메뉴 건너뛰기




Volumn 51, Issue 2, 2012, Pages 188-196

A novel disulfide-stabilized single-chain variable antibody fragment against rabies virus G protein with enhanced in vivo neutralizing potency

Author keywords

Disulfide bond; G protein; Molecular modification; Monoclonal antibody; Rabies virus; Single chain Fv fragment; Stability

Indexed keywords

CYSTEINE; DISULFIDE; DISULFIDE FV57; GUANINE NUCLEOTIDE BINDING PROTEIN; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY MAB57; RABIES IMMUNOGLOBULIN; SINGLE CHAIN FRAGMENT VARIABLE ANTIBODY; UNCLASSIFIED DRUG;

EID: 84860381852     PISSN: 01615890     EISSN: 18729142     Source Type: Journal    
DOI: 10.1016/j.molimm.2012.03.015     Document Type: Article
Times cited : (24)

References (49)
  • 1
    • 0019868697 scopus 로고
    • Structure of the glycoprotein gene in rabies virus
    • Anilionis A., Wunner W.H., Curtis P.J. Structure of the glycoprotein gene in rabies virus. Nature 1981, 294:275-278.
    • (1981) Nature , vol.294 , pp. 275-278
    • Anilionis, A.1    Wunner, W.H.2    Curtis, P.J.3
  • 3
    • 0026091179 scopus 로고
    • Identification of a protein required for disulfide bond formation in vivo
    • Bardwell J.C.A., McGovern K., Beckwith J. Identification of a protein required for disulfide bond formation in vivo. Cell 1991, 67:581-589.
    • (1991) Cell , vol.67 , pp. 581-589
    • Bardwell, J.C.A.1    McGovern, K.2    Beckwith, J.3
  • 4
    • 0023258208 scopus 로고
    • Measurement of monoclonal antibody affinity by non-competitive enzyme immunoassay
    • Beatty J.D., Beatty B.G., Vlahos W.G. Measurement of monoclonal antibody affinity by non-competitive enzyme immunoassay. J. Immunol. Methods 1987, 100:173-179.
    • (1987) J. Immunol. Methods , vol.100 , pp. 173-179
    • Beatty, J.D.1    Beatty, B.G.2    Vlahos, W.G.3
  • 6
    • 43849113623 scopus 로고    scopus 로고
    • Novel human 3-domain disulfide-stabilized antibody fragment against glycoprotein of rabies virus
    • Cai K., Wang H., Bao S., Shi J., Hou X., Gao X., Liu H., Yin J. Novel human 3-domain disulfide-stabilized antibody fragment against glycoprotein of rabies virus. Microbes and Infection 2008, 10:548-555.
    • (2008) Microbes and Infection , vol.10 , pp. 548-555
    • Cai, K.1    Wang, H.2    Bao, S.3    Shi, J.4    Hou, X.5    Gao, X.6    Liu, H.7    Yin, J.8
  • 7
    • 0033962738 scopus 로고    scopus 로고
    • The development of monoclonal human rabies virus-neutralizing antibodies as a substitute for pooled human immune globulin in the prophylactic treatment of rabies virus exposure
    • Champion J., Kean R., Rupprecht C., Notkins A., Koprowski H., Dietzschold B., Hooper D. The development of monoclonal human rabies virus-neutralizing antibodies as a substitute for pooled human immune globulin in the prophylactic treatment of rabies virus exposure. J. Immunol. Methods 2000, 235:81-90.
    • (2000) J. Immunol. Methods , vol.235 , pp. 81-90
    • Champion, J.1    Kean, R.2    Rupprecht, C.3    Notkins, A.4    Koprowski, H.5    Dietzschold, B.6    Hooper, D.7
  • 8
    • 0029170457 scopus 로고
    • The glycoprotein G of rhabdoviruses
    • Coll J.M. The glycoprotein G of rhabdoviruses. Arch. Virol. 1995, 140:827-851.
    • (1995) Arch. Virol. , vol.140 , pp. 827-851
    • Coll, J.M.1
  • 10
    • 0020977127 scopus 로고
    • Structural basis of antibody function
    • Davies D.R., Metzger H. Structural basis of antibody function. Annu. Rev. Immunol. 1983, 1:87-117.
    • (1983) Annu. Rev. Immunol. , vol.1 , pp. 87-117
    • Davies, D.R.1    Metzger, H.2
  • 13
    • 79957627071 scopus 로고    scopus 로고
    • Thermal stability and structural variations of survivin and its deletants in aqueous solution as revealed by spectroscopy
    • Gao Y., Zhang M., Zhang H., Yu X., Kong W., Zha X., Wu Y. Thermal stability and structural variations of survivin and its deletants in aqueous solution as revealed by spectroscopy. The Journal of Physical Chemistry B 2011.
    • (2011) The Journal of Physical Chemistry B
    • Gao, Y.1    Zhang, M.2    Zhang, H.3    Yu, X.4    Kong, W.5    Zha, X.6    Wu, Y.7
  • 18
    • 34250971354 scopus 로고
    • Beitrag zur kollektiven Behandlung pharmakologischer Reihenversuche
    • Karber G. Beitrag zur kollektiven Behandlung pharmakologischer Reihenversuche. Naunyn Schmiedebergs Arch. Pharmacol. 1931, 162:480-483.
    • (1931) Naunyn Schmiedebergs Arch. Pharmacol. , vol.162 , pp. 480-483
    • Karber, G.1
  • 21
    • 0028057249 scopus 로고
    • Recombinant immunotoxins containing anti-Tac (Fv) and derivatives of Pseudomonas exotoxin produce complete regression in mice of an interleukin-2 receptor-expressing human carcinoma
    • Kreitman R.J., Bailon P., Chaudhary V., FitzGerald D., Pastan I. Recombinant immunotoxins containing anti-Tac (Fv) and derivatives of Pseudomonas exotoxin produce complete regression in mice of an interleukin-2 receptor-expressing human carcinoma. Blood 1994, 83:426-434.
    • (1994) Blood , vol.83 , pp. 426-434
    • Kreitman, R.J.1    Bailon, P.2    Chaudhary, V.3    FitzGerald, D.4    Pastan, I.5
  • 25
    • 16244382346 scopus 로고    scopus 로고
    • Production of rabies neutralizing antibody in hen's eggs using a part of the G protein expressed in Escherichia coli
    • Motoi Y., Sato K., Hatta H., Morimoto K., Inoue S., Yamada A. Production of rabies neutralizing antibody in hen's eggs using a part of the G protein expressed in Escherichia coli. Vaccine 2005, 23:3026-3032.
    • (2005) Vaccine , vol.23 , pp. 3026-3032
    • Motoi, Y.1    Sato, K.2    Hatta, H.3    Morimoto, K.4    Inoue, S.5    Yamada, A.6
  • 26
    • 34547841644 scopus 로고    scopus 로고
    • Development and evaluation of a competitive ELISA for estimation of rabies neutralizing antibodies after post-exposure rabies vaccination in humans
    • Muhamuda K., Madhusudana S.N., Ravi V. Development and evaluation of a competitive ELISA for estimation of rabies neutralizing antibodies after post-exposure rabies vaccination in humans. Int. J. Infect. Dis. 2007, 11:441-445.
    • (2007) Int. J. Infect. Dis. , vol.11 , pp. 441-445
    • Muhamuda, K.1    Madhusudana, S.N.2    Ravi, V.3
  • 28
    • 0032870332 scopus 로고    scopus 로고
    • Pharmacokinetics and biodistribution of engineered single-chain antibody constructs of MAb CC49 in colon carcinoma xenografts
    • Pavlinkova G., Beresford G.W., Booth B.J., Batra S.K., Colcher D. Pharmacokinetics and biodistribution of engineered single-chain antibody constructs of MAb CC49 in colon carcinoma xenografts. J. Nucl. Med. 1999, 40:1536-1546.
    • (1999) J. Nucl. Med. , vol.40 , pp. 1536-1546
    • Pavlinkova, G.1    Beresford, G.W.2    Booth, B.J.3    Batra, S.K.4    Colcher, D.5
  • 29
    • 0022415294 scopus 로고
    • Rabies immunosome (subunit vaccine) structure and immunogenicity. Pre- and post-exposure protection studies
    • Perrin P., Thibodeau L., Sureau P. Rabies immunosome (subunit vaccine) structure and immunogenicity. Pre- and post-exposure protection studies. Vaccine 1985, 3:325-332.
    • (1985) Vaccine , vol.3 , pp. 325-332
    • Perrin, P.1    Thibodeau, L.2    Sureau, P.3
  • 30
    • 0037963574 scopus 로고    scopus 로고
    • Development of a cocktail of recombinant-expressed human rabies virus-neutralizing monoclonal antibodies for postexposure prophylaxis of rabies
    • Prosniak M., Faber M., Hanlon C.A., Rupprecht C.E., Hooper D.C., Dietzschold B. Development of a cocktail of recombinant-expressed human rabies virus-neutralizing monoclonal antibodies for postexposure prophylaxis of rabies. Journal of Infectious Diseases 2003, 188:53-56.
    • (2003) Journal of Infectious Diseases , vol.188 , pp. 53-56
    • Prosniak, M.1    Faber, M.2    Hanlon, C.A.3    Rupprecht, C.E.4    Hooper, D.C.5    Dietzschold, B.6
  • 32
    • 0034906211 scopus 로고    scopus 로고
    • Selection of single chain variable fragments (scFv) against the glycoprotein antigen of the rabies virus from a human synthetic scFv phage display library and their fusion with the Fc region of human IgG1
    • Ray K., Embleton M., Jailkhani B., Bhan M., Kumar R. Selection of single chain variable fragments (scFv) against the glycoprotein antigen of the rabies virus from a human synthetic scFv phage display library and their fusion with the Fc region of human IgG1. Clinical & Experimental Immunology 2001, 125:94-101.
    • (2001) Clinical & Experimental Immunology , vol.125 , pp. 94-101
    • Ray, K.1    Embleton, M.2    Jailkhani, B.3    Bhan, M.4    Kumar, R.5
  • 33
    • 0028285899 scopus 로고
    • Improved binding and antitumor activity of a recombinant anti-erbB2 immunotoxin by disulfide stabilization of the Fv fragment
    • Reiter Y., Brinkmann U., Jung S.H., Lee B., Kasprzyk P.G., King C.R., Pastan I. Improved binding and antitumor activity of a recombinant anti-erbB2 immunotoxin by disulfide stabilization of the Fv fragment. Journal of Biological Chemistry 1994, 269:18327-18331.
    • (1994) Journal of Biological Chemistry , vol.269 , pp. 18327-18331
    • Reiter, Y.1    Brinkmann, U.2    Jung, S.H.3    Lee, B.4    Kasprzyk, P.G.5    King, C.R.6    Pastan, I.7
  • 34
    • 0028335616 scopus 로고
    • Stabilization of the Fv fragments in recombinant immunotoxins by disulfide bonds engineered into conserved framework regions
    • Reiter Y., Brinkmann U., Kreitman R.J., Jung S.H., Lee B., Pastan I. Stabilization of the Fv fragments in recombinant immunotoxins by disulfide bonds engineered into conserved framework regions. Biochemistry 1994, 33:5451-5459.
    • (1994) Biochemistry , vol.33 , pp. 5451-5459
    • Reiter, Y.1    Brinkmann, U.2    Kreitman, R.J.3    Jung, S.H.4    Lee, B.5    Pastan, I.6
  • 35
    • 0028216376 scopus 로고
    • Engineering interchain disulfide bonds into conserved framework regions of Fv fragments: improved biochemical characteristics of recombinant immunotoxins containing disulfide-stabilized Fv
    • Reiter Y., Brinkmann U., Webber K.O., Jung S.H., Lee B., Pastan I. Engineering interchain disulfide bonds into conserved framework regions of Fv fragments: improved biochemical characteristics of recombinant immunotoxins containing disulfide-stabilized Fv. Protein Eng. 1994, 7:697-704.
    • (1994) Protein Eng. , vol.7 , pp. 697-704
    • Reiter, Y.1    Brinkmann, U.2    Webber, K.O.3    Jung, S.H.4    Lee, B.5    Pastan, I.6
  • 36
    • 0029960032 scopus 로고    scopus 로고
    • Antibody engineering of recombinant Fv immunotoxins for improved targeting of cancer: disulfide-stabilized Fv immunotoxins
    • Reiter Y., Pastan I. Antibody engineering of recombinant Fv immunotoxins for improved targeting of cancer: disulfide-stabilized Fv immunotoxins. Clin. Cancer Res. 1996, 2:245-252.
    • (1996) Clin. Cancer Res. , vol.2 , pp. 245-252
    • Reiter, Y.1    Pastan, I.2
  • 39
    • 0015183913 scopus 로고
    • Effective protection of monkeys against death from street virus by post-exposure administration of tissue-culture rabies vaccine
    • Sikes R., Cleary W., Koprowski H., Wiktor T., Kaplan M.M. Effective protection of monkeys against death from street virus by post-exposure administration of tissue-culture rabies vaccine. Bull. World Health Organ. 1971, 45:1-11.
    • (1971) Bull. World Health Organ. , vol.45 , pp. 1-11
    • Sikes, R.1    Cleary, W.2    Koprowski, H.3    Wiktor, T.4    Kaplan, M.M.5
  • 40
    • 0024292736 scopus 로고
    • Assembly of a functional immunoglobulin Fv fragment in Escherichia coli
    • Skerra A., Pluckthun A. Assembly of a functional immunoglobulin Fv fragment in Escherichia coli. Science 1988, 240:1038-1041.
    • (1988) Science , vol.240 , pp. 1038-1041
    • Skerra, A.1    Pluckthun, A.2
  • 41
    • 0015749522 scopus 로고
    • A rapid reproducible test for determining rabies neutralizing antibody
    • Smith J.S., Yager P.A., Baer G.M. A rapid reproducible test for determining rabies neutralizing antibody. Bull. World Health Organ. 1973, 48:535.
    • (1973) Bull. World Health Organ. , vol.48 , pp. 535
    • Smith, J.S.1    Yager, P.A.2    Baer, G.M.3
  • 42
    • 84979120254 scopus 로고
    • The method of 'right and wrong cases' ('constant stimuli') without Gauss's formulae
    • Spearman C. The method of 'right and wrong cases' ('constant stimuli') without Gauss's formulae. British Journal of Psychology, 1904-1920 1908, 2:227-242.
    • (1908) British Journal of Psychology, 1904-1920 , vol.2 , pp. 227-242
    • Spearman, C.1
  • 43
    • 0002221242 scopus 로고    scopus 로고
    • Characteristics and molecular biology of the rabies virus
    • World Health Organization, Geneva, Switzerland
    • Tordo N. Characteristics and molecular biology of the rabies virus. Laboratory Techniques in Rabies 1996, World Health Organization, Geneva, Switzerland, pp. 28-51. 4th edn.
    • (1996) Laboratory Techniques in Rabies , pp. 28-51
    • Tordo, N.1
  • 44
    • 0034717064 scopus 로고    scopus 로고
    • Protein folding and stability investigated by fluorescence, circular dichroism (CD), and nuclear magnetic resonance (NMR) spectroscopy: the flavodoxin story
    • van Mierlo C.P.M., Steensma E. Protein folding and stability investigated by fluorescence, circular dichroism (CD), and nuclear magnetic resonance (NMR) spectroscopy: the flavodoxin story. J. Biotechnol. 2000, 79:281-298.
    • (2000) J. Biotechnol. , vol.79 , pp. 281-298
    • van Mierlo, C.P.M.1    Steensma, E.2
  • 45
    • 1642355140 scopus 로고    scopus 로고
    • Rabies and other lyssavirus diseases
    • Warrell M.J., Warrell D.A. Rabies and other lyssavirus diseases. Lancet 2004, 363:959-969.
    • (2004) Lancet , vol.363 , pp. 959-969
    • Warrell, M.J.1    Warrell, D.A.2
  • 46
    • 84860357200 scopus 로고
    • WHO, World Health Organization Expert Committee on Rabies. World Health Organization technical report, ser. 121, World Health Organization, Geneva.
    • WHO, 1957. World Health Organization Expert Committee on Rabies. World Health Organization technical report, ser. 121, World Health Organization, Geneva.
    • (1957)


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.