메뉴 건너뛰기




Volumn 118, Issue SEPT., 2003, Pages 115-124

Expression & immunogenicity of malaria merozoite peptides displayed on the small coat protein of chimaeric cowpea mosaic virus

Author keywords

Antigenicity; Cowpea mosaic virus; Immunogenicity; Malaria; Peptide epitope; Plasmodium falciparum viral peptide display

Indexed keywords

ANTIBODY; ANTIGEN; ANTISERUM; COAT PROTEIN; EPITOPE; MALARIA VACCINE; PEPTIDE; VIRUS VECTOR;

EID: 0346266176     PISSN: 09715916     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (12)

References (31)
  • 1
    • 0022503821 scopus 로고
    • A poliovirus neutralisation epitope expressed on hybrid hepatitis B surface antigen particles
    • Delpeyroux F, Chenciner N, Lim A, Malpiece T, Blondel B, Crainic R, et al. A poliovirus neutralisation epitope expressed on hybrid hepatitis B surface antigen particles. Science 1986; 233 : 472-5.
    • (1986) Science , vol.233 , pp. 472-475
    • Delpeyroux, F.1    Chenciner, N.2    Lim, A.3    Malpiece, T.4    Blondel, B.5    Crainic, R.6
  • 2
    • 0023546339 scopus 로고
    • Improved immunogenicity of a peptide epitope after fusion to hepatitis B core protein
    • Clarke BE, Newton SE, Carrol AR, Francis MJ, Appleyard G, Syred A, et al. Improved immunogenicity of a peptide epitope after fusion to hepatitis B core protein. Nature 1987; 330 : 381-4.
    • (1987) Nature , vol.330 , pp. 381-384
    • Clarke, B.E.1    Newton, S.E.2    Carrol, A.R.3    Francis, M.J.4    Appleyard, G.5    Syred, A.6
  • 3
    • 0025933214 scopus 로고
    • The synthesis and structure of comovirus capsids
    • Lomonossoff GP, Johnson JE. The synthesis and structure of comovirus capsids. Prog Biophys Mol Biol 1991; 55 : 107-37.
    • (1991) Prog Biophys Mol Biol , vol.55 , pp. 107-137
    • Lomonossoff, G.P.1    Johnson, J.E.2
  • 4
    • 0029921999 scopus 로고    scopus 로고
    • Use of macromolecular assemblies as expression systems for peptides and synthetic vaccines
    • Lomonossoff GP, Johnson JE. Use of macromolecular assemblies as expression systems for peptides and synthetic vaccines. Curr Opin Struct Biol 1996; 6 : 176-82.
    • (1996) Curr Opin Struct Biol , vol.6 , pp. 176-182
    • Lomonossoff, G.P.1    Johnson, J.E.2
  • 5
    • 0027514862 scopus 로고
    • Expression of an animal virus antigenic site on the surface of a plant virus particle
    • Usha R, Rohll JB, Spall VE, Shanks M, Maule AJ, Johnson JE et al. Expression of an animal virus antigenic site on the surface of a plant virus particle. Virology 1993; 197 : 366-74.
    • (1993) Virology , vol.197 , pp. 366-374
    • Usha, R.1    Rohll, J.B.2    Spall, V.E.3    Shanks, M.4    Maule, A.J.5    Johnson, J.E.6
  • 6
    • 0030175998 scopus 로고    scopus 로고
    • Stimulation of neutralising antibodies to human immunodeficiency virus type 1 in three strains of mice immunised with a 22 amino acid peptide of gp41 expressed on the surface of a plant virus
    • McLain L, Durrani Z, Wisniewski LA, Porta C, Lomonossoff GP, Dimmock NJ. Stimulation of neutralising antibodies to human immunodeficiency virus type 1 in three strains of mice immunised with a 22 amino acid peptide of gp41 expressed on the surface of a plant virus. Vaccine 1996; 14 : 799-810.
    • (1996) Vaccine , vol.14 , pp. 799-810
    • McLain, L.1    Durrani, Z.2    Wisniewski, L.A.3    Porta, C.4    Lomonossoff, G.P.5    Dimmock, N.J.6
  • 7
    • 0028122633 scopus 로고
    • Development of cowpea mosaic virus as a high-yielding system for the presentation of foreign peptides
    • Porta C, Spall VE, Loveland J, Johnson JE, Barker PJ, Lomonossoff GP. Development of cowpea mosaic virus as a high-yielding system for the presentation of foreign peptides. Virology 1994; 202 : 949-55.
    • (1994) Virology , vol.202 , pp. 949-955
    • Porta, C.1    Spall, V.E.2    Loveland, J.3    Johnson, J.E.4    Barker, P.J.5    Lomonossoff, G.P.6
  • 10
    • 9044237688 scopus 로고    scopus 로고
    • A recombinant baculovirus 42-kilodalton C-terminal fragment of Plasmodium falciparum merozoite surface protein 1 protects Aotus monkeys against malaria
    • Chang SP, Case SE, Gosnell WL, Hashimoto A, Kramer KJ, Tam LQ, et al. A recombinant baculovirus 42-kilodalton C-terminal fragment of Plasmodium falciparum merozoite surface protein 1 protects Aotus monkeys against malaria. Infect Immun 1996; 64 : 253-61.
    • (1996) Infect Immun , vol.64 , pp. 253-261
    • Chang, S.P.1    Case, S.E.2    Gosnell, W.L.3    Hashimoto, A.4    Kramer, K.J.5    Tam, L.Q.6
  • 11
    • 0023028535 scopus 로고
    • Immunisation with synthetic peptides of a Plasmodium falciparum surface antigen induces antimerozoite antibodies
    • Cheung A, Leban J, Shaw AR, Merkli B, Stocker J, Chizzolini C, et al. Immunisation with synthetic peptides of a Plasmodium falciparum surface antigen induces antimerozoite antibodies. Proc Natl Acad Sci USA 1986; 83 : 8328-32.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 8328-8332
    • Cheung, A.1    Leban, J.2    Shaw, A.R.3    Merkli, B.4    Stocker, J.5    Chizzolini, C.6
  • 12
    • 0022360581 scopus 로고
    • Primary structure of the precursor to the three major surface antigens of Plasmodium falciparum merozoites
    • Holder AA, Lockyer MJ, Odink KG, Sandhu JS, Riveros-Moreno V, Nicholls SC, et al. Primary structure of the precursor to the three major surface antigens of Plasmodium falciparum merozoites. Nature 1985; 317 : 270-3.
    • (1985) Nature , vol.317 , pp. 270-273
    • Holder, A.A.1    Lockyer, M.J.2    Odink, K.G.3    Sandhu, J.S.4    Riveros-Moreno, V.5    Nicholls, S.C.6
  • 13
    • 0028290381 scopus 로고
    • Antibodies to epitopes on merozoite and sporozoite surface antigens as serologic markers of malaria transmission: Studies at a site in the dry zone of Sri Lanka
    • Ramasamy R, Nagendran K, Ramasamy MS. Antibodies to epitopes on merozoite and sporozoite surface antigens as serologic markers of malaria transmission: Studies at a site in the dry zone of Sri Lanka. Am J Trop Med Hyg 1994; 50 : 537-47.
    • (1994) Am J Trop Med Hyg , vol.50 , pp. 537-547
    • Ramasamy, R.1    Nagendran, K.2    Ramasamy, M.S.3
  • 15
    • 0028023529 scopus 로고
    • Analysis of human T cell clones specific for conserved peptide sequences within malaria proteins-paucity of clones responsive to intact parasites
    • Quakyi IA, Currier J, Fell A, Taylor DW, Roberts T, Houghten RA, et al. Analysis of human T cell clones specific for conserved peptide sequences within malaria proteins-paucity of clones responsive to intact parasites. J Immunol 1994; 153 : 2082-92.
    • (1994) J Immunol , vol.153 , pp. 2082-2092
    • Quakyi, I.A.1    Currier, J.2    Fell, A.3    Taylor, D.W.4    Roberts, T.5    Houghten, R.A.6
  • 16
    • 0028925869 scopus 로고
    • Antibody and clinical responses in volunteers to immunisation with malaria peptide-diphtheria toxoid conjugates
    • Ramasamy R, Wijesundere DA, Nagendran K, Ramasamy MS. Antibody and clinical responses in volunteers to immunisation with malaria peptide-diphtheria toxoid conjugates. Clin Exp Immunol 1995; 99 : 168-74.
    • (1995) Clin Exp Immunol , vol.99 , pp. 168-174
    • Ramasamy, R.1    Wijesundere, D.A.2    Nagendran, K.3    Ramasamy, M.S.4
  • 17
    • 0027241045 scopus 로고
    • Analysis of sequence diversity in the Plasmodium falciparum merozoite surface protein-1 (MSP-1)
    • Miller LH, Roberts T, Shahabuddin M, McCutchan TF. Analysis of sequence diversity in the Plasmodium falciparum merozoite surface protein-1 (MSP-1). Mol Biochem Parasitol 1993; 59 : 1-14.
    • (1993) Mol Biochem Parasitol , vol.59 , pp. 1-14
    • Miller, L.H.1    Roberts, T.2    Shahabuddin, M.3    McCutchan, T.F.4
  • 18
    • 0025797365 scopus 로고
    • Primary structure of the merozoite surface antigen 1 of Plasmodium vivax reveals sequences conserved between different Plasmodium species
    • Del Portillo HA, Longacre S, Khouri E, David PH. Primary structure of the merozoite surface antigen 1 of Plasmodium vivax reveals sequences conserved between different Plasmodium species. Proc Natl Acad Sci USA 1991; 88 : 4030-4.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 4030-4034
    • Del Portillo, H.A.1    Longacre, S.2    Khouri, E.3    David, P.H.4
  • 19
    • 0027297890 scopus 로고
    • Cauliflower mosaic virus 35S promoter-controlled DNA copies of cowpea mosaic virus RNAs are infectious on plants
    • Dessens JT, Lomonossoff GP. Cauliflower mosaic virus 35S promoter-controlled DNA copies of cowpea mosaic virus RNAs are infectious on plants. J Gen Virol 1993; 74 : 889-92.
    • (1993) J Gen Virol , vol.74 , pp. 889-892
    • Dessens, J.T.1    Lomonossoff, G.P.2
  • 20
    • 0014077979 scopus 로고
    • Purification and properties of the components of cowpea mosaic virus
    • Van Kammen A. Purification and properties of the components of cowpea mosaic virus. Virology 1967; 31 : 633-42.
    • (1967) Virology , vol.31 , pp. 633-642
    • Van Kammen, A.1
  • 22
    • 0003448569 scopus 로고
    • New York : Cold Spring Harbor Laboratory Press, Cold Spring Harbor
    • Harlow ED, David L. Using Antibodies: A Laboratory Manual. New York : Cold Spring Harbor Laboratory Press, Cold Spring Harbor; 1989; p. 574-585.
    • (1989) Using Antibodies: A Laboratory Manual , pp. 574-585
    • Harlow, E.D.1    David, L.2
  • 23
    • 0032898740 scopus 로고    scopus 로고
    • Model multiple antigenic and homopolymeric peptides from non-repetitive sequences of malaria merozoite proteins elicit biologically irrelevant antibodies
    • Ramasamy R, Kanagaratnam R, Chandanie PD, Kulachelvy K, Ramasamy MS, Dharmasena PM. Model multiple antigenic and homopolymeric peptides from non-repetitive sequences of malaria merozoite proteins elicit biologically irrelevant antibodies. Biochim Biophys Acta 1999; 1453 : 115-25.
    • (1999) Biochim Biophys Acta , vol.1453 , pp. 115-125
    • Ramasamy, R.1    Kanagaratnam, R.2    Chandanie, P.D.3    Kulachelvy, K.4    Ramasamy, M.S.5    Dharmasena, P.M.6
  • 24
    • 0033102432 scopus 로고    scopus 로고
    • The cleavable carboxyl-terminus of the small coat protein of cowpea mosaic virus is involved in RNA encapsidation
    • Tayler KM, Spall VE, Butler PJG, Lomonossoff GP. The cleavable carboxyl-terminus of the small coat protein of cowpea mosaic virus is involved in RNA encapsidation. Virology 1999; 255 : 129-37.
    • (1999) Virology , vol.255 , pp. 129-137
    • Tayler, K.M.1    Spall, V.E.2    Butler, P.J.G.3    Lomonossoff, G.P.4
  • 25
    • 0023472689 scopus 로고
    • Studies on glycoproteins in the human malaria parasite Plasmodium falciparum. Identification of a myristilated 45kDa merozoite membrane glycoprotein
    • Ramasamy R. Studies on glycoproteins in the human malaria parasite Plasmodium falciparum. Identification of a myristilated 45kDa merozoite membrane glycoprotein. Immunol Cell Biol 1987; 65 : 419-24.
    • (1987) Immunol Cell Biol , vol.65 , pp. 419-424
    • Ramasamy, R.1
  • 26
    • 0033043930 scopus 로고    scopus 로고
    • Position dependent processing of peptides presented on the surface of cowpea mosaic virus
    • Taylor KM, Porta C, Lin T, Johnson JE, Barker PJ, Lomonossoff G.P. Position dependent processing of peptides presented on the surface of cowpea mosaic virus. Biol Chem 1999; 380 : 387-92.
    • (1999) Biol Chem , vol.380 , pp. 387-392
    • Taylor, K.M.1    Porta, C.2    Lin, T.3    Johnson, J.E.4    Barker, P.J.5    Lomonossoff, G.P.6
  • 27
    • 0030334824 scopus 로고    scopus 로고
    • Structure-based design of peptide presentation on a viral surface: The crystal structure of a plant/animal virus chimera at 2.8A resolution
    • Lin T, Porta C, Lomonossoff GP, Johnson JE. Structure-based design of peptide presentation on a viral surface: The crystal structure of a plant/animal virus chimera at 2.8A resolution. Fold Des 1996; 1 : 179-87.
    • (1996) Fold Des , vol.1 , pp. 179-187
    • Lin, T.1    Porta, C.2    Lomonossoff, G.P.3    Johnson, J.E.4
  • 28
    • 0022470348 scopus 로고
    • Peptides as antigens. Importance of orientation
    • Dyrberg T, Oldstone MBA. Peptides as antigens. Importance of orientation. J Exp Med 1986; 164 : 1344-9.
    • (1986) J Exp Med , vol.164 , pp. 1344-1349
    • Dyrberg, T.1    Oldstone, M.B.A.2
  • 29
    • 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 KM, Lin T, Porta C, Mosser AG, Giesing HA, Lomonossoff GP, et al. Influence of three-dimensional structure on the immunogenicity of a peptide expressed on the surface of a plant virus. J Mol Recognit 2000; 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
  • 30
    • 0032876566 scopus 로고    scopus 로고
    • Expression and immunogenicity of a liver stage malaria epitope presented as a foreign peptide on the surface of RNA-free MS 2 bacteriophage capsids
    • Heal KG, Hill HR, Stockley PG, Hollingdale MR, Taylor-Robinson AW. Expression and immunogenicity of a liver stage malaria epitope presented as a foreign peptide on the surface of RNA-free MS 2 bacteriophage capsids. Vaccine 2000; 18 : 251-8.
    • (2000) Vaccine , vol.18 , pp. 251-258
    • Heal, K.G.1    Hill, H.R.2    Stockley, P.G.3    Hollingdale, M.R.4    Taylor-Robinson, A.W.5
  • 31
    • 0032903183 scopus 로고    scopus 로고
    • Chimeric plant virus particles administered nasally orally induce systemic and mucosal immune responses in mice
    • Brennan FR, Bellaby T, Helliwell SM, Jones TD, Kasnstrup S, Daligaard K, et al. Chimeric plant virus particles administered nasally orally induce systemic and mucosal immune responses in mice. J Virol 1999; 73 : 930-8.
    • (1999) J Virol , vol.73 , pp. 930-938
    • Brennan, F.R.1    Bellaby, T.2    Helliwell, S.M.3    Jones, T.D.4    Kasnstrup, S.5    Daligaard, K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.