메뉴 건너뛰기




Volumn 107, Issue 7, 2010, Pages 3099-3104

Delivery of foreign antigens by engineered outer membrane vesicle vaccines

Author keywords

Adjuvant; Protein subunit

Indexed keywords

ALUMINUM HYDROXIDE; CHIMERIC PROTEIN; GREEN FLUORESCENT PROTEIN; HEMOLYSIN; HYBRID PROTEIN; OUTER MEMBRANE PROTEIN; RECOMBINANT PROTEIN;

EID: 77649248408     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0805532107     Document Type: Article
Times cited : (229)

References (45)
  • 1
    • 0142058176 scopus 로고    scopus 로고
    • Recent advances in the discovery and delivery of vaccine adjuvants
    • O'Hagan DT, Valiante NM (2003) Recent advances in the discovery and delivery of vaccine adjuvants. Nat Rev Drug Discov 2:727-735.
    • (2003) Nat Rev Drug Discov , vol.2 , pp. 727-735
    • O'Hagan, D.T.1    Valiante, N.M.2
  • 2
    • 33845343230 scopus 로고    scopus 로고
    • Sustained high-titer antibody responses induced by conjugating a malarial vaccine candidate to outer-membrane protein complex
    • Wu YM, et al. (2006) Sustained high-titer antibody responses induced by conjugating a malarial vaccine candidate to outer-membrane protein complex. Proc Natl Acad Sci USA 103:18243-18248.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 18243-18248
    • Wu, Y.M.1
  • 3
    • 3042636653 scopus 로고    scopus 로고
    • Rabies virus nucleoprotein as a carrier for foreign antigens
    • Koser ML, et al. (2004) Rabies virus nucleoprotein as a carrier for foreign antigens. Proc Natl Acad Sci USA 101:9405-9410.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 9405-9410
    • Koser, M.L.1
  • 4
    • 35349027729 scopus 로고    scopus 로고
    • Nanoparticles and microparticles as vaccine-delivery systems
    • Singh M, Chakrapani A, O'Hagan D (2007) Nanoparticles and microparticles as vaccine-delivery systems. Expert Rev Vaccines 6:797-808.
    • (2007) Expert Rev Vaccines , vol.6 , pp. 797-808
    • Singh, M.1    Chakrapani, A.2    O'Hagan, D.3
  • 5
    • 0021255985 scopus 로고
    • Iscom, a novel structure for antigenic presentation of membrane proteins from enveloped viruses
    • Morein B, Sundquist B, Höglund S, Dalsgaard K, Osterhaus A (1984) Iscom, a novel structure for antigenic presentation of membrane proteins from enveloped viruses. Nature 308:457-460.
    • (1984) Nature , vol.308 , pp. 457-460
    • Morein, B.1    Sundquist, B.2    Höglund, S.3    Dalsgaard, K.4    Osterhaus, A.5
  • 6
    • 0023943993 scopus 로고
    • Proteosome-lipopeptide vaccines: Enhancement of immunogenicity for malaria CS peptides
    • Lowell GH, et al. (1988) Proteosome-lipopeptide vaccines: Enhancement of immunogenicity for malaria CS peptides. Science 240:800-802.
    • (1988) Science , vol.240 , pp. 800-802
    • Lowell, G.H.1
  • 7
    • 0023860096 scopus 로고
    • Peptides bound to proteosomes via hydrophobic feet become highly immunogenic without adjuvants
    • Lowell GH, Smith LF, Seid RC, Zollinger WD (1988) Peptides bound to proteosomes via hydrophobic feet become highly immunogenic without adjuvants. J Exp Med 167: 658-663.
    • (1988) J Exp Med , vol.167 , pp. 658-663
    • Lowell, G.H.1    Smith, L.F.2    Seid, R.C.3    Zollinger, W.D.4
  • 8
    • 9244234954 scopus 로고    scopus 로고
    • Liposomes and virosomes as delivery systems for antigens, nucleic acids and drugs
    • Felnerova D, Viret JF, Glück R, Moser C (2004) Liposomes and virosomes as delivery systems for antigens, nucleic acids and drugs. Curr Opin Biotechnol 15:518-529.
    • (2004) Curr Opin Biotechnol , vol.15 , pp. 518-529
    • Felnerova, D.1    Viret, J.F.2    Glück, R.3    Moser, C.4
  • 9
    • 16344384382 scopus 로고    scopus 로고
    • Lipid based particulate formulations for the delivery of antigen
    • Copland MJ, Rades T, Davies NM, Baird MA (2005) Lipid based particulate formulations for the delivery of antigen. Immunol Cell Biol 83:97-105.
    • (2005) Immunol Cell Biol , vol.83 , pp. 97-105
    • Copland, M.J.1    Rades, T.2    Davies, N.M.3    Baird, M.A.4
  • 10
    • 33750862932 scopus 로고    scopus 로고
    • Vaccine manufacturing: Challenges and solutions
    • Ulmer JB, Valley U, Rappuoli R (2006) Vaccine manufacturing: Challenges and solutions. Nat Biotechnol 24:1377-1383.
    • (2006) Nat Biotechnol , vol.24 , pp. 1377-1383
    • Ulmer, J.B.1    Valley, U.2    Rappuoli, R.3
  • 11
    • 14844296966 scopus 로고    scopus 로고
    • MeNZB: A safe and highly immunogenic tailor-made vaccine against the New Zealand Neisseria meningitidis serogroup B disease epidemic strain
    • Oster P, et al. (2005) MeNZB: A safe and highly immunogenic tailor-made vaccine against the New Zealand Neisseria meningitidis serogroup B disease epidemic strain. Vaccine 23:2191-2196.
    • (2005) Vaccine , vol.23 , pp. 2191-2196
    • Oster, P.1
  • 12
    • 33748045136 scopus 로고    scopus 로고
    • Persisting immune responses indicating long-term protection after booster dose with meningococcal group B outer membrane vesicle vaccine
    • Feiring B, et al. (2006) Persisting immune responses indicating long-term protection after booster dose with meningococcal group B outer membrane vesicle vaccine. Clin Vaccine Immunol 13:790-796.
    • (2006) Clin Vaccine Immunol , vol.13 , pp. 790-796
    • Feiring, B.1
  • 13
    • 0032839616 scopus 로고    scopus 로고
    • Structures of gram-negative cell walls and their derived membrane vesicles
    • Beveridge TJ (1999) Structures of gram-negative cell walls and their derived membrane vesicles. J Bacteriol 181:4725-4733.
    • (1999) J Bacteriol , vol.181 , pp. 4725-4733
    • Beveridge, T.J.1
  • 14
    • 27744480818 scopus 로고    scopus 로고
    • Bacterial outer membrane vesicles and the host-pathogen interaction
    • Kuehn MJ, Kesty NC (2005) Bacterial outer membrane vesicles and the host-pathogen interaction. Genes Dev 19:2645-2655.
    • (2005) Genes Dev , vol.19 , pp. 2645-2655
    • Kuehn, M.J.1    Kesty, N.C.2
  • 15
    • 0030197578 scopus 로고    scopus 로고
    • Production, characterization and control of a Neisseria meningitidis hexavalent class 1 outer membrane protein containing vesicle vaccine
    • Claassen I, et al. (1996) Production, characterization and control of a Neisseria meningitidis hexavalent class 1 outer membrane protein containing vesicle vaccine. Vaccine 14:1001-1008.
    • (1996) Vaccine , vol.14 , pp. 1001-1008
    • Claassen, I.1
  • 16
    • 1642575080 scopus 로고    scopus 로고
    • Stability of mono- and trivalent meningococcal outer membrane vesicle vaccines
    • Arigita C, et al. (2004) Stability of mono- and trivalent meningococcal outer membrane vesicle vaccines. Vaccine 22:629-642.
    • (2004) Vaccine , vol.22 , pp. 629-642
    • Arigita, C.1
  • 17
    • 0033971102 scopus 로고    scopus 로고
    • Immunogenicity and safety of a hexavalent meningococcal outer-membrane-vesicle vaccine in children of 2-3 and 7-8 years of age
    • de Kleijn ED, et al. (2000) Immunogenicity and safety of a hexavalent meningococcal outer-membrane-vesicle vaccine in children of 2-3 and 7-8 years of age. Vaccine 18: 1456-1466.
    • (2000) Vaccine , vol.18 , pp. 1456-1466
    • de Kleijn, E.D.1
  • 18
    • 34948901495 scopus 로고    scopus 로고
    • Immunogenicity and safety of a combination of two serogroup B meningococcal outer membrane vesicle vaccines
    • Sandbu S, et al. (2007) Immunogenicity and safety of a combination of two serogroup B meningococcal outer membrane vesicle vaccines. Clin Vaccine Immunol 14: 1062-1069.
    • (2007) Clin Vaccine Immunol , vol.14 , pp. 1062-1069
    • Sandbu, S.1
  • 19
    • 0346457133 scopus 로고    scopus 로고
    • Incorporation of heterologous outer membrane and periplasmic proteins into Escherichia coli outer membrane vesicles
    • Kesty NC, Kuehn MJ (2004) Incorporation of heterologous outer membrane and periplasmic proteins into Escherichia coli outer membrane vesicles. J Biol Chem 279: 2069-2076.
    • (2004) J Biol Chem , vol.279 , pp. 2069-2076
    • Kesty, N.C.1    Kuehn, M.J.2
  • 20
    • 32844455630 scopus 로고    scopus 로고
    • Outer membrane vesicle-mediated export of a poreforming cytotoxin from Escherichia coli
    • Kouokam JC, Wai SN (2006) Outer membrane vesicle-mediated export of a poreforming cytotoxin from Escherichia coli. Toxin Reviews 25:31-46.
    • (2006) Toxin Reviews , vol.25 , pp. 31-46
    • Kouokam, J.C.1    Wai, S.N.2
  • 21
    • 10744220460 scopus 로고    scopus 로고
    • Vesicle-mediated export and assembly of pore-forming oligomers of the enterobacterial ClyA cytotoxin
    • Wai SN, et al. (2003) Vesicle-mediated export and assembly of pore-forming oligomers of the enterobacterial ClyA cytotoxin. Cell 115:25-35.
    • (2003) Cell , vol.115 , pp. 25-35
    • Wai, S.N.1
  • 22
    • 44649126639 scopus 로고    scopus 로고
    • Engineered bacterial outer membrane vesicles with enhanced functionality
    • Kim J-Y, et al. (2008) Engineered bacterial outer membrane vesicles with enhanced functionality. J Mol Biol 380:51-66.
    • (2008) J Mol Biol , vol.380 , pp. 51-66
    • Kim, J.-Y.1
  • 23
    • 9244246299 scopus 로고    scopus 로고
    • Adaptation of the endogenous Salmonella enterica serovar Typhi clyA-encoded hemolysin for antigen export enhances the immunogenicity of anthrax protective antigen domain 4 expressed by the attenuated live-vector vaccine strain CVD 908-htrA
    • Galen JE, et al. (2004) Adaptation of the endogenous Salmonella enterica serovar Typhi clyA-encoded hemolysin for antigen export enhances the immunogenicity of anthrax protective antigen domain 4 expressed by the attenuated live-vector vaccine strain CVD 908-htrA. Infect Immun 72:7096-7106.
    • (2004) Infect Immun , vol.72 , pp. 7096-7106
    • Galen, J.E.1
  • 25
    • 0004155654 scopus 로고    scopus 로고
    • Levine MM, et al, ed , Marcel Dekker, Inc, New York, 3rd Ed
    • Levine MM, et al., ed (2004) New Generation Vaccines (Marcel Dekker, Inc., New York), 3rd Ed.
    • (2004) New Generation Vaccines
  • 26
    • 0037047626 scopus 로고    scopus 로고
    • Medicine. The intangible value of vaccination
    • Rappuoli R, Miller HI, Falkow S (2002) Medicine. The intangible value of vaccination. Science 297:937-939.
    • (2002) Science , vol.297 , pp. 937-939
    • Rappuoli, R.1    Miller, H.I.2    Falkow, S.3
  • 28
    • 0032490610 scopus 로고    scopus 로고
    • Aluminum compounds as vaccine adjuvants
    • Gupta RK (1998) Aluminum compounds as vaccine adjuvants. Adv Drug Deliv Rev 32: 155-172.
    • (1998) Adv Drug Deliv Rev , vol.32 , pp. 155-172
    • Gupta, R.K.1
  • 29
    • 0037205082 scopus 로고    scopus 로고
    • Workshop summary. Aluminum in vaccines
    • Eickhoff TC, Myers M (2002) Workshop summary. Aluminum in vaccines. Vaccine 20 (Suppl 3):S1-S4.
    • (2002) Vaccine , vol.20 , Issue.SUPPL. 3
    • Eickhoff, T.C.1    Myers, M.2
  • 30
    • 38849135564 scopus 로고    scopus 로고
    • Membrane vesicles are immunogenic facsimiles of Salmonella typhimurium that potently activate dendritic cells, prime B and T cell responses, and stimulate protective immunity in vivo
    • Alaniz RC, Deatherage BL, Lara JC, Cookson BT (2007) Membrane vesicles are immunogenic facsimiles of Salmonella typhimurium that potently activate dendritic cells, prime B and T cell responses, and stimulate protective immunity in vivo. J Immunol 179:7692-7701.
    • (2007) J Immunol , vol.179 , pp. 7692-7701
    • Alaniz, R.C.1    Deatherage, B.L.2    Lara, J.C.3    Cookson, B.T.4
  • 31
    • 33749353869 scopus 로고    scopus 로고
    • Purification of outer membrane vesicles from Pseudomonas aeruginosa and their activation of an IL-8 response
    • Bauman SJ, Kuehn MJ (2006) Purification of outer membrane vesicles from Pseudomonas aeruginosa and their activation of an IL-8 response. Microbes Infect 8: 2400-2408.
    • (2006) Microbes Infect , vol.8 , pp. 2400-2408
    • Bauman, S.J.1    Kuehn, M.J.2
  • 32
    • 0035856571 scopus 로고    scopus 로고
    • Secretion of the Escherichia coli K-12 SheA hemolysin is independent of its cytolytic activity
    • del Castillo FJ, Moreno F, del Castillo I (2001) Secretion of the Escherichia coli K-12 SheA hemolysin is independent of its cytolytic activity. FEMS Microbiol Lett 204: 281-285.
    • (2001) FEMS Microbiol Lett , vol.204 , pp. 281-285
    • del Castillo, F.J.1    Moreno, F.2    del Castillo, I.3
  • 33
    • 33745748447 scopus 로고    scopus 로고
    • Cytotoxin ClyA from Escherichia coli assembles to a 13-meric pore independent of its redox-state
    • Eifler N, et al. (2006) Cytotoxin ClyA from Escherichia coli assembles to a 13-meric pore independent of its redox-state. EMBO J 25:2652-2661.
    • (2006) EMBO J , vol.25 , pp. 2652-2661
    • Eifler, N.1
  • 35
    • 0042838115 scopus 로고    scopus 로고
    • Characterization of dominantly negative mutant ClyA cytotoxin proteins in Escherichia coli
    • Wai SN, et al. (2003) Characterization of dominantly negative mutant ClyA cytotoxin proteins in Escherichia coli. J Bacteriol 185:5491-5499.
    • (2003) J Bacteriol , vol.185 , pp. 5491-5499
    • Wai, S.N.1
  • 36
    • 0027764291 scopus 로고
    • The influence of antigen organization on B cell responsiveness
    • Bachmann MF, et al. (1993) The influence of antigen organization on B cell responsiveness. Science 262:1448-1451.
    • (1993) Science , vol.262 , pp. 1448-1451
    • Bachmann, M.F.1
  • 37
    • 0035873381 scopus 로고    scopus 로고
    • Cell-associated ovalbumin is cross-presented much more efficiently than soluble ovalbumin in vivo
    • Li M, et al. (2001) Cell-associated ovalbumin is cross-presented much more efficiently than soluble ovalbumin in vivo. J Immunol 166:6099-6103.
    • (2001) J Immunol , vol.166 , pp. 6099-6103
    • Li, M.1
  • 38
    • 0032858030 scopus 로고    scopus 로고
    • Immunogenicity of outer membrane proteins in a lipopolysaccharide-deficient mutant of Neisseria meningitidis: Influence of adjuvants on the immune response
    • Steeghs L, et al. (1999) Immunogenicity of outer membrane proteins in a lipopolysaccharide-deficient mutant of Neisseria meningitidis: Influence of adjuvants on the immune response. Infect Immun 67:4988-4993.
    • (1999) Infect Immun , vol.67 , pp. 4988-4993
    • Steeghs, L.1
  • 39
    • 0032959537 scopus 로고    scopus 로고
    • Export of virulence genes and Shiga toxin by membrane vesicles of Escherichia coli O157:H7
    • Kolling GL, Matthews KR (1999) Export of virulence genes and Shiga toxin by membrane vesicles of Escherichia coli O157:H7. Appl Environ Microbiol 65:1843-1848.
    • (1999) Appl Environ Microbiol , vol.65 , pp. 1843-1848
    • Kolling, G.L.1    Matthews, K.R.2
  • 41
    • 0029973636 scopus 로고    scopus 로고
    • FACS-optimized mutants of the green fluorescent protein (GFP)
    • Cormack BP, Valdivia RH, Falkow S (1996) FACS-optimized mutants of the green fluorescent protein (GFP). Gene 173:33-38.
    • (1996) Gene , vol.173 , pp. 33-38
    • Cormack, B.P.1    Valdivia, R.H.2    Falkow, S.3
  • 42
    • 0028334116 scopus 로고
    • Assays of hemolytic toxins
    • Rowe GE, Welch RA (1994) Assays of hemolytic toxins. Methods Enzymol 235:657-667.
    • (1994) Methods Enzymol , vol.235 , pp. 657-667
    • Rowe, G.E.1    Welch, R.A.2
  • 43
    • 0018087520 scopus 로고
    • A new and improved microassay to determine 2-keto-3-deoxyoctonate in lipopolysaccharide of Gram-negative bacteria
    • Karkhanis YD, Zeltner JY, Jackson JJ, Carlo DJ (1978) A new and improved microassay to determine 2-keto-3-deoxyoctonate in lipopolysaccharide of Gram-negative bacteria. Anal Biochem 85:595-601.
    • (1978) Anal Biochem , vol.85 , pp. 595-601
    • Karkhanis, Y.D.1    Zeltner, J.Y.2    Jackson, J.J.3    Carlo, D.J.4
  • 44
    • 19744371191 scopus 로고    scopus 로고
    • Role of lipopolysaccharide on the structure and function of alpha-hemolysin from Escherichia coli
    • Herlax V, de Alaniz MJT, Bakás L (2005) Role of lipopolysaccharide on the structure and function of alpha-hemolysin from Escherichia coli. Chem Phys Lipids 135:107-115.
    • (2005) Chem Phys Lipids , vol.135 , pp. 107-115
    • Herlax, V.1    de Alaniz, M.J.T.2    Bakás, L.3
  • 45
    • 0033081239 scopus 로고    scopus 로고
    • Quantification of bacterial lipopolysaccharides by the purpald assay: Measuring formaldehyde generated from 2-keto-3-deoxyoctonate and heptose at the inner core by periodate oxidation
    • Lee CH, Tsai CM (1999) Quantification of bacterial lipopolysaccharides by the purpald assay: Measuring formaldehyde generated from 2-keto-3-deoxyoctonate and heptose at the inner core by periodate oxidation. Anal Biochem 267:161-168.
    • (1999) Anal Biochem , vol.267 , pp. 161-168
    • Lee, C.H.1    Tsai, C.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.