메뉴 건너뛰기




Volumn 30, Issue 3, 2010, Pages 239-254

Proteomics for the development of vaccines and therapeutics

Author keywords

Antigen identification; B cell epitopes; Bacillus anthracis; Immunoproteomics; LC MS MS; MALDI TOF; Moonlighting proteins; Proteomics; Therapeutics; Vaccines

Indexed keywords

ADJUVANT; ANTHRAX VACCINE; ANTIGEN; BACTERIAL PROTEIN; CHAPERONE; EPITOPE; IMMUNOMODULATING AGENT; BACTERIAL VACCINE; IMMUNOLOGICAL ADJUVANT;

EID: 77950975441     PISSN: 10408401     EISSN: None     Source Type: Journal    
DOI: 10.1615/critrevimmunol.v30.i3.20     Document Type: Review
Times cited : (6)

References (35)
  • 1
    • 35649020232 scopus 로고    scopus 로고
    • Recombinant exosporium protein BclA of Bacillus anthracis is efective as a booster for mice primed with suboptimal amounts of protective antigen
    • Nov
    • Brahmbhatt TN Darnell SC Carvalho HM Sanz P Kang TJ Bull RL Rasmussen SB Cross AS O'Brien AD. Recombinant exosporium protein BclA of Bacillus anthracis is efective as a booster for mice primed with suboptimal amounts of protective antigen. Infect Immun. 2007, Nov 75. 11, 5240-5247
    • (2007) Infect Immun , vol.75 , Issue.11 , pp. 5240-5247
    • Brahmbhatt, T.N.1    Darnell, S.C.2    Carvalho, H.M.3    Sanz, P.4    Kang, T.J.5    Bull, R.L.6    Rasmussen, S.B.7    Cross, A.S.8    O'Brien, A.D.9
  • 2
    • 0036151303 scopus 로고    scopus 로고
    • Anthrax spores make an essential contribution to vaccine efcacy
    • Feb
    • Brossier F, Levy M, Mock M. Anthrax spores make an essential contribution to vaccine efcacy. Infect Immun. 2002 Feb;70(2):661-664
    • (2002) Infect Immun , vol.70 , Issue.2 , pp. 661-664
    • Brossier, F.1    Levy, M.2    Mock, M.3
  • 3
    • 62449245698 scopus 로고    scopus 로고
    • Efcacy of a vaccine based on protective antigen and killed spores against experimental inhalational anthrax
    • Mar
    • Gauthier YP, Tournier JN, Paucod JC, Corre JP, Mock M, Goossens PL, Vidal DR. Efcacy of a vaccine based on protective antigen and killed spores against experimental inhalational anthrax. Infect Immun. 2009 Mar;77(3):1197-1207
    • (2009) Infect Immun , vol.77 , Issue.3 , pp. 1197-1207
    • Gauthier, Y.P.1    Tournier, J.N.2    Paucod, J.C.3    Corre, J.P.4    Mock, M.5    Goossens, P.L.6    Vidal, D.R.7
  • 4
    • 0028175130 scopus 로고
    • Human live anthrax vaccine in the former USSR
    • DOI 10.1016/0264-410X(94)90223-2
    • Shlyakhov EN, Rubinstein E. Human live anthrax vaccine in the former USSR. Vaccine. 1994;12(8):727-730 (Pubitemid 24182373)
    • (1994) Vaccine , vol.12 , Issue.8 , pp. 727-730
    • Shlyakhov, E.N.1    Rubinstein, E.2
  • 10
    • 0023119101 scopus 로고
    • Antigen speci-fcity and cross-reactivity of monoclonal anti-lysozyme antibodies
    • Feb
    • Harper M, Lema F, Boulot G, Poljak RJ. Antigen speci-fcity and cross-reactivity of monoclonal anti-lysozyme antibodies. Mol Immunol. 1987 Feb;24(2):97-108.
    • (1987) Mol Immunol , vol.24 , Issue.2 , pp. 97-108
    • Harper, M.1    Lema, F.2    Boulot, G.3    Poljak, R.J.4
  • 11
    • 0022497692 scopus 로고
    • Mapping epitopes on a protein antigen by the proteolysis of antigen-antibody complexes
    • May 23
    • Jemmerson R, Paterson Y. Mapping epitopes on a protein antigen by the proteolysis of antigen-antibody complexes. Science. 1986 May 23;232(4753): 1001-1004
    • (1986) Science , vol.232 , Issue.4753 , pp. 1001-1004
    • Jemmerson, R.1    Paterson, Y.2
  • 12
    • 0033135224 scopus 로고    scopus 로고
    • Direct identification of protein epitopes by mass spectrometry without immobilization of antibody and isolation of antibody-peptide complexes
    • May 1
    • Kiselar JG, Downard KM. Direct identification of protein epitopes by mass spectrometry without immobilization of antibody and isolation of antibody-peptide complexes. Anal Chem. 1999 May 1;71(9):1792-1801
    • (1999) Anal Chem , vol.71 , Issue.9 , pp. 1792-1801
    • Kiselar, J.G.1    Downard, K.M.2
  • 13
    • 0034477744 scopus 로고    scopus 로고
    • Preservation and detection of specifc antibody-peptide complexes by matrix-assisted laser desorption ionization mass spectrometry
    • Aug
    • Kiselar JG, Downard KM. Preservation and detection of specifc antibody-peptide complexes by matrix-assisted laser desorption ionization mass spectrometry. J Am Soc Mass Spectrom. 2000 Aug;11(8):746-750
    • (2000) J Am Soc Mass Spectrom , vol.11 , Issue.8 , pp. 746-750
    • Kiselar, J.G.1    Downard, K.M.2
  • 14
    • 27844471239 scopus 로고    scopus 로고
    • Mass spectrometry and the search for moonlighting proteins
    • Nov
    • Jefery CJ. Mass spectrometry and the search for moonlighting proteins. Mass Spectrom Rev. 2005 Nov;24(6):772-782
    • (2005) Mass Spectrom Rev , vol.24 , Issue.6 , pp. 772-782
    • Jefery, C.J.1
  • 15
    • 52449135569 scopus 로고    scopus 로고
    • Alpha-Enolase binds to human plasminogen on the surface of Bacillus anthracis
    • Jul 1784
    • Agarwal S, Kulshreshtha P, Bambah MD, Bhatnagar R. alpha-Enolase binds to human plasminogen on the surface of Bacillus anthracis. Biochim Biophys Acta. 2008 Jul;1784(7-8):986-994
    • (2008) Biochim Biophys Acta , vol.1784 , Issue.7-8 , pp. 986-994
    • Agarwal, S.1    Kulshreshtha, P.2    Bambah, M.D.3    Bhatnagar, R.4
  • 16
    • 33745589526 scopus 로고    scopus 로고
    • Stress wars: The direct role of host and bacterial molecular chap-erones in bacterial infection
    • Jul
    • Henderson B, Allan E, Coates AR. Stress wars: the direct role of host and bacterial molecular chap-erones in bacterial infection. Infect Immun. 2006 Jul;74(7):3693-3706
    • (2006) Infect Immun , vol.74 , Issue.7 , pp. 3693-3706
    • Henderson, B.1    Allan, E.2    Coates, A.R.3
  • 17
    • 12944325306 scopus 로고    scopus 로고
    • Bacterial metastasis: The host plasminogen system in bacterial invasion
    • Feb
    • Lahteenmaki K, Edelman S, Korhonen TK. Bacterial metastasis: the host plasminogen system in bacterial invasion. Trends Microbiol. 2005 Feb;13(2):79-85.
    • (2005) Trends Microbiol , vol.13 , Issue.2 , pp. 79-85
    • Lahteenmaki, K.1    Edelman, S.2    Korhonen, T.K.3
  • 19
    • 33745973006 scopus 로고    scopus 로고
    • Proteomic analysis of Brucella abortus cell envelope and identifcation of immunogenic candidate proteins for vaccine development
    • Jul
    • DelVecchio VG. Proteomic analysis of Brucella abortus cell envelope and identifcation of immunogenic candidate proteins for vaccine development. Proteomics. 2006 Jul;6(13):3767-3780
    • (2006) Proteomics , vol.6 , Issue.13 , pp. 3767-3780
    • Delvecchio, V.G.1
  • 20
    • 34249332380 scopus 로고    scopus 로고
    • Role of secreted glyceraldehyde-3-phosphate dehydrogenase in the infection mechanism of enterohemorrhagic and enteropathogenic Escherichia coli: Interaction of the extracellular enzyme with human plasminogen and fbrinogen
    • Egea L, Aguilera L, Gimenez R, Sorolla MA, Aguilar J, Badia J, Baldoma L. Role of secreted glyceraldehyde-3-phosphate dehydrogenase in the infection mechanism of enterohemorrhagic and enteropathogenic Escherichia coli: interaction of the extracellular enzyme with human plasminogen and fbrinogen. Int J Biochem Cell Biol. 2007;39(6):1190-1203
    • (2007) Int J Biochem Cell Biol , vol.39 , Issue.6 , pp. 1190-1203
    • Egea, L.1    Aguilera, L.2    Gimenez, R.3    Sorolla, M.A.4    Aguilar, J.5    Badia, J.6    Baldoma, L.7
  • 21
    • 34247854961 scopus 로고    scopus 로고
    • Cytosolic proteins contribute to surface plasminogen recruitment of Neisseria men-ingitidis
    • Apr
    • Knaust A, Weber MV, Hammerschmidt S, Bergmann S, Frosch M, Kurzai O. Cytosolic proteins contribute to surface plasminogen recruitment of Neisseria men-ingitidis. J Bacteriol. 2007 Apr;189(8):3246-3255
    • (2007) J Bacteriol , vol.189 , Issue.8 , pp. 3246-3255
    • Knaust, A.1    Weber, M.V.2    Hammerschmidt, S.3    Bergmann, S.4    Frosch, M.5    Kurzai, O.6
  • 22
    • 35148826082 scopus 로고    scopus 로고
    • Interaction with human plasminogen system turns on proteolytic activity in Streptococcus agalactiae and enhances its virulence in a mouse model
    • Sep
    • Magalhaes V, Veiga-Malta I, Almeida MR, Baptista M, Ribeiro A, Trieu-Cuot P, Ferreira P. Interaction with human plasminogen system turns on proteolytic activity in Streptococcus agalactiae and enhances its virulence in a mouse model. Microbes Infect. 2007 Sep;9(11):1276-1284
    • (2007) Microbes Infect , vol.9 , Issue.11 , pp. 1276-1284
    • Magalhaes, V.1    Veiga-Malta, I.2    Almeida, M.R.3    Baptista, M.4    Ribeiro, A.5    Trieu-Cuot, P.6    Ferreira, P.7
  • 23
    • 0347753321 scopus 로고    scopus 로고
    • Housekeeping enzymes as virulence factors for pathogens
    • Dec
    • Pancholi V, Chhatwal GS. Housekeeping enzymes as virulence factors for pathogens. Int J Med Microbiol. 2003 Dec;293(6):391-401.
    • (2003) Int J Med Microbiol , vol.293 , Issue.6 , pp. 391-401
    • Pancholi, V.1    Chhatwal, G.S.2
  • 24
    • 0038501069 scopus 로고    scopus 로고
    • Identifcation of a novel plasmin(ogen)-binding motif in surface displayed alpha-enolase of Streptococcus pneumoniae
    • Jul
    • Bergmann S, Wild D, Diekmann O, Frank R, Bracht D, Chhatwal GS, Hammerschmidt S. Identifcation of a novel plasmin(ogen)-binding motif in surface displayed alpha-enolase of Streptococcus pneumoniae. Mol Microbiol. 2003 Jul;49(2):411-423
    • (2003) Mol Microbiol , vol.49 , Issue.2 , pp. 411-423
    • Bergmann, S.1    Wild, D.2    Diekmann, O.3    Frank, R.4    Bracht, D.5    Chhatwal, G.S.6    Hammerschmidt, S.7
  • 25
    • 36148995456 scopus 로고    scopus 로고
    • Comparative study of the physiological roles of three peroxidases (NADH peroxidase Alkyl hydroperoxide reductase and Tiol peroxidase) in oxidative stress response survival inside macrophages and virulence of Enterococcus faecalis
    • Dec
    • La CS, Sauvageot N, Giard JC, Benachour A, Posteraro B, Aufray Y, Sanguinetti M, Hartke A. Comparative study of the physiological roles of three peroxidases (NADH peroxidase, Alkyl hydroperoxide reductase and Tiol peroxidase) in oxidative stress response, survival inside macrophages and virulence of Enterococcus faecalis. Mol Microbiol. 2007 Dec;66(5):1148-1163
    • (2007) Mol Microbiol , vol.66 , Issue.5 , pp. 1148-1163
    • La Cs Sauvageot, N.1    Giard, J.C.2    Benachour, A.3    Posteraro, B.4    Aufray, Y.5    Sanguinetti, M.6    Hartke, A.7
  • 27
    • 0037344772 scopus 로고    scopus 로고
    • Candida albicans binds human plas-minogen: Identifcation of eight plasminogen-binding proteins
    • Mar
    • Crowe JD, Sievwright IK, Auld GC, Moore NR, Gow NA, Booth NA. Candida albicans binds human plas-minogen: identifcation of eight plasminogen-binding proteins. Mol Microbiol. 2003 Mar;47(6):1637-1651
    • (2003) Mol Microbiol , vol.47 , Issue.6 , pp. 1637-1651
    • Crowe, J.D.1    Sievwright, I.K.2    Auld, G.C.3    Moore, N.R.4    Gow, N.A.5    Booth, N.A.6
  • 29
    • 35648977084 scopus 로고    scopus 로고
    • Protective properties and surface localization of Plasmodium falciparum enolase
    • Nov
    • Pal-Bhowmick I, Mehta M, Coppens I, Sharma S, Jarori GK. Protective properties and surface localization of Plasmodium falciparum enolase. Infect Immun. 2007 Nov;75(11):5500-5508
    • (2007) Infect Immun , vol.75 , Issue.11 , pp. 5500-5508
    • Pal-Bhowmick, I.1    Mehta, M.2    Coppens, I.3    Sharma, S.4    Jarori, G.K.5
  • 30
    • 65549164868 scopus 로고    scopus 로고
    • Surface-expressed enolase contributes to the pathogenesis of clinical isolate SSU of Aeromonas hydrophila
    • May
    • Sha J, Erova TE, Alyea RA, Wang S, Olano JP, Pancholi V, Chopra AK. Surface-expressed enolase contributes to the pathogenesis of clinical isolate SSU of Aeromonas hydrophila. J Bacteriol. 2009 May;191(9):3095-3107
    • (2009) J Bacteriol , vol.191 , Issue.9 , pp. 3095-3107
    • Sha, J.1    Erova, T.E.2    Alyea, R.A.3    Wang, S.4    Olano, J.P.5    Pancholi, V.6    Chopra, A.K.7
  • 31
    • 59649104375 scopus 로고    scopus 로고
    • Identifcation and characterization of a novel protective antigen Enolase of Streptococcus suis serotype 2
    • Feb 25
    • Zhang A, Chen B, Mu X, Li R, Zheng P, Zhao Y, Chen H, Jin M. Identifcation and characterization of a novel protective antigen, Enolase of Streptococcus suis serotype 2. Vaccine. 2009 Feb 25;27(9): 1348-1353
    • (2009) Vaccine , vol.27 , Issue.9 , pp. 1348-1353
    • Zhang, A.1    Chen, B.2    Mu, X.3    Li, R.4    Zheng, P.5    Zhao, Y.6    Chen, H.7    Jin, M.8
  • 32
    • 9644259128 scopus 로고    scopus 로고
    • A humanized monoclonal antibody targeting Staphylococcus aureus
    • Patti JM. A humanized monoclonal antibody targeting Staphylococcus aureus. Vaccine. 2004;22(Suppl 1): S39-43.
    • (2004) Vaccine , vol.22 , Issue.SUPPL 1
    • Patti, J.M.1
  • 33
    • 14744277458 scopus 로고    scopus 로고
    • Open-label dose escalation study of the safety and pharmacokinetic profle of tefbazumab in healthy volunteers
    • Mar
    • Reilley S, Wenzel E, Reynolds L, Bennett B, Patti JM, Hetherington S. Open-label, dose escalation study of the safety and pharmacokinetic profle of tefbazumab in healthy volunteers. Antimicrob Agents Chemother. 2005 Mar;49(3):959-962
    • (2005) Antimicrob Agents Chemother , vol.49 , Issue.3 , pp. 959-962
    • Reilley, S.1    Wenzel, E.2    Reynolds, L.3    Bennett, B.4    Patti, J.M.5    Hetherington, S.6
  • 35
    • 24744447203 scopus 로고    scopus 로고
    • An immune response directed to proteinase and adhesin functional epitopes protects against Porphyromonas gingivalis-induced peri-odontal bone loss
    • Sep 15
    • O?Brien-Simpson NM, Pathirana RD, Paolini RA, Chen YY, Veith PD, Tam V, Ally N, Pike RN, Reynolds EC. An immune response directed to proteinase and adhesin functional epitopes protects against Porphyromonas gingivalis-induced peri-odontal bone loss. J Immunol. 2005 Sep 15;175(6): 3980-3989
    • (2005) J Immunol , vol.175 , Issue.6 , pp. 3980-3989
    • Obrien-Simpson, N.M.1    Pathirana, R.D.2    Paolini, R.A.3    Chen, Y.Y.4    Veith, P.D.5    Tam, V.6    Ally, N.7    Pike, R.N.8    Reynolds, E.C.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.