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Volumn 76, Issue 3, 2008, Pages 1223-1229

Physical linkage of naturally complexed bacterial outer membrane proteins enhances immunogenicity

Author keywords

[No Author keywords available]

Indexed keywords

ANTIGEN; CD4 ANTIGEN; IMMUNOGLOBULIN G; MAJOR SURFACE PROTEIN 1A; MAJOR SURFACE PROTEIN 1B1; OUTER MEMBRANE PROTEIN; UNCLASSIFIED DRUG; BACTERIUM ANTIBODY; EPITOPE; HYBRID PROTEIN; MAJOR SURFACE PROTEIN 1A, ANAPLASMA; MAJOR SURFACE PROTEIN 1B, ANAPLASMA;

EID: 40749087672     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/IAI.01356-07     Document Type: Article
Times cited : (24)

References (40)
  • 1
    • 18944375014 scopus 로고    scopus 로고
    • + T lymphocyte responses specific for Anaplasma marginale major surface protein-2 (MSP2) in MSP2 vaccinates following challenge with live A. marginale
    • + T lymphocyte responses specific for Anaplasma marginale major surface protein-2 (MSP2) in MSP2 vaccinates following challenge with live A. marginale. J. Immunol. 174:6702-6715.
    • (2005) J. Immunol , vol.174 , pp. 6702-6715
    • Abbott, J.R.1    Palmer, G.H.2    Kegerreis, K.A.3    Hetrick, P.F.4    Howard, C.J.5    Hope, J.C.6    Brown, W.C.7
  • 2
    • 0025255264 scopus 로고
    • Molecular basis for surface antigen size polymorphisms and conservation of a neutralization-sensitive epitope in Anaplasma marginale
    • Allred, D. R., T. C. McGuire, G. H. Palmer, S. R. Leib, T. M. Harkins, T. F. McElwain, and A. F. Barbet. 1990. Molecular basis for surface antigen size polymorphisms and conservation of a neutralization-sensitive epitope in Anaplasma marginale. Proc. Natl. Acad. Sci. USA 87:3220-3224.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 3220-3224
    • Allred, D.R.1    McGuire, T.C.2    Palmer, G.H.3    Leib, S.R.4    Harkins, T.M.5    McElwain, T.F.6    Barbet, A.F.7
  • 3
    • 0021319748 scopus 로고
    • Role of disulfide bonding in outer membrane structure and permeability in Chlamydia trachomatis
    • Bavoil, P., A. Ohlin, and J. Schachter. 1984. Role of disulfide bonding in outer membrane structure and permeability in Chlamydia trachomatis. Infect. Immun. 44:479-485.
    • (1984) Infect. Immun , vol.44 , pp. 479-485
    • Bavoil, P.1    Ohlin, A.2    Schachter, J.3
  • 4
    • 33744502352 scopus 로고    scopus 로고
    • Flagella as a platform for epitope-based vaccines
    • Ben-Yedidia, T., and R. Arnon. 2006. Flagella as a platform for epitope-based vaccines. Isr. Med. Assoc. J. 8:316-318.
    • (2006) Isr. Med. Assoc. J , vol.8 , pp. 316-318
    • Ben-Yedidia, T.1    Arnon, R.2
  • 5
    • 33750601397 scopus 로고    scopus 로고
    • Towards an epitope-based human vaccine for influenza
    • Ben-Yedidia, T., and R. Arnon. 2005. Towards an epitope-based human vaccine for influenza. Hum. Vaccines 1:95-101.
    • (2005) Hum. Vaccines , vol.1 , pp. 95-101
    • Ben-Yedidia, T.1    Arnon, R.2
  • 7
    • 0034781872 scopus 로고    scopus 로고
    • + T lymphocytes from calves immunized with Anaplasma marginale major surface protein 1 (MSP1), a heteromeric complex of MSP1a and MSP1b, preferentially recognize the MSP1a carboxyl terminus that is conserved among strains
    • + T lymphocytes from calves immunized with Anaplasma marginale major surface protein 1 (MSP1), a heteromeric complex of MSP1a and MSP1b, preferentially recognize the MSP1a carboxyl terminus that is conserved among strains. Infect. Immun. 69:6853-6862.
    • (2001) Infect. Immun , vol.69 , pp. 6853-6862
    • Brown, W.C.1    Palmer, G.H.2    Lewin, H.A.3    McGuire, T.C.4
  • 8
    • 0032425064 scopus 로고    scopus 로고
    • + T-lymphocyte and immunoglobulin G2 responses in calves immunized with Anaplasma marginale outer membranes and protected against homologous challenge
    • + T-lymphocyte and immunoglobulin G2 responses in calves immunized with Anaplasma marginale outer membranes and protected against homologous challenge. Infect. Immun. 66:5406-5413.
    • (1998) Infect. Immun , vol.66 , pp. 5406-5413
    • Brown, W.C.1    Shkap, V.2    Zhu, D.3    McGuire, T.C.4    Tuo, W.5    McElwain, T.F.6    Palmer, G.H.7
  • 10
    • 0028853805 scopus 로고
    • Role of lipopolysaccharide and a major outer membrane protein from Francisella tularensis in the induction of immunity against tularemia
    • Fulop, M., R. Manchee, and R. Titball. 1995. Role of lipopolysaccharide and a major outer membrane protein from Francisella tularensis in the induction of immunity against tularemia. Vaccine 13:1220-1225.
    • (1995) Vaccine , vol.13 , pp. 1220-1225
    • Fulop, M.1    Manchee, R.2    Titball, R.3
  • 11
    • 0342576235 scopus 로고    scopus 로고
    • Role of two outer membrane antigens in the induction of protective immunity against Francisella tularensis strains of different virulence
    • Fulop, M., R. Manchee, and R. Titball. 1996. Role of two outer membrane antigens in the induction of protective immunity against Francisella tularensis strains of different virulence. FEMS. Immunol. Med. Microbiol. 13:245-247.
    • (1996) FEMS. Immunol. Med. Microbiol , vol.13 , pp. 245-247
    • Fulop, M.1    Manchee, R.2    Titball, R.3
  • 12
    • 0027243733 scopus 로고
    • Evaluation of mixtures of purified Haemophilus influenzae outer membrane proteins in protection against challenge with nontypeable H. influenzae in the chinchilla otitis media model
    • Green, B. A., M. E. Vazquez, G. W. Zlotnick, G. Quigley-Reape, J. D. Swarts, I. Green, J. L. Cowell, C. D. Bluestone, and W. J. Doyle. 1993. Evaluation of mixtures of purified Haemophilus influenzae outer membrane proteins in protection against challenge with nontypeable H. influenzae in the chinchilla otitis media model. Infect. Immun. 61:1950-1957.
    • (1993) Infect. Immun , vol.61 , pp. 1950-1957
    • Green, B.A.1    Vazquez, M.E.2    Zlotnick, G.W.3    Quigley-Reape, G.4    Swarts, J.D.5    Green, I.6    Cowell, J.L.7    Bluestone, C.D.8    Doyle, W.J.9
  • 13
    • 0032702291 scopus 로고    scopus 로고
    • Leptospiral outer membrane proteins OmpL1 and LipL41 exhibit synergistic immunoprotection
    • Haake, D. A., M. K. Mazel, A. M. McCoy, F. Milward, G. Chao, J. Matsunaga, and E. A. Wagar. 1999. Leptospiral outer membrane proteins OmpL1 and LipL41 exhibit synergistic immunoprotection. Infect. Immun. 67:6572-6582.
    • (1999) Infect. Immun , vol.67 , pp. 6572-6582
    • Haake, D.A.1    Mazel, M.K.2    McCoy, A.M.3    Milward, F.4    Chao, G.5    Matsunaga, J.6    Wagar, E.A.7
  • 14
    • 0030027256 scopus 로고    scopus 로고
    • Disulfide cross-linked envelope proteins: The functional equivalent of peptidoglycan in chlamydiae?
    • Hatch, T. P. 1996. Disulfide cross-linked envelope proteins: the functional equivalent of peptidoglycan in chlamydiae? J. Bacteriol. 178:1-5.
    • (1996) J. Bacteriol , vol.178 , pp. 1-5
    • Hatch, T.P.1
  • 15
    • 0022444940 scopus 로고
    • Synthesis of disulfide-bonded outer membrane proteins during the developmental cycle of Chlamydia psittaci and Chlamydia trachomatis
    • Hatch, T. P., M. Miceli, and J. E. Sublett. 1986. Synthesis of disulfide-bonded outer membrane proteins during the developmental cycle of Chlamydia psittaci and Chlamydia trachomatis. J. Bacteriol. 165:379-385.
    • (1986) J. Bacteriol , vol.165 , pp. 379-385
    • Hatch, T.P.1    Miceli, M.2    Sublett, J.E.3
  • 17
    • 34248341795 scopus 로고    scopus 로고
    • Immunogenicity of Anaplasma marginale type IV secretion system proteins in a protective outer membrane vaccine
    • Lopez, J. E., G. H. Palmer, K. A. Brayton, M. J. Dark, S. E. Leach, and W. C. Brown. 2007. Immunogenicity of Anaplasma marginale type IV secretion system proteins in a protective outer membrane vaccine. Infect. Immun. 75:2333-2342.
    • (2007) Infect. Immun , vol.75 , pp. 2333-2342
    • Lopez, J.E.1    Palmer, G.H.2    Brayton, K.A.3    Dark, M.J.4    Leach, S.E.5    Brown, W.C.6
  • 18
    • 28444444136 scopus 로고    scopus 로고
    • Identification of novel antigenic proteins in a complex Anaplasma marginale outer membrane immunogen by mass spectrometry and genomic mapping
    • Lopez, J. E., W. F. Siems, G. H. Palmer, K. A. Brayton, T. C. McGuire, J. Norimine, and W. C. Brown. 2005. Identification of novel antigenic proteins in a complex Anaplasma marginale outer membrane immunogen by mass spectrometry and genomic mapping. Infect. Immun. 73:8109-8118.
    • (2005) Infect. Immun , vol.73 , pp. 8109-8118
    • Lopez, J.E.1    Siems, W.F.2    Palmer, G.H.3    Brayton, K.A.4    McGuire, T.C.5    Norimine, J.6    Brown, W.C.7
  • 19
    • 33745460376 scopus 로고    scopus 로고
    • Analysis of the Anaplasma marginale major surface protein 1 complex protein composition by tandem mass spectrometry
    • Macmillan, H., K. A. Brayton, G. H. Palmer, T. C. McGuire, G. Munske, W. F. Siems, and W. C. Brown. 2006. Analysis of the Anaplasma marginale major surface protein 1 complex protein composition by tandem mass spectrometry. J. Bacteriol. 188:4983-4991.
    • (2006) J. Bacteriol , vol.188 , pp. 4983-4991
    • Macmillan, H.1    Brayton, K.A.2    Palmer, G.H.3    McGuire, T.C.4    Munske, G.5    Siems, W.F.6    Brown, W.C.7
  • 20
    • 0021276130 scopus 로고
    • Common and isolate-restricted antigens of Anaplasma marginale detected with monoclonal antibodies
    • McGuire, T. C., G. H. Palmer, W. L. Goff, M. I. Johnson, and W. C. Davis. 1984. Common and isolate-restricted antigens of Anaplasma marginale detected with monoclonal antibodies. Infect. Immun. 45:697-700.
    • (1984) Infect. Immun , vol.45 , pp. 697-700
    • McGuire, T.C.1    Palmer, G.H.2    Goff, W.L.3    Johnson, M.I.4    Davis, W.C.5
  • 21
    • 4043179979 scopus 로고    scopus 로고
    • Generation and use of epitope-tagged receptors
    • McIlhinney, R. A. 2004. Generation and use of epitope-tagged receptors. Methods Mol. Biol. 259:81-98.
    • (2004) Methods Mol. Biol , vol.259 , pp. 81-98
    • McIlhinney, R.A.1
  • 22
    • 0023074775 scopus 로고
    • Biosynthesis and disulfide cross-linking of outer membrane components during the growth cycle of Chlamydia trachomatis
    • Newhall, W. J. V. 1987. Biosynthesis and disulfide cross-linking of outer membrane components during the growth cycle of Chlamydia trachomatis. Infect. Immun. 55:162-168.
    • (1987) Infect. Immun , vol.55 , pp. 162-168
    • Newhall, W.J.V.1
  • 23
    • 33646926111 scopus 로고    scopus 로고
    • Differential expression and sequence conservation of the Anaplasma marginale msp2 gene superfamily outer membrane proteins
    • Noh, S. M., K. A. Brayton, D. P. Knowles, J. T. Agnes, M. J. Dark, W. C. Brown, T. V. Baszler, and G. H. Palmer. 2006. Differential expression and sequence conservation of the Anaplasma marginale msp2 gene superfamily outer membrane proteins. Infect. Immun. 74:3471-3479.
    • (2006) Infect. Immun , vol.74 , pp. 3471-3479
    • Noh, S.M.1    Brayton, K.A.2    Knowles, D.P.3    Agnes, J.T.4    Dark, M.J.5    Brown, W.C.6    Baszler, T.V.7    Palmer, G.H.8
  • 26
    • 0030743650 scopus 로고    scopus 로고
    • Immunization with an acellular vaccine consisting of the outer membrane complex of Chlamydia trachomatis induces protection against a genital challenge
    • Pal, S., I. Theodor, E. M. Peterson, and L. M. de la Maza. 1997. Immunization with an acellular vaccine consisting of the outer membrane complex of Chlamydia trachomatis induces protection against a genital challenge. Infect. Immun. 65:3361-3369.
    • (1997) Infect. Immun , vol.65 , pp. 3361-3369
    • Pal, S.1    Theodor, I.2    Peterson, E.M.3    de la Maza, L.M.4
  • 27
    • 0022461701 scopus 로고
    • Immunization with an isolate-common surface protein protects cattle against anaplasmosis
    • Palmer, G. H., A. F. Barbet, W. C. Davis, and T. C. McGuire. 1986. Immunization with an isolate-common surface protein protects cattle against anaplasmosis. Science 231:1299-1302.
    • (1986) Science , vol.231 , pp. 1299-1302
    • Palmer, G.H.1    Barbet, A.F.2    Davis, W.C.3    McGuire, T.C.4
  • 28
    • 0021269520 scopus 로고
    • Immune serum against Anaplasma marginale initial bodies neutralizes infectivity for cattle
    • Palmer, G. H., and T. C. McGuire. 1984. Immune serum against Anaplasma marginale initial bodies neutralizes infectivity for cattle. J. Immunol. 133: 1010-1015.
    • (1984) J. Immunol , vol.133 , pp. 1010-1015
    • Palmer, G.H.1    McGuire, T.C.2
  • 29
    • 0027981121 scopus 로고
    • Heterologous strain challenge of cattle immunized with Anaplasma marginale outer membranes
    • Palmer, G. H., D. Munodzana, N. Tebele, T. Ushe, and T. F. McElwain. 1994. Heterologous strain challenge of cattle immunized with Anaplasma marginale outer membranes. Vet. Immunol. Immunopathol. 42:265-273.
    • (1994) Vet. Immunol. Immunopathol , vol.42 , pp. 265-273
    • Palmer, G.H.1    Munodzana, D.2    Tebele, N.3    Ushe, T.4    McElwain, T.F.5
  • 30
    • 0035122645 scopus 로고    scopus 로고
    • Strain composition of the ehrlichia Anaplasma marginale within persistently infected cattle, a mammalian reservoir for tick transmission
    • Palmer, G. H., F. R. Rurangirwa, and T. F. McElwain. 2001. Strain composition of the ehrlichia Anaplasma marginale within persistently infected cattle, a mammalian reservoir for tick transmission. J. Clin. Microbiol. 39: 631-635.
    • (2001) J. Clin. Microbiol , vol.39 , pp. 631-635
    • Palmer, G.H.1    Rurangirwa, F.R.2    McElwain, T.F.3
  • 31
    • 3042849127 scopus 로고    scopus 로고
    • Characterization of lymphocyte subpopulations and major histocompatibility complex haplotypes of mastitis-resistant and susceptible cows
    • Park, Y. H., Y. S. Joo, J. Y. Park, J. S. Moon, S. H. Kim, N. H. Kwon, J. S. Ahn, W. C. Davis, and C. J. Davies. 2004. Characterization of lymphocyte subpopulations and major histocompatibility complex haplotypes of mastitis-resistant and susceptible cows. J. Vet. Sci. 5:29-39.
    • (2004) J. Vet. Sci , vol.5 , pp. 29-39
    • Park, Y.H.1    Joo, Y.S.2    Park, J.Y.3    Moon, J.S.4    Kim, S.H.5    Kwon, N.H.6    Ahn, J.S.7    Davis, W.C.8    Davies, C.J.9
  • 32
    • 33646083005 scopus 로고    scopus 로고
    • Effect of different hapten-carrier conjugation ratios and molecular orientations on antibody affinity against a peptide antigen
    • Pedersen, M. K., N. S. Sorensen, P. M. Heegaard, N. H. Beyer, and L. Bruun. 2006. Effect of different hapten-carrier conjugation ratios and molecular orientations on antibody affinity against a peptide antigen. J. Immunol. Methods 311:198-206.
    • (2006) J. Immunol. Methods , vol.311 , pp. 198-206
    • Pedersen, M.K.1    Sorensen, N.S.2    Heegaard, P.M.3    Beyer, N.H.4    Bruun, L.5
  • 33
    • 32944462721 scopus 로고    scopus 로고
    • Bacterial adhesion and entry into host cells
    • Pizarro-Cerda, J., and P. Cossart. 2006. Bacterial adhesion and entry into host cells. Cell 124:715-727.
    • (2006) Cell , vol.124 , pp. 715-727
    • Pizarro-Cerda, J.1    Cossart, P.2
  • 34
    • 34249668763 scopus 로고    scopus 로고
    • Conservation of transmission phenotype of Anaplasma marginale (Rickettsiales: Anaplasmataceae) strains among Dermacentor and Rhipicephalus ticks (Acari: Ixodidae)
    • Scoles, G. A., M. W. Ueti, S. M. Noh, D. P. Knowles, and G. H. Palmer. 2007. Conservation of transmission phenotype of Anaplasma marginale (Rickettsiales: Anaplasmataceae) strains among Dermacentor and Rhipicephalus ticks (Acari: Ixodidae). J. Med. Entomol. 44:484-491.
    • (2007) J. Med. Entomol , vol.44 , pp. 484-491
    • Scoles, G.A.1    Ueti, M.W.2    Noh, S.M.3    Knowles, D.P.4    Palmer, G.H.5
  • 35
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • Shevchenko, A., M. Wilm, O. Vorm, and M. Mann. 1996. Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal. Chem. 68: 850-858.
    • (1996) Anal. Chem , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 36
    • 0025800571 scopus 로고
    • Induction of protective immunity by using Anaplasma marginale initial body membranes
    • Tebele, N., T. C. McGuire, and G. H. Palmer. 1991. Induction of protective immunity by using Anaplasma marginale initial body membranes. Infect. Immun. 59:3199-3204.
    • (1991) Infect. Immun , vol.59 , pp. 3199-3204
    • Tebele, N.1    McGuire, T.C.2    Palmer, G.H.3
  • 37
    • 0027029189 scopus 로고
    • Extensive polymorphism of the BoLA-DRB3 gene distinguished by PCR-RFLP
    • Van Ejjk, M. J., A. Stewart-Haynes, and H. A. Lewin. 1992. Extensive polymorphism of the BoLA-DRB3 gene distinguished by PCR-RFLP. Anim. Genet. 23:483-496.
    • (1992) Anim. Genet , vol.23 , pp. 483-496
    • Van Ejjk, M.J.1    Stewart-Haynes, A.2    Lewin, H.A.3
  • 38
    • 0028241842 scopus 로고    scopus 로고
    • Vidotto, M. C., T. C. McGuire, T. F. McElwain, G. H. Palmer, and D. P. Knowles, Jr. 1994. Intermolecular relationships of major surface proteins of Anaplasma marginale. Infect. Immun. 62:2940-2946.
    • Vidotto, M. C., T. C. McGuire, T. F. McElwain, G. H. Palmer, and D. P. Knowles, Jr. 1994. Intermolecular relationships of major surface proteins of Anaplasma marginale. Infect. Immun. 62:2940-2946.
  • 39
    • 33746852673 scopus 로고    scopus 로고
    • Identification of a protein complex that assembles lipopolysaccharide in the outer membrane of Escherichia coli
    • Wu, T., A. C. McCandlish, L. S. Gronenberg, S. S. Chng, T. J. Silhavy, and D. Kahne. 2006. Identification of a protein complex that assembles lipopolysaccharide in the outer membrane of Escherichia coli. Proc. Natl. Acad. Sci. USA 103:11754-11759.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 11754-11759
    • Wu, T.1    McCandlish, A.C.2    Gronenberg, L.S.3    Chng, S.S.4    Silhavy, T.J.5    Kahne, D.6
  • 40
    • 17644403146 scopus 로고    scopus 로고
    • Characterization of the disulfide bonds and free cysteine residues of the Chlamydia trachomatis mouse pneumonitis major outer membrane protein
    • Yen, T. Y., S. Pal, and L. M. de la Maza. 2005. Characterization of the disulfide bonds and free cysteine residues of the Chlamydia trachomatis mouse pneumonitis major outer membrane protein. Biochemistry 44:6250-6256.
    • (2005) Biochemistry , vol.44 , pp. 6250-6256
    • Yen, T.Y.1    Pal, S.2    de la Maza, L.M.3


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