메뉴 건너뛰기




Volumn 115, Issue 1, 2004, Pages 83-92

Generation and characterization of single-chain antibody fragments specific against transmembrane envelope glycoprotein gp46 of maedi-visna virus

Author keywords

gp46; Intracellular immunization; Maedi visna virus; Phage display

Indexed keywords

GLYCOPROTEIN GP 46; IMMUNOGLOBULIN FRAGMENT; IMMUNOGLOBULIN LIGHT CHAIN; PEPTIDE LIBRARY; SINGLE CHAIN FRAGMENT VARIABLE ANTIBODY; UNCLASSIFIED DRUG; VIRUS ANTIBODY; VIRUS ENVELOPE PROTEIN; VIRUS GLYCOPROTEIN;

EID: 0344628609     PISSN: 01660934     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jviromet.2003.09.020     Document Type: Article
Times cited : (23)

References (33)
  • 2
    • 0027961025 scopus 로고
    • Antibody reactivity to the immunodominant epitopes of the caprine arthritis-encephalitis virus gp38 transmembrane protein associates with the development of arthritis
    • Bertoni G., Zahno M.L., Zanoni R., Vogt H.R., Peterhans E., Ruff G., Cheevers W.P., Sonigo P., Pancino G. Antibody reactivity to the immunodominant epitopes of the caprine arthritis-encephalitis virus gp38 transmembrane protein associates with the development of arthritis. J. Virol. 68(11):1994;7139-7147.
    • (1994) J. Virol. , vol.68 , Issue.11 , pp. 7139-7147
    • Bertoni, G.1    Zahno, M.L.2    Zanoni, R.3    Vogt, H.R.4    Peterhans, E.5    Ruff, G.6    Cheevers, W.P.7    Sonigo, P.8    Pancino, G.9
  • 5
    • 0023972977 scopus 로고
    • Precursor polypeptides of caprine arthritis-encephalitis lentivirus structural proteins
    • Cheevers W.P., Stem T.A., Knowles D.P., McGuire T.C. Precursor polypeptides of caprine arthritis-encephalitis lentivirus structural proteins. J. Gen. Virol. 69(3):1988;675-681.
    • (1988) J. Gen. Virol. , vol.69 , Issue.3 , pp. 675-681
    • Cheevers, W.P.1    Stem, T.A.2    Knowles, D.P.3    McGuire, T.C.4
  • 6
    • 13344261388 scopus 로고    scopus 로고
    • Molecular biology and pathogenesis of animal lentivirus infections
    • Clements J.E., Zink M.C. Molecular biology and pathogenesis of animal lentivirus infections. Clin. Microbiol. Rev. 9(1):1996;100-117.
    • (1996) Clin. Microbiol. Rev. , vol.9 , Issue.1 , pp. 100-117
    • Clements, J.E.1    Zink, M.C.2
  • 8
    • 0031887368 scopus 로고    scopus 로고
    • Effects of substitutions in the binding surface of an antibody on antigen affinity
    • Dougan D.A., Malby R.L., Gruen L.C., Kortt A.A., Hudson P.J. Effects of substitutions in the binding surface of an antibody on antigen affinity. Protein Eng. 11(1):1998;65-74.
    • (1998) Protein Eng. , vol.11 , Issue.1 , pp. 65-74
    • Dougan, D.A.1    Malby, R.L.2    Gruen, L.C.3    Kortt, A.A.4    Hudson, P.J.5
  • 9
    • 0032794624 scopus 로고    scopus 로고
    • Development of a monoclonal antibody blocking-ELISA for detection of antibodies against Maedi-Visna virus
    • Fevereiro M., Barros S., Fagulha T. Development of a monoclonal antibody blocking-ELISA for detection of antibodies against Maedi-Visna virus. J. Virol. Methods. 81(1-2):1999;101-108.
    • (1999) J. Virol. Methods , vol.81 , Issue.12 , pp. 101-108
    • Fevereiro, M.1    Barros, S.2    Fagulha, T.3
  • 11
    • 0037199960 scopus 로고    scopus 로고
    • Functional neutralization of HIV-1 Vif protein by intracellular immunization inhibits reverse transcription and viral replication
    • Goncalves J., Silva F., Freitas-Vieira A., Santa-Marta M., Malho R., Yang X., Gabuzda D., Barbas C. 3rd. Functional neutralization of HIV-1 Vif protein by intracellular immunization inhibits reverse transcription and viral replication. J. Biol. Chem. 277(35):2002;32036-32045.
    • (2002) J. Biol. Chem. , vol.277 , Issue.35 , pp. 32036-32045
    • Goncalves, J.1    Silva, F.2    Freitas-Vieira, A.3    Santa-Marta, M.4    Malho, R.5    Yang, X.6    Gabuzda, D.7    Barbas III, C.8
  • 14
    • 0032779583 scopus 로고    scopus 로고
    • Properties of a panel of single chain variable fragments against Potato leafroll virus obtained from two phage display libraries
    • Harper K., Toth R.L., Mayo M.A., Torrance L. Properties of a panel of single chain variable fragments against Potato leafroll virus obtained from two phage display libraries. J. Virol. Methods. 81(1-2):1999;159-168.
    • (1999) J. Virol. Methods , vol.81 , Issue.12 , pp. 159-168
    • Harper, K.1    Toth, R.L.2    Mayo, M.A.3    Torrance, L.4
  • 15
    • 0028246609 scopus 로고
    • Oligopeptide-based enzyme immunoassay for ovine lentivirus antibody detection
    • Kwang J., Torres J.V. Oligopeptide-based enzyme immunoassay for ovine lentivirus antibody detection. J. Clin. Microbiol. 32(7):1994;1813-1815.
    • (1994) J. Clin. Microbiol. , vol.32 , Issue.7 , pp. 1813-1815
    • Kwang, J.1    Torres, J.V.2
  • 16
    • 0034074811 scopus 로고    scopus 로고
    • Design and intracellular activity of a human single-chain antibody to human immunodeficiency virus type 1 conserved gp41 epitope
    • Legastelois I., Desgranges C. Design and intracellular activity of a human single-chain antibody to human immunodeficiency virus type 1 conserved gp41 epitope. J. Virol. 74(12):2000;5712-5715.
    • (2000) J. Virol. , vol.74 , Issue.12 , pp. 5712-5715
    • Legastelois, I.1    Desgranges, C.2
  • 17
    • 0036401232 scopus 로고    scopus 로고
    • Rapid pathotyping of Newcastle disease virus using a single-chain Fv displayed on phage against the C-terminal end of the F2 polypeptide
    • Li Y., Collins M.S., Whitelam G.C., Alexander D.J. Rapid pathotyping of Newcastle disease virus using a single-chain Fv displayed on phage against the C-terminal end of the F2 polypeptide. Arch. Virol. 147(10):2002;2025-2037.
    • (2002) Arch. Virol. , vol.147 , Issue.10 , pp. 2025-2037
    • Li, Y.1    Collins, M.S.2    Whitelam, G.C.3    Alexander, D.J.4
  • 18
    • 0035902564 scopus 로고    scopus 로고
    • The trimer-of-hairpins motif in membrane fusion: Visna virus
    • Malashkevich V.N., Singh M., Kim P.S. The trimer-of-hairpins motif in membrane fusion: visna virus. Proc. Natl. Acad. Sci. U.S.A. 98(15):2001;8502- 8506.
    • (2001) Proc. Natl. Acad. Sci. U.S.A , vol.98 , Issue.15 , pp. 8502-8506
    • Malashkevich, V.N.1    Singh, M.2    Kim, P.S.3
  • 19
    • 0031016269 scopus 로고    scopus 로고
    • Intrabodies: Turning the humoral immune system outside in for intracellular immunization
    • Marasco W.A. Intrabodies: turning the humoral immune system outside in for intracellular immunization. Gene Ther. 4(1):1997;11-15.
    • (1997) Gene Ther. , vol.4 , Issue.1 , pp. 11-15
    • Marasco, W.A.1
  • 20
    • 0033037725 scopus 로고    scopus 로고
    • Variable constraints on the principal immunodominant domain of the transmembrane glycoprotein of human immunodeficiency virus type 1
    • Merat R., Raoul H., Leste-Lasserre T., Sonigo P., Pancino G. Variable constraints on the principal immunodominant domain of the transmembrane glycoprotein of human immunodeficiency virus type 1. J. Virol. 73(7):1999;5698-5706.
    • (1999) J. Virol. , vol.73 , Issue.7 , pp. 5698-5706
    • Merat, R.1    Raoul, H.2    Leste-Lasserre, T.3    Sonigo, P.4    Pancino, G.5
  • 21
    • 0030861243 scopus 로고    scopus 로고
    • Inhibition of human immunodeficiency virus type 1 replication in vitro by a novel combination of anti-Tat single-chain intrabodies and NF-kappa B antagonists
    • Mhashilkar A.M., Biswas D.K., LaVecchio J., Pardee A.B., Marasco W.A. Inhibition of human immunodeficiency virus type 1 replication in vitro by a novel combination of anti-Tat single-chain intrabodies and NF-kappa B antagonists. J. Virol. 71(9):1997;6486-6494.
    • (1997) J. Virol. , vol.71 , Issue.9 , pp. 6486-6494
    • Mhashilkar, A.M.1    Biswas, D.K.2    Lavecchio, J.3    Pardee, A.B.4    Marasco, W.A.5
  • 22
    • 0023652396 scopus 로고
    • A C-terminal signal prevents secretion of luminal ER proteins
    • Munro S., Pelham H.R. A C-terminal signal prevents secretion of luminal ER proteins. Cell. 48(5):1987;899-907.
    • (1987) Cell , vol.48 , Issue.5 , pp. 899-907
    • Munro, S.1    Pelham, H.R.2
  • 23
    • 0028903355 scopus 로고
    • Structural analysis of the principal immunodominant domain of the feline immunodeficiency virus transmembrane glycoprotein
    • Pancino G., Camoin L., Sonigo P. Structural analysis of the principal immunodominant domain of the feline immunodeficiency virus transmembrane glycoprotein. J. Virol. 69(4):1995;2110-2118.
    • (1995) J. Virol. , vol.69 , Issue.4 , pp. 2110-2118
    • Pancino, G.1    Camoin, L.2    Sonigo, P.3
  • 24
  • 26
    • 0036922697 scopus 로고    scopus 로고
    • Visna/maedi virus Env protein expressed by a vaccinia virus recombinant induces cell-to-cell fusion in cells of different origins in the apparent absence of Env cleavage: Role of glycosylation and of proteoglycans
    • Sanchez A.B., Rodriguez D., Garzon A., Amorena B., Esteban M., Rodriguez J.R. Visna/maedi virus Env protein expressed by a vaccinia virus recombinant induces cell-to-cell fusion in cells of different origins in the apparent absence of Env cleavage: role of glycosylation and of proteoglycans. Arch. Virol. 147(12):2002;2377-2392.
    • (2002) Arch. Virol. , vol.147 , Issue.12 , pp. 2377-2392
    • Sanchez, A.B.1    Rodriguez, D.2    Garzon, A.3    Amorena, B.4    Esteban, M.5    Rodriguez, J.R.6
  • 27
    • 0026739609 scopus 로고
    • Conserved structural features in the interaction between retroviral surface and transmembrane glycoproteins
    • Schulz T.F., Jameson B.A., Lopalco L., Siccardi A.G., Weiss R.A., Moore J.P. Conserved structural features in the interaction between retroviral surface and transmembrane glycoproteins. AIDS Res. Hum. Retroviruses. 8(9):1992;1571-1580.
    • (1992) AIDS Res. Hum. Retroviruses , vol.8 , Issue.9 , pp. 1571-1580
    • Schulz, T.F.1    Jameson, B.A.2    Lopalco, L.3    Siccardi, A.G.4    Weiss, R.A.5    Moore, J.P.6
  • 30
    • 0028216374 scopus 로고
    • Enhancement of EIAV replication and disease by immunization with a baculovirus-expressed recombinant envelope surface glycoprotein
    • Wang S.Z., Rushlow K.E., Issel C.J., Cook R.F., Cook S.J., Raabe M.L., Chong Y.H., Costa L., Montelaro R.C. Enhancement of EIAV replication and disease by immunization with a baculovirus-expressed recombinant envelope surface glycoprotein. Virology. 199(1):1994;247-251.
    • (1994) Virology , vol.199 , Issue.1 , pp. 247-251
    • Wang, S.Z.1    Rushlow, K.E.2    Issel, C.J.3    Cook, R.F.4    Cook, S.J.5    Raabe, M.L.6    Chong, Y.H.7    Costa, L.8    Montelaro, R.C.9
  • 31
    • 0010296944 scopus 로고
    • Biosynthesis, cleavage, and degradation of the human immunodeficiency virus 1 envelope glycoprotein gp160
    • Willey R.L., Bonifacino J.S., Potts B.J., Martin M.A., Klausner R.D. Biosynthesis, cleavage, and degradation of the human immunodeficiency virus 1 envelope glycoprotein gp160. Proc. Natl. Acad. Sci. U.S.A. 85(24):1988;9580- 9584.
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , Issue.24 , pp. 9580-9584
    • Willey, R.L.1    Bonifacino, J.S.2    Potts, B.J.3    Martin, M.A.4    Klausner, R.D.5
  • 32
    • 0031892153 scopus 로고    scopus 로고
    • Cells transfected with a non-neutralizing antibody gene are resistant to HIV infection: Targeting the endoplasmic reticulum and trans-Golgi network
    • Zhou P., Goldstein S., Devadas K., Tewari D., Notkins A.L. Cells transfected with a non-neutralizing antibody gene are resistant to HIV infection: targeting the endoplasmic reticulum and trans-Golgi network. J. Immunol. 160(3):1998;1489-1496.
    • (1998) J. Immunol. , vol.160 , Issue.3 , pp. 1489-1496
    • Zhou, P.1    Goldstein, S.2    Devadas, K.3    Tewari, D.4    Notkins, A.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.