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Volumn 102, Issue 2, 2013, Pages 454-461

Rapid deamidation of recombinant protective antigen when adsorbed on aluminum hydroxide gel correlates with reduced potency of vaccine

Author keywords

Biotechnology; Chemical stability; Deamidation; Formulation; Protein; Vaccines

Indexed keywords

ALUMINUM HYDROXIDE; ANTHRAX VACCINE; RECOMBINANT ANTIGEN; RECOMBINANT PROTECTIVE ANTIGEN; UNCLASSIFIED DRUG;

EID: 84872497981     PISSN: 00223549     EISSN: 15206017     Source Type: Journal    
DOI: 10.1002/jps.23422     Document Type: Article
Times cited : (31)

References (29)
  • 2
    • 12344260644 scopus 로고    scopus 로고
    • Center for Disease Control and Prevention. Atlanta, Georgia: Center for Disease Control and Prevention.
    • Center for Disease Control and Prevention. 2011. Bioterrorism agents/diseases. Atlanta, Georgia: Center for Disease Control and Prevention.
    • (2011) Bioterrorism agents/diseases
  • 4
    • 84872497853 scopus 로고    scopus 로고
    • Anthrax countermeasures better than in 2001, but work remains
    • Minneapolis, Minnesota: Center for Infectious Diseases Research and Policy (CIDRP).
    • Roos R. 2011. Anthrax countermeasures better than in 2001, but work remains. Center for Infectious Diseases Research and Policy (CIDRP) News. Minneapolis, Minnesota: Center for Infectious Diseases Research and Policy (CIDRP).
    • (2011) Center for Infectious Diseases Research and Policy (CIDRP) News
    • Roos, R.1
  • 6
    • 33344473535 scopus 로고    scopus 로고
    • Duration of protection of rabbits after vaccination with Bacillus anthracis recombinant protective antigen vaccine
    • Little SF, Ivins BE, Webster WM, Fellows PF, Pitt ML, Norris SL, Andrews GP. 2006. Duration of protection of rabbits after vaccination with Bacillus anthracis recombinant protective antigen vaccine. Vaccine 24(14):2530-2536.
    • (2006) Vaccine , vol.24 , Issue.14 , pp. 2530-2536
    • Little, S.F.1    Ivins, B.E.2    Webster, W.M.3    Fellows, P.F.4    Pitt, M.L.5    Norris, S.L.6    Andrews, G.P.7
  • 10
    • 0023895994 scopus 로고
    • Production and characterization of monoclonal antibodies to the protective antigen component of Bacillus anthracis toxin
    • Little SF, Leppla SH, Cora E. 1988. Production and characterization of monoclonal antibodies to the protective antigen component of Bacillus anthracis toxin. Infect Immun 56(7):1807-1813.
    • (1988) Infect Immun , vol.56 , Issue.7 , pp. 1807-1813
    • Little, S.F.1    Leppla, S.H.2    Cora, E.3
  • 11
    • 85046915570 scopus 로고    scopus 로고
    • Is new always better than old? The development of human vaccines for anthrax
    • Baillie LW. 2009. Is new always better than old? The development of human vaccines for anthrax. Hum Vaccin 5(12):806-816.
    • (2009) Hum Vaccin , vol.5 , Issue.12 , pp. 806-816
    • Baillie, L.W.1
  • 12
    • 33746058634 scopus 로고    scopus 로고
    • Immunogenicity and tolerance of ascending doses of a recombinant protective antigen (rPA102) anthrax vaccine: A randomized, double-blinded, controlled, multicenter trial
    • Gorse GJ, Keitel W, Keyserling H, Taylor DN, Lock M, Alves K, Kenner J, Deans L, Gurwith M. 2006. Immunogenicity and tolerance of ascending doses of a recombinant protective antigen (rPA102) anthrax vaccine: A randomized, double-blinded, controlled, multicenter trial. Vaccine 24(33-34):5950-5959.
    • (2006) Vaccine , vol.24 , Issue.33-34 , pp. 5950-5959
    • Gorse, G.J.1    Keitel, W.2    Keyserling, H.3    Taylor, D.N.4    Lock, M.5    Alves, K.6    Kenner, J.7    Deans, L.8    Gurwith, M.9
  • 13
    • 84865988677 scopus 로고    scopus 로고
    • Structural and immunological analysis of anthrax recombinant protective antigen adsorbed to aluminum hydroxide adjuvant
    • Wagner L, Verma A, Meade BD, Reiter K, Narum DL, Brady RA, Little SF, Burns DL. 2012. Structural and immunological analysis of anthrax recombinant protective antigen adsorbed to aluminum hydroxide adjuvant. Clin Vaccin Immunol 19(9):1465-1473.
    • (2012) Clin Vaccin Immunol , vol.19 , Issue.9 , pp. 1465-1473
    • Wagner, L.1    Verma, A.2    Meade, B.D.3    Reiter, K.4    Narum, D.L.5    Brady, R.A.6    Little, S.F.7    Burns, D.L.8
  • 14
    • 83955164227 scopus 로고    scopus 로고
    • Anthrax sub-unit vaccine: The structural consequences of binding rPA83 to Alhydrogel(R)
    • Soliakov A, Kelly IF, Lakey JH, Watkinson A. 2012. Anthrax sub-unit vaccine: The structural consequences of binding rPA83 to Alhydrogel(R). Eur J Pharm Biopharm 80(1):25-32.
    • (2012) Eur J Pharm Biopharm , vol.80 , Issue.1 , pp. 25-32
    • Soliakov, A.1    Kelly, I.F.2    Lakey, J.H.3    Watkinson, A.4
  • 15
    • 84866356164 scopus 로고    scopus 로고
    • Comparison of the structural stability and dynamic properties of recombinant anthrax protective antigen and its 2-fluorohistidine-labeled analogue
    • Hu L, Joshi SB, Andra KK, Thakkar SV, Volkin DB, Bann JG, Middaugh CR. 2012. Comparison of the structural stability and dynamic properties of recombinant anthrax protective antigen and its 2-fluorohistidine-labeled analogue. J Pharm Sci 101(11):4118-4128.
    • (2012) J Pharm Sci , vol.101 , Issue.11 , pp. 4118-4128
    • Hu, L.1    Joshi, S.B.2    Andra, K.K.3    Thakkar, S.V.4    Volkin, D.B.5    Bann, J.G.6    Middaugh, C.R.7
  • 16
    • 84870501377 scopus 로고    scopus 로고
    • Biophysical characterisation of thermal-induced precipitates of recombinant anthrax protective antigen: Evidence for kinetically trapped unfolding domains in solid-state
    • Ganesan A, Watkinson A, Moore BD. 2012. Biophysical characterisation of thermal-induced precipitates of recombinant anthrax protective antigen: Evidence for kinetically trapped unfolding domains in solid-state. Eur J Pharm Biopharm 82(3):475-484.
    • (2012) Eur J Pharm Biopharm , vol.82 , Issue.3 , pp. 475-484
    • Ganesan, A.1    Watkinson, A.2    Moore, B.D.3
  • 17
    • 34250796766 scopus 로고    scopus 로고
    • Multiple asparagine deamidation of Bacillus anthracis protective antigen causes charge isoforms whose complexity correlates with reduced biological activity
    • Powell BS, Enama JT, Ribot WJ, Webster W, Little S, Hoover T, Adamovicz JJ, Andrews GP. 2007. Multiple asparagine deamidation of Bacillus anthracis protective antigen causes charge isoforms whose complexity correlates with reduced biological activity. Proteins 68(2):458-479.
    • (2007) Proteins , vol.68 , Issue.2 , pp. 458-479
    • Powell, B.S.1    Enama, J.T.2    Ribot, W.J.3    Webster, W.4    Little, S.5    Hoover, T.6    Adamovicz, J.J.7    Andrews, G.P.8
  • 20
    • 0032904703 scopus 로고    scopus 로고
    • Secondary structure and protein deamidation
    • Xie M, Schowen RL. 1999. Secondary structure and protein deamidation. J Pharm Sci 88(1):8-13.
    • (1999) J Pharm Sci , vol.88 , Issue.1 , pp. 8-13
    • Xie, M.1    Schowen, R.L.2
  • 21
    • 1542270987 scopus 로고    scopus 로고
    • Effect of microenvironment pH of aluminum hydroxide adjuvant on the chemical stability of adsorbed antigen
    • Wittayanukulluk A, Jiang D, Regnier FE, Hem SL. 2004. Effect of microenvironment pH of aluminum hydroxide adjuvant on the chemical stability of adsorbed antigen. Vaccine 22(9-10):1172-1176.
    • (2004) Vaccine , vol.22 , Issue.9-10 , pp. 1172-1176
    • Wittayanukulluk, A.1    Jiang, D.2    Regnier, F.E.3    Hem, S.L.4
  • 23
    • 29644440248 scopus 로고    scopus 로고
    • Immunological correlates for protection against intranasal challenge of Bacillus anthracis spores conferred by a protective antigen-based vaccine in rabbits
    • Weiss S, Kobiler D, Levy H, Marcus H, Pass A, Rothschild N, Altboum Z. 2006. Immunological correlates for protection against intranasal challenge of Bacillus anthracis spores conferred by a protective antigen-based vaccine in rabbits. Infect Immun 74(1):394-398.
    • (2006) Infect Immun , vol.74 , Issue.1 , pp. 394-398
    • Weiss, S.1    Kobiler, D.2    Levy, H.3    Marcus, H.4    Pass, A.5    Rothschild, N.6    Altboum, Z.7
  • 24
    • 0037205534 scopus 로고    scopus 로고
    • New drug and biological drug products; evidence needed to demonstrate effectiveness of new drugs when human efficacy studies are not ethical or feasible. Final rule
    • Food and Drug Administration, HHS. ():-.
    • Food and Drug Administration, HHS. 2002. New drug and biological drug products; evidence needed to demonstrate effectiveness of new drugs when human efficacy studies are not ethical or feasible. Final rule. Fed Regist 67(105):37988-37998.
    • (2002) Fed Regist , vol.67 , Issue.105 , pp. 37988-37998
  • 25
    • 0025858389 scopus 로고
    • The carboxyl-terminal end of protective antigen is required for receptor binding and anthrax toxin activity
    • Singh Y, Klimpel KR, Quinn CP, Chaudhary VK, Leppla SH. 1991. The carboxyl-terminal end of protective antigen is required for receptor binding and anthrax toxin activity. J Biol Chem 266(23):15493-15497.
    • (1991) J Biol Chem , vol.266 , Issue.23 , pp. 15493-15497
    • Singh, Y.1    Klimpel, K.R.2    Quinn, C.P.3    Chaudhary, V.K.4    Leppla, S.H.5
  • 26
    • 28844507784 scopus 로고    scopus 로고
    • Effects of spontaneous deamidation on the cytotoxic activity of the Bacillus anthracis protective antigen
    • Zomber G, Reuveny S, Garti N, Shafferman A, Elhanany E. 2005. Effects of spontaneous deamidation on the cytotoxic activity of the Bacillus anthracis protective antigen. J Biol Chem 280(48):39897-39906.
    • (2005) J Biol Chem , vol.280 , Issue.48 , pp. 39897-39906
    • Zomber, G.1    Reuveny, S.2    Garti, N.3    Shafferman, A.4    Elhanany, E.5
  • 27
    • 0029958827 scopus 로고    scopus 로고
    • Characterization of lethal factor binding and cell receptor binding domains of protective antigen of Bacillus anthracis using monoclonal antibodies
    • Little SF, Novak JM, Lowe JR, Leppla SH, Singh Y, Klimpel KR, Lidgerding BC, Friedlander AM. 1996. Characterization of lethal factor binding and cell receptor binding domains of protective antigen of Bacillus anthracis using monoclonal antibodies. Microbiology 142(Pt 3):707-715.
    • (1996) Microbiology , vol.142 , Issue.PART 3 , pp. 707-715
    • Little, S.F.1    Novak, J.M.2    Lowe, J.R.3    Leppla, S.H.4    Singh, Y.5    Klimpel, K.R.6    Lidgerding, B.C.7    Friedlander, A.M.8
  • 28
    • 37349109629 scopus 로고    scopus 로고
    • Modeling the structure of mAb 14B7 bound to the anthrax protective antigen
    • Sivasubramanian A, Maynard JA, Gray JJ. 2008. Modeling the structure of mAb 14B7 bound to the anthrax protective antigen. Proteins 70(1):218-230.
    • (2008) Proteins , vol.70 , Issue.1 , pp. 218-230
    • Sivasubramanian, A.1    Maynard, J.A.2    Gray, J.J.3
  • 29
    • 70350463878 scopus 로고    scopus 로고
    • Neutralizing monoclonal antibodies directed against defined linear epitopes on domain 4 of anthrax protective antigen
    • Kelly-Cirino CD, Mantis NJ. 2009. Neutralizing monoclonal antibodies directed against defined linear epitopes on domain 4 of anthrax protective antigen. Infect Immun 77(11):4859-4867.
    • (2009) Infect Immun , vol.77 , Issue.11 , pp. 4859-4867
    • Kelly-Cirino, C.D.1    Mantis, N.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.