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Volumn 9, Issue 7, 2013, Pages

Mutated and Bacteriophage T4 Nanoparticle Arrayed F1-V Immunogens from Yersinia pestis as Next Generation Plague Vaccines

Author keywords

[No Author keywords available]

Indexed keywords

CAPSULAR PROTEIN F1; EPITOPE; GAMMA INTERFERON; HYBRID PROTEIN; IMMUNOGLOBULIN G; INTERLEUKIN 10; LOW CALCIUM RESPONSE V ANTIGEN; NANOPARTICLE; PLAGUE VACCINE; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG;

EID: 84884751020     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1003495     Document Type: Article
Times cited : (57)

References (65)
  • 1
    • 0031029062 scopus 로고    scopus 로고
    • Yersinia pestis-etiologic agent of plague
    • Perry RD, Fetherston JD, (1997) Yersinia pestis-etiologic agent of plague. Clin Microbiol Rev 10: 35-66.
    • (1997) Clin Microbiol Rev , vol.10 , pp. 35-66
    • Perry, R.D.1    Fetherston, J.D.2
  • 2
    • 16844371347 scopus 로고    scopus 로고
    • Risk of person-to-person transmission of pneumonic plague
    • Kool JL, (2005) Risk of person-to-person transmission of pneumonic plague. Clin Infect Dis 40: 1166-1172.
    • (2005) Clin Infect Dis , vol.40 , pp. 1166-1172
    • Kool, J.L.1
  • 4
    • 0034600229 scopus 로고    scopus 로고
    • Plague as a biological weapon: medical and public health management. Working Group on Civilian Biodefense
    • Inglesby TV, Dennis DT, Henderson DA, Bartlett JG, Ascher MS, et al. (2000) Plague as a biological weapon: medical and public health management. Working Group on Civilian Biodefense. JAMA 283: 2281-2290.
    • (2000) JAMA , vol.283 , pp. 2281-2290
    • Inglesby, T.V.1    Dennis, D.T.2    Henderson, D.A.3    Bartlett, J.G.4    Ascher, M.S.5
  • 5
    • 33644782630 scopus 로고    scopus 로고
    • The anti-plague system and the Soviet biological warfare program
    • Zilinskas RA, (2006) The anti-plague system and the Soviet biological warfare program. Crit Rev Microbiol 32: 47-64.
    • (2006) Crit Rev Microbiol , vol.32 , pp. 47-64
    • Zilinskas, R.A.1
  • 6
    • 40549101035 scopus 로고    scopus 로고
    • Current challenges in the development of vaccines for pneumonic plague
    • Smiley ST, (2008) Current challenges in the development of vaccines for pneumonic plague. Expert Rev Vaccines 7: 209-221.
    • (2008) Expert Rev Vaccines , vol.7 , pp. 209-221
    • Smiley, S.T.1
  • 7
    • 84874669741 scopus 로고    scopus 로고
    • Deletion of Braun lipoprotein encoding gene and altering the function of lipopolysaccharide attenuate plague bacterium
    • Sha J, Kirtley ML, van Lier CJ, Wang S, Erova TE, et al. (2013) Deletion of Braun lipoprotein encoding gene and altering the function of lipopolysaccharide attenuate plague bacterium. Infect Immun 81 (3) (): 815-28.
    • (2013) Infect Immun , vol.81 , Issue.3 , pp. 815-828
    • Sha, J.1    Kirtley, M.L.2    van Lier, C.J.3    Wang, S.4    Erova, T.E.5
  • 9
    • 84862699865 scopus 로고    scopus 로고
    • The natural history and incidence of Yersinia pestis and prospects for vaccination
    • Williamson ED, Oyston PC, (2012) The natural history and incidence of Yersinia pestis and prospects for vaccination. J Med Microbiol 61: 911-918.
    • (2012) J Med Microbiol , vol.61 , pp. 911-918
    • Williamson, E.D.1    Oyston, P.C.2
  • 10
    • 0038820383 scopus 로고    scopus 로고
    • Structure and biogenesis of the capsular F1 antigen from Yersinia pestis: preserved folding energy drives fiber formation
    • Zavialov AV, Berglund J, Pudney AF, Fooks LJ, Ibrahim TM, et al. (2003) Structure and biogenesis of the capsular F1 antigen from Yersinia pestis: preserved folding energy drives fiber formation. Cell 113: 587-596.
    • (2003) Cell , vol.113 , pp. 587-596
    • Zavialov, A.V.1    Berglund, J.2    Pudney, A.F.3    Fooks, L.J.4    Ibrahim, T.M.5
  • 12
    • 1242328668 scopus 로고    scopus 로고
    • The structure of Yersinia pestis V-antigen, an essential virulence factor and mediator of immunity against plague
    • Derewenda U, Mateja A, Devedjiev Y, Routzahn KM, Evdokimov AG, et al. (2004) The structure of Yersinia pestis V-antigen, an essential virulence factor and mediator of immunity against plague. Structure 12: 301-306.
    • (2004) Structure , vol.12 , pp. 301-306
    • Derewenda, U.1    Mateja, A.2    Devedjiev, Y.3    Routzahn, K.M.4    Evdokimov, A.G.5
  • 13
    • 0037973623 scopus 로고    scopus 로고
    • Interleukin-10 and inhibition of innate immunity to Yersiniae: roles of Yops and LcrV (V antigen)
    • Brubaker RR, (2003) Interleukin-10 and inhibition of innate immunity to Yersiniae: roles of Yops and LcrV (V antigen). Infect Immun 71: 3673-3681.
    • (2003) Infect Immun , vol.71 , pp. 3673-3681
    • Brubaker, R.R.1
  • 16
    • 0031750789 scopus 로고    scopus 로고
    • Protection against experimental bubonic and pneumonic plague by a recombinant capsular F1-V antigen fusion protein vaccine
    • Heath DG, Anderson GW Jr, Mauro JM, Welkos SL, Andrews GP, et al. (1998) Protection against experimental bubonic and pneumonic plague by a recombinant capsular F1-V antigen fusion protein vaccine. Vaccine 16: 1131-1137.
    • (1998) Vaccine , vol.16 , pp. 1131-1137
    • Heath, D.G.1    Anderson Jr., G.W.2    Mauro, J.M.3    Welkos, S.L.4    Andrews, G.P.5
  • 17
    • 77957748020 scopus 로고    scopus 로고
    • Plague
    • Williamson ED, (2009) Plague. Vaccine 27 Suppl 4: D56-60.
    • (2009) Vaccine , vol.27 , Issue.SUPPL.
    • Williamson, E.D.1
  • 18
    • 21144478755 scopus 로고    scopus 로고
    • Human immune response to a plague vaccine comprising recombinant F1 and V antigens
    • Williamson ED, Flick-Smith HC, Lebutt C, Rowland CA, Jones SM, et al. (2005) Human immune response to a plague vaccine comprising recombinant F1 and V antigens. Infect Immun 73: 3598-3608.
    • (2005) Infect Immun , vol.73 , pp. 3598-3608
    • Williamson, E.D.1    Flick-Smith, H.C.2    Lebutt, C.3    Rowland, C.A.4    Jones, S.M.5
  • 19
    • 58149392737 scopus 로고    scopus 로고
    • Flagellin-F1-V fusion protein is an effective plague vaccine in mice and two species of nonhuman primates
    • Mizel SB, Graff AH, Sriranganathan N, Ervin S, Lees CJ, et al. (2009) Flagellin-F1-V fusion protein is an effective plague vaccine in mice and two species of nonhuman primates. Clin Vaccine Immunol 16: 21-28.
    • (2009) Clin Vaccine Immunol , vol.16 , pp. 21-28
    • Mizel, S.B.1    Graff, A.H.2    Sriranganathan, N.3    Ervin, S.4    Lees, C.J.5
  • 20
    • 33847156757 scopus 로고    scopus 로고
    • Purification and protective efficacy of monomeric and modified Yersinia pestis capsular F1-V antigen fusion proteins for vaccination against plague
    • Goodin JL, Nellis DF, Powell BS, Vyas VV, Enama JT, et al. (2007) Purification and protective efficacy of monomeric and modified Yersinia pestis capsular F1-V antigen fusion proteins for vaccination against plague. Protein Expr Purif 53: 63-79.
    • (2007) Protein Expr Purif , vol.53 , pp. 63-79
    • Goodin, J.L.1    Nellis, D.F.2    Powell, B.S.3    Vyas, V.V.4    Enama, J.T.5
  • 21
    • 78650171693 scopus 로고    scopus 로고
    • Purification and characterization of a recombinant Yersinia pestis V-F1 "Reversed" fusion protein for use as a new subunit vaccine against plague
    • Goodin JL, Powell BS, Enama JT, Raab RW, McKown RL, et al. (2011) Purification and characterization of a recombinant Yersinia pestis V-F1 "Reversed" fusion protein for use as a new subunit vaccine against plague. Protein Expr Purif 76: 136-144.
    • (2011) Protein Expr Purif , vol.76 , pp. 136-144
    • Goodin, J.L.1    Powell, B.S.2    Enama, J.T.3    Raab, R.W.4    McKown, R.L.5
  • 22
    • 26644448730 scopus 로고    scopus 로고
    • Design and testing for a nontagged F1-V fusion protein as vaccine antigen against bubonic and pneumonic plague
    • Powell BS, Andrews GP, Enama JT, Jendrek S, Bolt C, et al. (2005) Design and testing for a nontagged F1-V fusion protein as vaccine antigen against bubonic and pneumonic plague. Biotechnol Prog 21: 1490-1510.
    • (2005) Biotechnol Prog , vol.21 , pp. 1490-1510
    • Powell, B.S.1    Andrews, G.P.2    Enama, J.T.3    Jendrek, S.4    Bolt, C.5
  • 24
    • 0028849883 scopus 로고
    • Relationship between virulence and immunity as revealed in recent studies of the F1 capsule of Yersinia pestis
    • Friedlander AM, Welkos SL, Worsham PL, Andrews GP, Heath DG, et al. (1995) Relationship between virulence and immunity as revealed in recent studies of the F1 capsule of Yersinia pestis. Clin Infect Dis 21 Suppl 2: S178-181.
    • (1995) Clin Infect Dis , vol.21 , Issue.SUPPL.
    • Friedlander, A.M.1    Welkos, S.L.2    Worsham, P.L.3    Andrews, G.P.4    Heath, D.G.5
  • 25
    • 0029420939 scopus 로고
    • Construction of defined F1 negative mutants of virulent Yersinia pestis
    • Worsham PL, Stein MP, Welkos SL, (1995) Construction of defined F1 negative mutants of virulent Yersinia pestis. Contrib Microbiol Immunol 13: 325-328.
    • (1995) Contrib Microbiol Immunol , vol.13 , pp. 325-328
    • Worsham, P.L.1    Stein, M.P.2    Welkos, S.L.3
  • 26
    • 0031018415 scopus 로고    scopus 로고
    • Passive immunity to infection with Yersinia spp. mediated by anti-recombinant V antigen is dependent on polymorphism of V antigen
    • Roggenkamp A, Geiger AM, Leitritz L, Kessler A, Heesemann J, (1997) Passive immunity to infection with Yersinia spp. mediated by anti-recombinant V antigen is dependent on polymorphism of V antigen. Infect Immun 65: 446-451.
    • (1997) Infect Immun , vol.65 , pp. 446-451
    • Roggenkamp, A.1    Geiger, A.M.2    Leitritz, L.3    Kessler, A.4    Heesemann, J.5
  • 27
    • 84874837967 scopus 로고    scopus 로고
    • Evaluation of protective potential of Yersinia pestis outer membrane protein antigens as possible candidates for a new generation recombinant plague vaccine
    • Erova TE, Rosenzweig JA, Sha J, Suarez G, Sierra JC, et al. (2013) Evaluation of protective potential of Yersinia pestis outer membrane protein antigens as possible candidates for a new generation recombinant plague vaccine. Clin Vaccine Immunol 20: 227-238.
    • (2013) Clin Vaccine Immunol , vol.20 , pp. 227-238
    • Erova, T.E.1    Rosenzweig, J.A.2    Sha, J.3    Suarez, G.4    Sierra, J.C.5
  • 28
    • 33746612813 scopus 로고    scopus 로고
    • Immunogenicity and protective immunity against bubonic plague and pneumonic plague by immunization of mice with the recombinant V10 antigen, a variant of LcrV
    • DeBord KL, Anderson DM, Marketon MM, Overheim KA, DePaolo RW, et al. (2006) Immunogenicity and protective immunity against bubonic plague and pneumonic plague by immunization of mice with the recombinant V10 antigen, a variant of LcrV. Infect Immun 74: 4910-4914.
    • (2006) Infect Immun , vol.74 , pp. 4910-4914
    • DeBord, K.L.1    Anderson, D.M.2    Marketon, M.M.3    Overheim, K.A.4    DePaolo, R.W.5
  • 29
    • 33748920016 scopus 로고    scopus 로고
    • Bacteriophage T4 capsid: a unique platform for efficient surface assembly of macromolecular complexes
    • Li Q, Shivachandra SB, Leppla SH, Rao VB, (2006) Bacteriophage T4 capsid: a unique platform for efficient surface assembly of macromolecular complexes. J Mol Biol 363: 577-588.
    • (2006) J Mol Biol , vol.363 , pp. 577-588
    • Li, Q.1    Shivachandra, S.B.2    Leppla, S.H.3    Rao, V.B.4
  • 30
    • 34250211126 scopus 로고    scopus 로고
    • Assembly of the small outer capsid protein, Soc, on bacteriophage T4: a novel system for high density display of multiple large anthrax toxins and foreign proteins on phage capsid
    • Li Q, Shivachandra SB, Zhang Z, Rao VB, (2007) Assembly of the small outer capsid protein, Soc, on bacteriophage T4: a novel system for high density display of multiple large anthrax toxins and foreign proteins on phage capsid. J Mol Biol 370: 1006-1019.
    • (2007) J Mol Biol , vol.370 , pp. 1006-1019
    • Li, Q.1    Shivachandra, S.B.2    Zhang, Z.3    Rao, V.B.4
  • 31
    • 33845940672 scopus 로고    scopus 로고
    • Multicomponent anthrax toxin display and delivery using bacteriophage T4
    • Shivachandra SB, Li Q, Peachman KK, Matyas GR, Leppla SH, et al. (2007) Multicomponent anthrax toxin display and delivery using bacteriophage T4. Vaccine 25: 1225-1235.
    • (2007) Vaccine , vol.25 , pp. 1225-1235
    • Shivachandra, S.B.1    Li, Q.2    Peachman, K.K.3    Matyas, G.R.4    Leppla, S.H.5
  • 32
    • 33746190697 scopus 로고    scopus 로고
    • Assembly of human immunodeficiency virus (HIV) antigens on bacteriophage T4: a novel in vitro approach to construct multicomponent HIV vaccines
    • Sathaliyawala T, Rao M, Maclean DM, Birx DL, Alving CR, et al. (2006) Assembly of human immunodeficiency virus (HIV) antigens on bacteriophage T4: a novel in vitro approach to construct multicomponent HIV vaccines. J Virol 80: 7688-7698.
    • (2006) J Virol , vol.80 , pp. 7688-7698
    • Sathaliyawala, T.1    Rao, M.2    Maclean, D.M.3    Birx, D.L.4    Alving, C.R.5
  • 33
    • 84858226068 scopus 로고    scopus 로고
    • Structure, assembly, and DNA packaging of the bacteriophage T4 head
    • Black LW, Rao VB, (2012) Structure, assembly, and DNA packaging of the bacteriophage T4 head. Adv Virus Res 82: 119-153.
    • (2012) Adv Virus Res , vol.82 , pp. 119-153
    • Black, L.W.1    Rao, V.B.2
  • 34
    • 73649087232 scopus 로고    scopus 로고
    • Structure of the small outer capsid protein, Soc: a clamp for stabilizing capsids of T4-like phages
    • Qin L, Fokine A, O'Donnell E, Rao VB, Rossmann MG, (2009) Structure of the small outer capsid protein, Soc: a clamp for stabilizing capsids of T4-like phages. J Mol Biol 395: 728-741.
    • (2009) J Mol Biol , vol.395 , pp. 728-741
    • Qin, L.1    Fokine, A.2    O'Donnell, E.3    Rao, V.B.4    Rossmann, M.G.5
  • 35
    • 79961196704 scopus 로고    scopus 로고
    • Structure of the three N-terminal immunoglobulin domains of the highly immunogenic outer capsid protein from a T4-like bacteriophage
    • Fokine A, Islam MZ, Zhang Z, Bowman VD, Rao VB, et al. (2011) Structure of the three N-terminal immunoglobulin domains of the highly immunogenic outer capsid protein from a T4-like bacteriophage. J Virol 85: 8141-8148.
    • (2011) J Virol , vol.85 , pp. 8141-8148
    • Fokine, A.1    Islam, M.Z.2    Zhang, Z.3    Bowman, V.D.4    Rao, V.B.5
  • 36
    • 77954368167 scopus 로고    scopus 로고
    • Functional analysis of the highly antigenic outer capsid protein, Hoc, a virus decoration protein from T4-like bacteriophages
    • Sathaliyawala T, Islam MZ, Li Q, Fokine A, Rossmann MG, et al. (2010) Functional analysis of the highly antigenic outer capsid protein, Hoc, a virus decoration protein from T4-like bacteriophages. Mol Microbiol 77: 444-455.
    • (2010) Mol Microbiol , vol.77 , pp. 444-455
    • Sathaliyawala, T.1    Islam, M.Z.2    Li, Q.3    Fokine, A.4    Rossmann, M.G.5
  • 37
    • 0017597092 scopus 로고
    • The two dispensable structural proteins (soc and hoc) of the T4 phage capsid; their purification and properties, isolation and characterization of the defective mutants, and their binding with the defective heads in vitro
    • Ishii T, Yanagida M, (1977) The two dispensable structural proteins (soc and hoc) of the T4 phage capsid; their purification and properties, isolation and characterization of the defective mutants, and their binding with the defective heads in vitro. J Mol Biol 109: 487-514.
    • (1977) J Mol Biol , vol.109 , pp. 487-514
    • Ishii, T.1    Yanagida, M.2
  • 38
    • 0029993925 scopus 로고    scopus 로고
    • Fraction 1 capsular antigen (F1) purification from Yersinia pestis CO92 and from an Escherichia coli recombinant strain and efficacy against lethal plague challenge
    • Andrews GP, Heath DG, Anderson GW Jr, Welkos SL, Friedlander AM, (1996) Fraction 1 capsular antigen (F1) purification from Yersinia pestis CO92 and from an Escherichia coli recombinant strain and efficacy against lethal plague challenge. Infect Immun 64: 2180-2187.
    • (1996) Infect Immun , vol.64 , pp. 2180-2187
    • Andrews, G.P.1    Heath, D.G.2    Anderson Jr., G.W.3    Welkos, S.L.4    Friedlander, A.M.5
  • 39
    • 0031849316 scopus 로고    scopus 로고
    • Macromolecular organisation of recombinant Yersinia pestis F1 antigen and the effect of structure on immunogenicity
    • Miller J, Williamson ED, Lakey JH, Pearce MJ, Jones SM, et al. (1998) Macromolecular organisation of recombinant Yersinia pestis F1 antigen and the effect of structure on immunogenicity. FEMS Immunol Med Microbiol 21: 213-221.
    • (1998) FEMS Immunol Med Microbiol , vol.21 , pp. 213-221
    • Miller, J.1    Williamson, E.D.2    Lakey, J.H.3    Pearce, M.J.4    Jones, S.M.5
  • 40
    • 33748752883 scopus 로고    scopus 로고
    • Sequential proteolytic processing of the capsular Caf1 antigen of Yersinia pestis for major histocompatibility complex class II-restricted presentation to T lymphocytes
    • Musson JA, Morton M, Walker N, Harper HM, McNeill HV, et al. (2006) Sequential proteolytic processing of the capsular Caf1 antigen of Yersinia pestis for major histocompatibility complex class II-restricted presentation to T lymphocytes. J Biol Chem 281: 26129-26135.
    • (2006) J Biol Chem , vol.281 , pp. 26129-26135
    • Musson, J.A.1    Morton, M.2    Walker, N.3    Harper, H.M.4    McNeill, H.V.5
  • 42
    • 23244442054 scopus 로고    scopus 로고
    • Immunization of mice with YscF provides protection from Yersinia pestis infections
    • Matson JS, Durick KA, Bradley DS, Nilles ML, (2005) Immunization of mice with YscF provides protection from Yersinia pestis infections. BMC Microbiol 5: 38.
    • (2005) BMC Microbiol , vol.5 , pp. 38
    • Matson, J.S.1    Durick, K.A.2    Bradley, D.S.3    Nilles, M.L.4
  • 43
    • 33845938871 scopus 로고    scopus 로고
    • Mutations in the Yersinia pseudotuberculosis type III secretion system needle protein, YscF, that specifically abrogate effector translocation into host cells
    • Davis AJ, Mecsas J, (2007) Mutations in the Yersinia pseudotuberculosis type III secretion system needle protein, YscF, that specifically abrogate effector translocation into host cells. J Bacteriol 189: 83-97.
    • (2007) J Bacteriol , vol.189 , pp. 83-97
    • Davis, A.J.1    Mecsas, J.2
  • 44
    • 85046915477 scopus 로고    scopus 로고
    • Plague vaccines and the molecular basis of immunity against Yersinia pestis
    • Quenee LE, Schneewind O, (2009) Plague vaccines and the molecular basis of immunity against Yersinia pestis. Hum Vaccin 5: 817-823.
    • (2009) Hum Vaccin , vol.5 , pp. 817-823
    • Quenee, L.E.1    Schneewind, O.2
  • 45
    • 52049114659 scopus 로고    scopus 로고
    • Immune defense against pneumonic plague
    • Smiley ST, (2008) Immune defense against pneumonic plague. Immunol Rev 225: 256-271.
    • (2008) Immunol Rev , vol.225 , pp. 256-271
    • Smiley, S.T.1
  • 46
    • 38349052185 scopus 로고    scopus 로고
    • Broad T cell immunity to the LcrV virulence protein is induced by targeted delivery to DEC-205/CD205-positive mouse dendritic cells
    • Do Y, Park CG, Kang YS, Park SH, Lynch RM, et al. (2008) Broad T cell immunity to the LcrV virulence protein is induced by targeted delivery to DEC-205/CD205-positive mouse dendritic cells. Eur J Immunol 38: 20-29.
    • (2008) Eur J Immunol , vol.38 , pp. 20-29
    • Do, Y.1    Park, C.G.2    Kang, Y.S.3    Park, S.H.4    Lynch, R.M.5
  • 47
    • 61449193110 scopus 로고    scopus 로고
    • Characterization of the rat pneumonic plague model: infection kinetics following aerosolization of Yersinia pestis CO92
    • Agar SL, Sha J, Foltz SM, Erova TE, Walberg KG, et al. (2009) Characterization of the rat pneumonic plague model: infection kinetics following aerosolization of Yersinia pestis CO92. Microbes Infect 11: 205-214.
    • (2009) Microbes Infect , vol.11 , pp. 205-214
    • Agar, S.L.1    Sha, J.2    Foltz, S.M.3    Erova, T.E.4    Walberg, K.G.5
  • 48
    • 33845475425 scopus 로고    scopus 로고
    • Immunogenicity of a Yersinia pestis vaccine antigen monomerized by circular permutation
    • Chalton DA, Musson JA, Flick-Smith H, Walker N, McGregor A, et al. (2006) Immunogenicity of a Yersinia pestis vaccine antigen monomerized by circular permutation. Infect Immun 74: 6624-6631.
    • (2006) Infect Immun , vol.74 , pp. 6624-6631
    • Chalton, D.A.1    Musson, J.A.2    Flick-Smith, H.3    Walker, N.4    McGregor, A.5
  • 49
    • 0037152173 scopus 로고    scopus 로고
    • Yersinia V-antigen exploits toll-like receptor 2 and CD14 for interleukin 10-mediated immunosuppression
    • Sing A, Rost D, Tvardovskaia N, Roggenkamp A, Wiedemann A, et al. (2002) Yersinia V-antigen exploits toll-like receptor 2 and CD14 for interleukin 10-mediated immunosuppression. J Exp Med 196: 1017-1024.
    • (2002) J Exp Med , vol.196 , pp. 1017-1024
    • Sing, A.1    Rost, D.2    Tvardovskaia, N.3    Roggenkamp, A.4    Wiedemann, A.5
  • 50
    • 22044451242 scopus 로고    scopus 로고
    • Yersinia rLcrV and rYopB inhibits the activation of murine peritoneal macrophages in vitro
    • Sodhi A, Sharma RK, Batra HV, (2005) Yersinia rLcrV and rYopB inhibits the activation of murine peritoneal macrophages in vitro. Immunol Lett 99: 146-152.
    • (2005) Immunol Lett , vol.99 , pp. 146-152
    • Sodhi, A.1    Sharma, R.K.2    Batra, H.V.3
  • 51
    • 78649692246 scopus 로고    scopus 로고
    • TNFalpha and IFNgamma contribute to F1/LcrV-targeted immune defense in mouse models of fully virulent pneumonic plague
    • Lin JS, Park S, Adamovicz JJ, Hill J, Bliska JB, et al. (2010) TNFalpha and IFNgamma contribute to F1/LcrV-targeted immune defense in mouse models of fully virulent pneumonic plague. Vaccine 29: 357-362.
    • (2010) Vaccine , vol.29 , pp. 357-362
    • Lin, J.S.1    Park, S.2    Adamovicz, J.J.3    Hill, J.4    Bliska, J.B.5
  • 52
    • 0037152192 scopus 로고    scopus 로고
    • A plague on host defense
    • Kopp E, Medzhitov R, (2002) A plague on host defense. J Exp Med 196: 1009-1012.
    • (2002) J Exp Med , vol.196 , pp. 1009-1012
    • Kopp, E.1    Medzhitov, R.2
  • 53
    • 79960553230 scopus 로고    scopus 로고
    • Involvement of CD8+ T cell-mediated immune responses in LcrV DNA vaccine induced protection against lethal Yersinia pestis challenge
    • Wang S, Goguen JD, Li F, Lu S, (2011) Involvement of CD8+ T cell-mediated immune responses in LcrV DNA vaccine induced protection against lethal Yersinia pestis challenge. Vaccine 29: 6802-6809.
    • (2011) Vaccine , vol.29 , pp. 6802-6809
    • Wang, S.1    Goguen, J.D.2    Li, F.3    Lu, S.4
  • 54
    • 33846786590 scopus 로고    scopus 로고
    • Vaccination with live Yersinia pestis primes CD4 and CD8 T cells that synergistically protect against lethal pulmonary Y. pestis infection
    • Philipovskiy AV, Smiley ST, (2007) Vaccination with live Yersinia pestis primes CD4 and CD8 T cells that synergistically protect against lethal pulmonary Y. pestis infection. Infect Immun 75: 878-885.
    • (2007) Infect Immun , vol.75 , pp. 878-885
    • Philipovskiy, A.V.1    Smiley, S.T.2
  • 55
    • 61849095284 scopus 로고    scopus 로고
    • CpG oligodeoxynucleotides augment the murine immune response to the Yersinia pestis F1-V vaccine in bubonic and pneumonic models of plague
    • Amemiya K, Meyers JL, Rogers TE, Fast RL, Bassett AD, et al. (2009) CpG oligodeoxynucleotides augment the murine immune response to the Yersinia pestis F1-V vaccine in bubonic and pneumonic models of plague. Vaccine 27: 2220-2229.
    • (2009) Vaccine , vol.27 , pp. 2220-2229
    • Amemiya, K.1    Meyers, J.L.2    Rogers, T.E.3    Fast, R.L.4    Bassett, A.D.5
  • 56
    • 84877830638 scopus 로고    scopus 로고
    • Intranasal prophylaxis with CpG oligodeoxynucleotide can protect against Yersinia pestis infection
    • Hickey AJ, Lin JS, Kummer LW, Szaba FM, Duso DK, et al. (2013) Intranasal prophylaxis with CpG oligodeoxynucleotide can protect against Yersinia pestis infection. Infect Immun 81 (6) (): 2123-32.
    • (2013) Infect Immun , vol.81 , Issue.6 , pp. 2123-2132
    • Hickey, A.J.1    Lin, J.S.2    Kummer, L.W.3    Szaba, F.M.4    Duso, D.K.5
  • 57
    • 84862954894 scopus 로고    scopus 로고
    • Anthrax vaccine antigen-adjuvant formulations completely protect New Zealand white rabbits against challenge with Bacillus anthracis Ames strain spores
    • Peachman KK, Li Q, Matyas GR, Shivachandra SB, Lovchik J, et al. (2012) Anthrax vaccine antigen-adjuvant formulations completely protect New Zealand white rabbits against challenge with Bacillus anthracis Ames strain spores. Clin Vaccine Immunol 19: 11-16.
    • (2012) Clin Vaccine Immunol , vol.19 , pp. 11-16
    • Peachman, K.K.1    Li, Q.2    Matyas, G.R.3    Shivachandra, S.B.4    Lovchik, J.5
  • 58
    • 78751575656 scopus 로고    scopus 로고
    • Highly effective generic adjuvant systems for orphan or poverty-related vaccines
    • Rao M, Peachman KK, Li Q, Matyas GR, Shivachandra SB, et al. (2011) Highly effective generic adjuvant systems for orphan or poverty-related vaccines. Vaccine 29: 873-877.
    • (2011) Vaccine , vol.29 , pp. 873-877
    • Rao, M.1    Peachman, K.K.2    Li, Q.3    Matyas, G.R.4    Shivachandra, S.B.5
  • 59
    • 21444458163 scopus 로고    scopus 로고
    • Human volunteers receiving Escherichia coli phage T4 orally: a safety test of phage therapy
    • Bruttin A, Brussow H, (2005) Human volunteers receiving Escherichia coli phage T4 orally: a safety test of phage therapy. Antimicrob Agents Chemother 49: 2874-2878.
    • (2005) Antimicrob Agents Chemother , vol.49 , pp. 2874-2878
    • Bruttin, A.1    Brussow, H.2
  • 60
    • 84876065936 scopus 로고    scopus 로고
    • In vitro and in vivo delivery of genes and proteins using the bacteriophage T4 DNA packaging machine
    • Tao P, Mahalingam M, Marasa BS, Zhang Z, Chopra AK, et al. (2013) In vitro and in vivo delivery of genes and proteins using the bacteriophage T4 DNA packaging machine. Proc Natl Acad Sci U S A 110: 5846-5851.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 5846-5851
    • Tao, P.1    Mahalingam, M.2    Marasa, B.S.3    Zhang, Z.4    Chopra, A.K.5
  • 61
    • 0024556150 scopus 로고
    • Engineering hybrid genes without the use of restriction enzymes: gene splicing by overlap extension
    • Horton RM, Hunt HD, Ho SN, Pullen JK, Pease LR, (1989) Engineering hybrid genes without the use of restriction enzymes: gene splicing by overlap extension. Gene 77: 61-68.
    • (1989) Gene , vol.77 , pp. 61-68
    • Horton, R.M.1    Hunt, H.D.2    Ho, S.N.3    Pullen, J.K.4    Pease, L.R.5
  • 63
    • 77954259597 scopus 로고    scopus 로고
    • MetaMHC: a meta approach to predict peptides binding to MHC molecules
    • Hu X, Zhou W, Udaka K, Mamitsuka H, Zhu S, (2010) MetaMHC: a meta approach to predict peptides binding to MHC molecules. Nucleic Acids Res 38: W474-479.
    • (2010) Nucleic Acids Res , vol.38
    • Hu, X.1    Zhou, W.2    Udaka, K.3    Mamitsuka, H.4    Zhu, S.5
  • 64
    • 78650071105 scopus 로고    scopus 로고
    • Acceptable levels of endotoxin in vaccine formulations during preclinical research
    • Brito LA, Singh M, (2011) Acceptable levels of endotoxin in vaccine formulations during preclinical research. J Pharm Sci 100: 34-37.
    • (2011) J Pharm Sci , vol.100 , pp. 34-37
    • Brito, L.A.1    Singh, M.2
  • 65
    • 51149099737 scopus 로고    scopus 로고
    • Characterization of a mouse model of plague after aerosolization of Yersinia pestis CO92
    • Agar SL, Sha J, Foltz SM, Erova TE, Walberg KG, et al. (2008) Characterization of a mouse model of plague after aerosolization of Yersinia pestis CO92. Microbiology 154: 1939-1948.
    • (2008) Microbiology , vol.154 , pp. 1939-1948
    • Agar, S.L.1    Sha, J.2    Foltz, S.M.3    Erova, T.E.4    Walberg, K.G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.