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Volumn 76, Issue 24, 2002, Pages 12646-12653

Identification of immunogenic hot spots within plum pox potyvirus capsid protein for efficient antigen presentation

Author keywords

[No Author keywords available]

Indexed keywords

CAPSID PROTEIN; VIRUS ANTIGEN;

EID: 0036891845     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.76.24.12646-12653.2002     Document Type: Article
Times cited : (31)

References (43)
  • 1
    • 0022408763 scopus 로고
    • Biochemical analysis of the capsid protein gene and capsid protein of tobacco etch virus: N-terminal amino acids are located on the virion's surface
    • Allison, R. F., W. G. Dougherty, T. D. Parks, J. Willis, R. E. Johnston, M. E. Kelly, and F. B. Armstrong. 1985. Biochemical analysis of the capsid protein gene and capsid protein of tobacco etch virus: N-terminal amino acids are located on the virion's surface. Virology 147:309-316.
    • (1985) Virology , vol.147 , pp. 309-316
    • Allison, R.F.1    Dougherty, W.G.2    Parks, T.D.3    Willis, J.4    Johnston, R.E.5    Kelly, M.E.6    Armstrong, F.B.7
  • 2
    • 0030934661 scopus 로고    scopus 로고
    • High-tech herbal medicine: Plant-based vaccines
    • Arntzen, C. J. 1997. High-tech herbal medicine: Plant-based vaccines. Nat. Biotechnol. 15:221-222.
    • (1997) Nat. Biotechnol. , vol.15 , pp. 221-222
    • Arntzen, C.J.1
  • 3
    • 0002186442 scopus 로고
    • Academic Press, New York, N.Y.
    • Atherton, E., and R. D. Sheppard. 1987. Peptides, vol. 9, p. 1-38. Academic Press, New York, N.Y.
    • (1987) Peptides , vol.9 , pp. 1-38
    • Atherton, E.1    Sheppard, R.D.2
  • 4
    • 0025141014 scopus 로고
    • A point mutation in the coat protein abolishes aphid transmissibility of a potyvirus
    • Atreya, C. D., B. Raccah, and T. D. Pirone. 1990. A point mutation in the coat protein abolishes aphid transmissibility of a potyvirus. Virology 178: 161-165.
    • (1990) Virology , vol.178 , pp. 161-165
    • Atreya, C.D.1    Raccah, B.2    Pirone, T.D.3
  • 5
    • 0025867217 scopus 로고
    • Amino acid substitutions in the coat protein results in loss of insect transmissibility of a plant virus
    • Atreya, P. L., C. D. Atreya, and T. P. Pirone. 1991. Amino acid substitutions in the coat protein results in loss of insect transmissibility of a plant virus. Proc. Natl. Acad. Sci. USA 88:7887-7891.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 7887-7891
    • Atreya, P.L.1    Atreya, C.D.2    Pirone, T.P.3
  • 6
    • 0027215357 scopus 로고
    • Serological diagnosis of feline immunodeficiency virus infection based on synthetic peptides from Env glycoproteins
    • Avrameas, A., A. D. Strosberg, A. Moraillon, P. Sonigo, and G. Pancino. 1993. Serological diagnosis of feline immunodeficiency virus infection based on synthetic peptides from Env glycoproteins. Res. Virol. 144:209-218.
    • (1993) Res. Virol. , vol.144 , pp. 209-218
    • Avrameas, A.1    Strosberg, A.D.2    Moraillon, A.3    Sonigo, P.4    Pancino, G.5
  • 8
    • 0028856089 scopus 로고
    • Peptide vaccine against canine parvovirus: Identification of two neutralization subsites in the N terminus of VP2 and optimization of the amino acid sequence
    • Casal, J. L, J. P. M. Langeveld, E. Cortés, W. W. M. Schaaper, E. van Dijk, C. Vela, S. Kamstrup, and R. H. Meloen. 1995. Peptide vaccine against canine parvovirus: Identification of two neutralization subsites in the N terminus of VP2 and optimization of the amino acid sequence. J. Virol. 69:7274-7277.
    • (1995) J. Virol. , vol.69 , pp. 7274-7277
    • Casal, J.L.1    Langeveld, J.P.M.2    Cortés, E.3    Schaaper, W.W.M.4    Van Dijk, E.5    Vela, C.6    Kamstrup, S.7    Meloen, R.H.8
  • 11
    • 0028288188 scopus 로고
    • Distinct functions of capsid protein in assembly and movement of tobacco etch potyvirus in plants
    • Dolja, V. V., R. Haldeman, N. L. Robertson, W. G. Dougherty, and J. C. Carrington. 1994. Distinct functions of capsid protein in assembly and movement of tobacco etch potyvirus in plants. EMBO J. 13:1482-1491.
    • (1994) EMBO J. , vol.13 , pp. 1482-1491
    • Dolja, V.V.1    Haldeman, R.2    Robertson, N.L.3    Dougherty, W.G.4    Carrington, J.C.5
  • 12
    • 0028895609 scopus 로고
    • Capsid protein determinants involved in cell-to-cell and long distance movement of tobacco etch potyvirus
    • Dolja, V. V., R. Haldeman-Cahill, A. E. Montgomery, K. A. Vandenbosch, and J. C. Carrington. 1995. Capsid protein determinants involved in cell-to-cell and long distance movement of tobacco etch potyvirus. Virology 206: 1007-1016.
    • (1995) Virology , vol.206 , pp. 1007-1016
    • Dolja, V.V.1    Haldeman-Cahill, R.2    Montgomery, A.E.3    Vandenbosch, K.A.4    Carrington, J.C.5
  • 14
    • 0029087838 scopus 로고
    • Plant virus expressing hybrid coat protein with added murine epitope elicits autoantibody response
    • Fitchen, J., R. N. Beachy, and M. B. Hein. 1995. Plant virus expressing hybrid coat protein with added murine epitope elicits autoantibody response. Vaccine 13:1051-1057.
    • (1995) Vaccine , vol.13 , pp. 1051-1057
    • Fitchen, J.1    Beachy, R.N.2    Hein, M.B.3
  • 15
    • 0026656122 scopus 로고
    • Spot-synthesis: An easy technique for the positionally addressable, parallel chemical synthesis on a membrane support
    • Frank, R. 1992. Spot-synthesis: An easy technique for the positionally addressable, parallel chemical synthesis on a membrane support. Tetrahedron 48:9217-9232.
    • (1992) Tetrahedron , vol.48 , pp. 9217-9232
    • Frank, R.1
  • 16
    • 0030329981 scopus 로고    scopus 로고
    • SPOT synthesis. Epitope analysis with arrays of synthetic peptides prepared on cellulose membranes
    • Frank, R., and H. Overwin. 1996. SPOT synthesis. Epitope analysis with arrays of synthetic peptides prepared on cellulose membranes. Methods Mol. Biol. 66:149-169.
    • (1996) Methods Mol. Biol. , vol.66 , pp. 149-169
    • Frank, R.1    Overwin, H.2
  • 17
    • 0026633058 scopus 로고
    • Proteolytic processing of the plum pox potyvirus polyprotein by the NIa protease at a novel cleavage site
    • Garcia, J. A., M. T. Martín, M. T. Cervera, and J. L. Riechmann. 1992. Proteolytic processing of the plum pox potyvirus polyprotein by the NIa protease at a novel cleavage site. Virology 188:697-703.
    • (1992) Virology , vol.188 , pp. 697-703
    • Garcia, J.A.1    Martín, M.T.2    Cervera, M.T.3    Riechmann, J.L.4
  • 18
    • 0022977872 scopus 로고
    • Development of a genetically-engineered, candidate polio vaccine employing the self-assembling properties of the tobacco mosaic virus coat protein
    • Haynes, J. R., J. Cunningham, A. von Seefried, M. Lennick, R. T. Garvin, and S.-H. Shen. 1986. Development of a genetically-engineered, candidate polio vaccine employing the self-assembling properties of the tobacco mosaic virus coat protein. Biotechnology 4:637-641.
    • (1986) Biotechnology , vol.4 , pp. 637-641
    • Haynes, J.R.1    Cunningham, J.2    Von Seefried, A.3    Lennick, M.4    Garvin, R.T.5    Shen, S.-H.6
  • 19
    • 0025063721 scopus 로고
    • A general and rapid mutagenesis method using polymerase chain reaction
    • Herlitze, S., and M. Koenen. 1990. A general and rapid mutagenesis method using polymerase chain reaction. Gene 91:143-147.
    • (1990) Gene , vol.91 , pp. 143-147
    • Herlitze, S.1    Koenen, M.2
  • 21
    • 0030793945 scopus 로고    scopus 로고
    • Presentation of heterologous peptides on plant viruses: Genetics, structure, and function
    • Johnson, J., T. Lin, and G. Lomonossoff. 1997. Presentation of heterologous peptides on plant viruses: Genetics, structure, and function. Annu. Rev. Phytopathol. 35:67-86.
    • (1997) Annu. Rev. Phytopathol. , vol.35 , pp. 67-86
    • Johnson, J.1    Lin, T.2    Lomonossoff, G.3
  • 22
    • 0035925697 scopus 로고    scopus 로고
    • The green revolution: Plants as heterologous expression vectors
    • Koprowski, H., and V. Yusibov. 2001. The green revolution: Plants as heterologous expression vectors. Vaccine 19:2735-2741.
    • (2001) Vaccine , vol.19 , pp. 2735-2741
    • Koprowski, H.1    Yusibov, V.2
  • 23
    • 0024677913 scopus 로고
    • The complete nucleotide sequence of plum pox potyvirus RNA
    • Laín, S., J. L. Riechmann, and J. A. García. 1989. The complete nucleotide sequence of plum pox potyvirus RNA. Virus Res. 13:157-172.
    • (1989) Virus Res. , vol.13 , pp. 157-172
    • Laín, S.1    Riechmann, J.L.2    García, J.A.3
  • 24
    • 0000624742 scopus 로고
    • Nucleotide sequence of the 3′ terminal region of plum pox potyvirus RNA
    • Laín, S., J. L. Riechmann, E. Méndez, and J. A. García. 1988. Nucleotide sequence of the 3′ terminal region of plum pox potyvirus RNA. Virus Res. 10:325-342.
    • (1988) Virus Res. , vol.10 , pp. 325-342
    • Laín, S.1    Riechmann, J.L.2    Méndez, E.3    García, J.A.4
  • 27
    • 0029122424 scopus 로고
    • Transmission by aphids of a naturally non-transmissible plum pox virus isolate with the aid of potato virus Y helper component
    • López-Moya, J. J., T. Canto, J. R. Díaz-Ruíz, and D. López-Abella. 1995. Transmission by aphids of a naturally non-transmissible plum pox virus isolate with the aid of potato virus Y helper component. J. Gen. Virol. 76:2293-2297.
    • (1995) J. Gen. Virol. , vol.76 , pp. 2293-2297
    • López-Moya, J.J.1    Canto, T.2    Díaz-Ruíz, J.R.3    López-Abella, D.4
  • 28
    • 0034631736 scopus 로고    scopus 로고
    • Construction of a stable and highly infectious intron-containing cDNA clone of plum pox potyvirus, and its use to infect plants by particle bombardment
    • López-Moya, J. J., and J. A. García. 2000. Construction of a stable and highly infectious intron-containing cDNA clone of plum pox potyvirus, and its use to infect plants by particle bombardment. Virus Res. 68:99-107.
    • (2000) Virus Res. , vol.68 , pp. 99-107
    • López-Moya, J.J.1    García, J.A.2
  • 29
    • 0026587042 scopus 로고
    • Infectious in vivo transcripts of a plum pox potyvirus full-length cDNA clone containing the cauliflower mosaic virus 35S RNA promoter
    • Maiss, E., U. Timpe, A. Briske-Rode, D.-E. Leseman, and R. Casper. 1992. Infectious in vivo transcripts of a plum pox potyvirus full-length cDNA clone containing the cauliflower mosaic virus 35S RNA promoter. J. Gen. Virol. 73:709-713.
    • (1992) J. Gen. Virol. , vol.73 , pp. 709-713
    • Maiss, E.1    Timpe, U.2    Briske-Rode, A.3    Leseman, D.-E.4    Casper, R.5
  • 30
    • 0034881226 scopus 로고    scopus 로고
    • Chimeric plant virus particles as immunogens for inducing murine and human immune responses against human immunodeficiency virus type 1
    • Marusic, C., P. Rizza, L. Lattanzi, C. Mancini, M. Spada, F. Belardelli, E. Benvenuto, and I. Capone. 2001. Chimeric plant virus particles as immunogens for inducing murine and human immune responses against human immunodeficiency virus type 1. J. Virol. 75.8434-8439.
    • (2001) J. Virol. , vol.75 , pp. 8434-8439
    • Marusic, C.1    Rizza, P.2    Lattanzi, L.3    Mancini, C.4    Spada, M.5    Belardelli, F.6    Benvenuto, E.7    Capone, I.8
  • 31
    • 0029828898 scopus 로고    scopus 로고
    • The development of cowpea mosaic virus as a potential source of novel vaccines
    • Porta, C., V. E. Spall, T. Lin, J. E. Johnson, and G. P. Lomonossoff. 1996. The development of cowpea mosaic virus as a potential source of novel vaccines. Intervirology 39:79-84.
    • (1996) Intervirology , vol.39 , pp. 79-84
    • Porta, C.1    Spall, V.E.2    Lin, T.3    Johnson, J.E.4    Lomonossoff, G.P.5
  • 32
    • 0032949311 scopus 로고    scopus 로고
    • New advances in understanding the molecular biology of plant/potyvirus interactions
    • Revers, F., O. Le Gall, T. Candresse, and A. Maule. 1999. New advances in understanding the molecular biology of plant/potyvirus interactions. Mol. Plant-Microbe Interact. 12:366-376.
    • (1999) Mol. Plant-Microbe Interact. , vol.12 , pp. 366-376
    • Revers, F.1    Le Gall, O.2    Candresse, T.3    Maule, A.4
  • 33
    • 0026573174 scopus 로고
    • Highlights and prospects of potyvirus molecular biology
    • Riechmann, J. L., S. Laín, and J. A. García. 1992. Highlights and prospects of potyvirus molecular biology. J. Gen. Virol. 73:1-16.
    • (1992) J. Gen. Virol. , vol.73 , pp. 1-16
    • Riechmann, J.L.1    Laín, S.2    García, J.A.3
  • 34
    • 0025357661 scopus 로고
    • Infectious in vitro transcripts from a plum pox potyvirus cDNA clone
    • Riechmann, J. L., S. Laín, and J. A. García. 1990. Infectious in vitro transcripts from a plum pox potyvirus cDNA clone. Virology 177:710-716.
    • (1990) Virology , vol.177 , pp. 710-716
    • Riechmann, J.L.1    Laín, S.2    García, J.A.3
  • 35
    • 0033543951 scopus 로고    scopus 로고
    • Minor displacements in the insertion site provoke major differences in the induction of antibody responses by chimeric parvovirus-like particles
    • Rueda, P., A. Hurtado, M. del Barrio, J. L. Martinez-Torrecuadrada, S. Kamstrup, C. Leclerc, and J. I. Casal. 1999. Minor displacements in the insertion site provoke major differences in the induction of antibody responses by chimeric parvovirus-like particles. Virology 263:89-99.
    • (1999) Virology , vol.263 , pp. 89-99
    • Rueda, P.1    Hurtado, A.2    Del Barrio, M.3    Martinez-Torrecuadrada, J.L.4    Kamstrup, S.5    Leclerc, C.6    Casal, J.I.7
  • 36
    • 0001595002 scopus 로고
    • The N and C termini of the coat proteins of potyviruses are surface-located and the N-terminus contains the major virus-specific epitopes
    • Shukla, D. D., P. M. Strike, S. L. Tracy, K. H. Gough, and C. W. Ward. 1988. The N and C termini of the coat proteins of potyviruses are surface-located and the N-terminus contains the major virus-specific epitopes. J. Gen. Virol. 69:1497-1508.
    • (1988) J. Gen. Virol. , vol.69 , pp. 1497-1508
    • Shukla, D.D.1    Strike, P.M.2    Tracy, S.L.3    Gough, K.H.4    Ward, C.W.5
  • 38
    • 0028800716 scopus 로고
    • Systemic production of foreign peptides on the particle surface of tobacco mosaic virus
    • Sugiyama, Y., H. Hamamato, S. Takemoto, Y. Watanabe, and Y. Okada. 1995. Systemic production of foreign peptides on the particle surface of tobacco mosaic virus. FEBS Lett. 359:247-250.
    • (1995) FEBS Lett. , vol.359 , pp. 247-250
    • Sugiyama, Y.1    Hamamato, H.2    Takemoto, S.3    Watanabe, Y.4    Okada, Y.5
  • 39
    • 0034099316 scopus 로고    scopus 로고
    • Influence of three-dimensional structure on the immunogenicity of a peptide expressed on the surface of a plant virus
    • Taylor, K. M., T. Lin, C. Porta, A. G. Mosser, H. A. Giesing, G. P. Lomonossoff, and J. E. Johnson. 2000. Influence of three-dimensional structure on the immunogenicity of a peptide expressed on the surface of a plant virus. J. Mol. Recognit. 13:71-82.
    • (2000) J. Mol. Recognit. , vol.13 , pp. 71-82
    • Taylor, K.M.1    Lin, T.2    Porta, C.3    Mosser, A.G.4    Giesing, H.A.5    Lomonossoff, G.P.6    Johnson, J.E.7


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