Phage-displayed and soluble mouse scFv fragments neutralize rabies virus

Journal of Virological Methods

Volumn 67, Issue 2, 1997, Pages 221-233

  Muller, Bruno H ^a   Lafay, Florence ^b   Demangel, Caroline ^a   Perrin, Pierre ^a   Tordo, Noël ^a   Flamand, Anne ^b   Lafaye, Pierre ^a   Guesdon, Jean Luc ^a  

^a INSTITUT PASTEUR   (France)

^b CNRS   (France)

Author keywords

Immunoglobulin variable regions; Phage surface expression; Rabies virus; Recombinant protein; scFv; Virus neutralization

Indexed keywords

MONOCLONAL ANTIBODY; NEUTRALIZING ANTIBODY; VIRUS ANTIBODY;

ANIMAL CELL; ARTICLE; BACTERIOPHAGE; DNA DETERMINATION; DNA SEQUENCE; ENZYME LINKED IMMUNOSORBENT ASSAY; NONHUMAN; PRIORITY JOURNAL; RABIES VIRUS; TECHNOLOGY; VIRUS EXPRESSION; VIRUS NEUTRALIZATION;

AMINO ACID SEQUENCE; ANIMALS; ANTIBODY SPECIFICITY; BASE SEQUENCE; BINDING SITES, ANTIBODY; CLONING, MOLECULAR; CRICETINAE; EPITOPES; IMMUNOGLOBULIN FRAGMENTS; IMMUNOGLOBULIN VARIABLE REGION; INOVIRIDAE; MICE; MOLECULAR SEQUENCE DATA; NEUTRALIZATION TESTS; RABIES VIRUS; SEQUENCE ANALYSIS, DNA; SOLUBILITY;

ANIMALIA; RABIES VIRUS;

EID: 0030761202     PISSN: 01660934     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0166-0934(97)00099-2     Document Type: Article

References (47)

1. Alt, F.W., Baltimore, D., 1982. Joining of immunoglobulin heavy chain gene segments: implications from a chromosome with evidence of three D-JH fusions. Proc. Natl. Acad. Sci. USA 79, 4118-4122.
2. Benmansour, A., Leblois, H., Coulon, P., Tuffereau, C., Gaudin, Y., Flamand, A., Lafay, F., 1991. Antigenicity of rabies virus glycoprotein. J. Virol. 65, 4198-4203.
3. Bunschoten, H., Gore, M., Claassen, I.J., Uytdehaag, F.G., Dietzschold, B., Wunner, W.H., Osterhaus, A.D., 1989. Characterization of a new virus-neutralizing epitope that denotes a sequential determinant on the rabies virus glycoprotein. J. Gen. Virol. 70, 291-298.
4. Burioni, R., Williamson, R.A., Sanna, P.P., Bloom, F.F., Burton, D.R., 1994. Recombinant human Fab to glycoprotein D neutralizes infectivity and prevents cell-to-cell transmission of herpes simplex viruses 1 and 2 in vitro. Proc. Natl. Acad. Sci. USA 91, 355-359.
5. Carter, P., Bedouelle, H., Winter, G., 1985. Improved oligonucleotide site-directed mutagenesis using M13 vectors. Nucleic Acids Res. 13, 4431-4443.
6. Cheung, S.C., Dietzschold, B., Koprowski, H., Notkins, A.L., Rando, R.F., 1992. A recombinant human Fab expressed in Escherichia coli neutralizes rabies virus. J. Virol. 66, 6714-6720.
7. Clackson, T., Hoogenboom, H.R., Griffiths, A.D., Winter, G., 1991. Making antibody fragments using phage-display libraries. Nature 352, 624-628.
8. Colcher, D., Bird, R., Roselli, M., Hardman, K.D., Johnson, S., Pope, S., Dodd, S.W., Pantoliano, M.W., Milenic, D.E., Schlom, J., 1990. In vivo tumor targeting of a recombinant single-chain antigen-binding protein. J. Natl. Cancer Inst. 82, 1191-1197.
9. Dietzschold, B., 1993. Antibody-mediated clearance of viruses from the mammalian central nervous system [Review]. Trends Microbiol. 1, 63-66.
10. Flamand, A., Raux, H., Gaudin, Y., Ruigrok, R.W., 1993. Mechanisms of rabies virus neutralization. Virology 194, 302-313.
11. Gaudin, Y., Tuffereau, C., Durrer, P., Flamand, A., Ruigrok, R.W., 1995. Biological function of the low-pH, fusion-inactive conformation of rabies virus glycoprotein (G): G is transported in a fusion-inactive state-like conformation. J. Virol. 69, 5528-5534.
12. Ho, S.N., Hunt, H.D., Horton, R.M., Pullen, J.K., Pease, L.R., 1989. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77, 51-59.
13. Hoogenboom, H.R., Griffiths, A.D., Johnson, K.S., Chiswell, D.J., Hudson, P., Winter, G., 1991. Multi-subunit proteins on the surface of filamentous phage: methodologies for displaying antibody (Fab) heavy and light chains. Nucleic Acids Res. 19, 4133-4137.
14. Huston, J.S., Mudgett, H.M., Tai, M.S., McCartney, J., Warren, F., Haber, E., Oppermann, H., 1991. In: J.J. Langone (Ed.), Molecular Design and Modeling: Concepts and Applications (Part B), Academic Press, San Diego, pp. 46-88.
15. Kabat, E.A., Wu, T.T., Perry, H.M., Gottesman, K.S., Foeller, C., 1991. Sequences of Proteins of Immunological Interest, 5th ed., US Department of Health and Human Services, Public Health Service, National Institutes of Health, Washington.
16. Kalinke, U., Krebber, A., Krebber, C., Bucher, E., Plückthun, A., Zinkernagel, R.M., Hengartner, H., 1996. Monovalent single-chain Fv fragments and bivalent miniantibodies bound to vesicular stomatitis virus protect against lethal infection. Eur. J. Immunol. 26, 2801-2806.
17. Kurosawa, Y., Tonegawa, S., 1982. Organization, structure, and assembly of immunoglobulin heavy chain diversity DNA segments. J. Exp. Med. 155, 201-218.
18. Lafon, M., Edelman, L., Bouvet, J.P., Lafage, M., Montchatre, E., 1990. Human monoclonal antibodies specific for the rabies virus glycoprotein and N protein. J. Gen. Virol. 71, 1689-1696.
19. Leahy, D.J., Rule, G.S., Whittaker, M.M., McConnell, H.M., 1988. Sequences of 12 monoclonal anti-dinitrophenyl spinlabel antibodies for NMR studies. Proc. Natl. Acad. Sci. USA 85, 3661-3665.
20. Libeau, G., Lafon, M., 1984. Production of monoclonal antibodies against the Pasteur (P.V.) strain of rabies virus: problems and results. Dev. Biol. Stand. 57, 213-218.
21. Marks, J.D., Hoogenboom, H.R., Bonnert, T.P., McCafferty, J., Griffiths, A.D., Winter, G., 1991. By-passing immunization. Human antibodies from V-gene libraries displayed on phage. J. Mol. Biol. 222, 581-597.
22. McCafferty, J., Griffiths, A.D., Winter, G., Chiswell, D.J., 1990. Phage antibodies: filamentous phage displaying antibody variable domains. Nature 348, 552-554.
23. Milenic, D.E., Yokota, T., Filpula, D.R., Finkelman, M.A., Dodd, S.W., Wood, J.F., Whitlow, M., Snoy, P., Schlom, J., 1991. Construction, binding properties, metabolism, and tumor targeting of a single-chain Fv derived from the pancarcinoma monoclonal antibody CC49. Cancer Res. 51, 6363-6371.
24. Pack, P., Muller, K., Zahn, R., Plückthun, A., 1995. Tetravalent miniantibodies with high avidity assembling in Escherichia coli. J. Mol. Biol. 246, 28-34.
25. Perrin, P., 1996. In: F.-X. Meslin, M.M. Kaplan, H. Koprowski (Eds.), Laboratory Techniques in Rabies, World Health Organization, Geneva, pp. 433-444.
26. Perrin, P., Versmisse, P., Delagneau, J.F., Lucas, G., Rollin, P.E., Sureau, P., 1986. The influence of the type of immunosorbent on rabies antibody EIA; advantages of purified glycoprotein over whole virus. J. Biol. Stand. 14, 95-102.
27. Prehaud, C., Coulon, P., Lafay, F., Thiers, C., Flamand, A., 1988. Antigenic site II of the rabies virus glycoprotein: structure and role in viral virulence. J. Virol. 62, 1-7.
28. Rando, R.F., Notkins, A.L., 1994. In: C.E. Rupprecht, B. Dietzschold, H. Koprowski (Eds.), Lyssaviruses, Springer-Verlag, Berlin, pp. 195-205.
29. Sablitzky, F., Rajewsky, K., 1984. Molecular basis of an isogeneic anti-idiotypic response. EMBO J. 3, 3005-3012.
30. Sakano, H., Huppi, K., Heinrich, G., Tonegawa, S., 1979. Sequences at the somatic recombination sites of immunoglobulin light-chain genes. Nature 280, 288-294.
31. Sakano, H., Maki, R., Kurosawa, Y., Roeder, W., Tonegawa, S., 1980. Two types of somatic recombination are necessary for the generation of complete immunoglobulin heavy-chain genes. Nature 286, 676-683.
32. Sambrook, J., Fritsch, E.F., Maniatis, T., 1989. Molecular Cloning: A Laboratory Manual, 2th ed., Cold Spring Harbor Laboratory Press, New York.
33. Sanger, F., Nicklen, S., Coulson, A.R., 1977. DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. USA 74, 5463-5467.
34. Seif, I., Coulon, P., Rollin, P.E., Flamand, A., 1985. Rabies virulence: effect on pathogenicity and sequence characterization of rabies virus mutations affecting antigenic site III of the glycoprotein. J. Virol. 53, 926-934.
35. Sequeira, A., Avrameas, S., Jouvin, M.E., 1992. Molecular characterization of the variable regions of a mouse polyreactive IgG2b antibody with rheumatoid factor activity. Immunogenetics 36, 15-21.
36. Sikes, R.K., Cleary, W.F., Koprowski, H., Wiktor, T.J., Kaplan, M.M., 1971. Effective protection of monkeys against death from street virus by post-exposure administration of tissue-culture rabies vaccine. Bull. WHO 45, 1-11.
37. Smith, J.S., 1996. New aspects of rabies with emphasis on epidemiology, diagnosis, and prevention of the disease in the united states. Clin. Microbiol. Rev. 9, 166-176.
38. Smith, J.S., Yager, P.A., Baer, G.M., 1996. In: F.-X. Meslin, M.M. Kaplan, H. Koprowski (Eds.), Laboratory Techniques in Rabies, World Health Organization, Geneva, pp. 181-192.
39. Srikantan, V., Wang, B., Satre, M.A., Ugen, K.E., Dang, K., Scales, F., Godillot, A.P., Williams, W.V., Weiner, D.B., 1994. Cloning and biological characterization of human single-chain Fv fragments that mediate neutralization of HIV-1. AIDS 8, 1525-1532.
40. Steeves, T., Barry, M.M., Duckworth, H.W., Waygood, E.B., Lee, J.S., 1991. Sequences of the variable regions of three monoclonal antibodies specific for histidine-containing protein of the bacterial phosphoenolpyruvate: sugar phosphotransferase system. Biochem. Cell Biol. 69, 297-302.
41. Stevens, P.W., Francis, C.H., Jolley, M.E., Bethell, D.R., 1993. Monoclonal antibodies to HIV-1 p24 core protein include pairs which exhibit synergistic binding. Mol. Immunol. 30, 243-254.
42. Tonegawa, S., 1983. Somatic generation of antibody diversity [Review]. Nature 302, 575-581.
43. Warrell, D.A., Warrell, M.J., 1995. Human rabies: a continuing challenge in the tropical world [Review]. Schweiz. Med. Wochenschr. 125, 879-885.
44. Winter, G., Griffiths, A.D., Hawkins, R.E., Hoogenboom, H.R., 1994. Making antibodies by phage display technology. Annu. Rev. Immunol. 12, 433-455.
45. Winter, G., Milstein, C., 1991. Man-made antibodies. Nature 349, 293-299.
46. Wu, A.M., Chen, W., Raubitschek, A., Williams, L.E., Neumaier, M., Fischer, R., Hu, S.Z., Odom-Maryon, T., Wong, J.Y.C., Shively, J.E., 1996. Tumor localization of anti-CEA single-chain Fvs: improved targeting by non-covalent dimers. Immunotechnology 2, 21-36.
47. Yokota, T., Milenic, D.E., Whitlow, M., Schlom, J., 1992. Rapid tumor penetration of a single-chain Fv and comparison with other immunoglobulin forms. Cancer Res. 52, 3402-3408.