sc.gc.ca/ahc-asc/media/advisories-avis/2010/201054-eng.php; 2010.
    • (2010) New expiry date for unused adjuvanted H1N1 vaccine , vol.2010
  • 4
    • 85030577432 scopus 로고    scopus 로고
    • Minnesota Department of Health
    • Minnesota Department of Health. Vaccine recalls. http://www.health.state.mn.us/divs/idepc/diseases/flu/hcp/vaccine/recalls.html; 2010.
    • (2010) Vaccine recalls
  • 5
    • 85030580958 scopus 로고    scopus 로고
    • Department of Health and Ageing
    • Therapeutic Goods Administration
    • Therapeutic Goods Administration, Department of Health and Ageing. Withdrawl of Panvax Junior. http://www.tga.gov.au/alerts/medicines/panvax-jr-withdrawal.htm; 2010.
    • (2010) Withdrawl of Panvax Junior
  • 6
    • 77956231586 scopus 로고    scopus 로고
    • Strain identification of commercial influenza vaccines by mass spectrometry
    • Creskey MC, Smith DG, Cyr TD. Strain identification of commercial influenza vaccines by mass spectrometry. Anal Biochem 2010.
    • (2010) Anal Biochem
    • Creskey, M.C.1    Smith, D.G.2    Cyr, T.D.3
  • 7
    • 77955553259 scopus 로고    scopus 로고
    • Qualitative and quantitative analyses of virtually all subtypes of influenza A and B viral neu-raminidases using antibodies targeting the universally conserved sequences
    • Gravel C, Li C, Wang J, Hashem AM, Jaentschke B, Xu KW, et al. Qualitative and quantitative analyses of virtually all subtypes of influenza A and B viral neu-raminidases using antibodies targeting the universally conserved sequences. Vaccine 2010;28:5774-84.
    • (2010) Vaccine , vol.28 , pp. 5774-5784
    • Gravel, C.1    Li, C.2    Wang, J.3    Hashem, A.M.4    Jaentschke, B.5    Xu, K.W.6
  • 8
  • 9
    • 77951165843 scopus 로고    scopus 로고
    • Structural basis of preexisting immunity to the 2009 H1N1 pandemic influenza virus
    • Xu R, Ekiert DC, Krause JC, Hai R, Crowe Jr JE, Wilson IA. Structural basis of preexisting immunity to the 2009 H1N1 pandemic influenza virus. Science 2010;328:357-60.
    • (2010) Science , vol.328 , pp. 357-360
    • Xu, R.1    Ekiert, D.C.2    Krause, J.C.3    Hai, R.4    Crowe Jr., J.E.5    Wilson, I.A.6
  • 10
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer:an environmentfor comparative protein modeling
    • Guex N,Peitsch MC. SWISS-MODEL and the Swiss-PdbViewer:an environmentfor comparative protein modeling. Electrophoresis 1997;18:2714-23.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 11
    • 0022886353 scopus 로고
    • Confor-mational changes in the hemagglutinin of influenza virus which accompany heat-induced fusion of virus with liposomes
    • Ruigrok RW, Martin SR, Wharton SA, Skehel JJ, Bayley PM, Wiley DC. Confor-mational changes in the hemagglutinin of influenza virus which accompany heat-induced fusion of virus with liposomes. Virology 1986;155:484-97.
    • (1986) Virology , vol.155 , pp. 484-497
    • Ruigrok, R.W.1    Martin, S.R.2    Wharton, S.A.3    Skehel, J.J.4    Bayley, P.M.5    Wiley, D.C.6
  • 12
    • 34247179103 scopus 로고    scopus 로고
    • Conformational change of influenza virus hemagglutinin is sensitive to ionic concentration
    • Korte T, Ludwig K, Huang Q, Rachakonda PS, Herrmann A. Conformational change of influenza virus hemagglutinin is sensitive to ionic concentration. Eur Biophys J 2007;36:327-35.
    • (2007) Eur Biophys J , vol.36 , pp. 327-335
    • Korte, T.1    Ludwig, K.2    Huang, Q.3    Rachakonda, P.S.4    Herrmann, A.5
  • 13
    • 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, et al. Introduction of intersubunit disulfide bonds in the membrane-distal region of the influenza hemagglutinin abolishes membrane fusion activity. Cell 1992;68:635-45.
    • (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
  • 14
    • 33947661927 scopus 로고    scopus 로고
    • The relevance of salt bridges for the stability of the influenza virus hemagglutinin
    • Rachakonda PS, Veit M, Korte T, Ludwig K, Böttcher C, Huang Q, et al. The relevance of salt bridges for the stability of the influenza virus hemagglutinin. FASEB J 2007;21:995-1002.
    • (2007) FASEB J , vol.21 , pp. 995-1002
    • Rachakonda, P.S.1    Veit, M.2    Korte, T.3    Ludwig, K.4    Böttcher, C.5    Huang, Q.6
  • 15
    • 43249090067 scopus 로고    scopus 로고
    • Theoretical analysis of binding specificity of influenza viral hemagglutinin toavian and human receptors basedonthe fragmentmolecular orbitalmethod
    • Iwata T, Fukuzawa K, Nakajima K, Aida-Hyugaji S, Mochizuki Y, Watanabe H, et al. Theoretical analysis of binding specificity of influenza viral hemagglutinin toavian and human receptors basedonthe fragmentmolecular orbitalmethod. Comput Biol Chem 2008;32:198-211.
    • (2008) Comput Biol Chem , vol.32 , pp. 198-211
    • Iwata, T.1    Fukuzawa, K.2    Nakajima, K.3    Aida-Hyugaji, S.4    Mochizuki, Y.5    Watanabe, H.6
  • 16
    • 0023341238 scopus 로고
    • The receptor-binding and membrane-fusion properties of influenza virus variants selected using anti-haemagglutinin monoclonal antibodies
    • Daniels PS, Jeffries S, Yates P, Schild GC, Rogers GN, Paulson JC, et al. The receptor-binding and membrane-fusion properties of influenza virus variants selected using anti-haemagglutinin monoclonal antibodies. EMBO J 1987;6:1459-65.
    • (1987) EMBO J , vol.6 , pp. 1459-1465
    • Daniels, P.S.1    Jeffries, S.2    Yates, P.3    Schild, G.C.4    Rogers, G.N.5    Paulson, J.C.6
  • 17
    • 77956837160 scopus 로고    scopus 로고
    • Recombinant soluble, multimeric HA and NA exhibit distinctive types of protection against pandemic swine-origin 2009 A(H1N1) influenza virus infection in ferrets
    • Bosch BJ, Bodewes R, de Vries RP, Kreijtz JH, Bartelink W, van Amerongen G, et al. Recombinant soluble, multimeric HA and NA exhibit distinctive types of protection against pandemic swine-origin 2009 A(H1N1) influenza virus infection in ferrets. J Virol 2010;84:10366-74.
    • (2010) J Virol , vol.84 , pp. 10366-10374
    • Bosch, B.J.1    Bodewes, R.2    de Vries, R.P.3    Kreijtz, J.H.4    Bartelink, W.5    van Amerongen, G.6
  • 18
    • 85030574158 scopus 로고    scopus 로고
    • Food and Drug Administration Vaccines
    • Influenza vaccine for the 2010-2011 season
    • Food and Drug Administration Vaccines, Blood & Biologics. Influenza vaccine for the 2010-2011 season http://www.fda.gov/biologicsbloodvaccines/guidancecomplianceregulatoryinformation/post-marketactivities/lotreleases/ucm202750.htm; 2010.
    • (2010) Blood & Biologics


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.