An immunoglobulin G based chimeric protein induced foot-and-mouth disease specific immune response in swine

Vaccine

Volumn 19, Issue 4-5, 2000, Pages 538-546

  Chan, E W C ^a   Wong, H T ^a   Cheng, S C S ^a   Yan, W Y ^a   Zheng, Z X ^a   Sheng, Z T ^a   Zhu, L Q ^a   Xie, Y ^a  

^a HONG KONG UNIVERSITY OF SCIENCE AND TECHNOLOGY   (Hong Kong)

Author keywords

Chimeric protein; Foot and mouth disease; Immunoglobulin G constant region

Indexed keywords

CHIMERIC PROTEIN; EPITOPE; IMMUNOGLOBULIN G; IMMUNOGLOBULIN HEAVY CHAIN; NEUTRALIZING ANTIBODY; VACCINE;

ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ANTIBODY RESPONSE; ARTICLE; CELL PROLIFERATION; CONTROLLED STUDY; FOOT AND MOUTH DISEASE; IMMUNE RESPONSE; NONHUMAN; PRIORITY JOURNAL; SWINE; SWINE DISEASE; T LYMPHOCYTE ACTIVATION;

ANIMAL; ANTIBODIES, VIRAL; ANTIGENS, VIRAL; APHTHOVIRUS; BASE SEQUENCE; CHIMERIC PROTEINS; DNA PRIMERS; EPITOPES; FOOT-AND-MOUTH DISEASE; IMMUNOGLOBULIN G; IN VITRO; LYMPHOCYTE ACTIVATION; MICE; NEUTRALIZATION TESTS; SUPPORT, NON-U.S. GOV'T; SWINE; T-LYMPHOCYTES; VIRAL VACCINES;

EID: 0034668214     PISSN: 0264410X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0264-410X(00)00186-9     Document Type: Article

References (37)

1. Greeing W.A. Emerging diseases of livestock. The diseases and their diagnosis. vol. I:1984;43-51 FAO, Rome.
2. Chapter 2.1.1 Foot-and-mouth disease. In: "OIE Manual". Office International des Epizooties, Paris, 1996. 47-56.
3. Bachrach H.L. Romberger J.A. Symposium on Agricultural Research. 1977;3-32 Beltsville.
4. Burroughs J.N., Dunn G., Ferguson M. Further evidence for multiple proteins in the foot-and-mouth disease virus particle. J. Gen. Virol. 13:1971;73-84.
5. Logan D., Abu-Ghazaleh R., Blakmore W., Curry S., Jaskson T., King A., Lea S., Lewis R., Newman J., Parry N., Rowlands D., Stuart D., Fry E. Structure of the major immunogenic site on foot-and-mouth disease virus. Nature. 362:1993;566-568.
6. Lea S., Hernandez J., Blakemore W., Brocchi E., Curry S., Domingo E., Fry E., Abu-Ghazaleh R., King A., Newman J., Stuart D., Mateu M.G. The structure and antigenicity of a type C foot-and-mouth disease virus. Structure. 2:1994;123-139.
7. Palmenberg A.C. Sequence alignments of picornaviral capsid proteins. Semler B.L., Ehrenfeld E. Molecular aspects of Picornavirus infection and detection. 1989;211-241 American Society for Microbiology, Washington, DC.
8. Leippert M., Beck E., Weiland F., Pfaff E. Point mutations within the βG-βH loop of foot-and-mouth disease virus O1K affect virus attachment to target cells. J. Virol. 1:1997;1046-1051.
9. Capstick P.B., Telling R.C., Chapman R.C., Stewart D.L. Growth of cloned strain of hamster kidney cells in suspended culture and their susceptibility to the virus of foot-and-mouth disease. Nature. 195:1962;1163-1170.
10. Brown F. Review of accidents caused by incomplete inactivation of viruses. Dev. Biol. Stand. 81:1993;103-107.
11. Brown F. An overview of the inactivation of FMDV and the implications when residual virus is present in vaccines. Dev. Biol. Stand. 75:1991;37-41.
12. Murdin A.D., Murray M.G., Wimmer E. Novel approaches to Picornavirus vaccines. Mizrahi A. Viral vaccines. 1990;301-323 Wiley-Liss, New York.
13. Broekhuijsen M.P., Blom T., Kottenhagen M., Pouwel P.H., Meloen R.H., Barteling S.J., Engel-Valk B.E. Synthesis if fusion protein containing antigenic determinants of foot-and-mouth disease virus. Vaccine. 4:1986;119-124.
14. Winther M.D., Allen G., Bomford R.H., Brown F. Bacterially expressed antigenic peptide from foot-and-mouth disease virus capsid elicits variable immunologic responses in animals. J. Immunol. 136:1986;1835-1840.
15. Zheng Z.X., Xu Q.X., Mao C.Q., Zhao H.X., Jin J.P., You Y.J., Yan W.Y., Zhou Z.T., Guo J.Y. Biosynthetic peptide vaccine against foot-and-mouth disease virus. Talwan G.P., Rao K.V.S., Chauhn V.S. Recombinant and synthetic vaccines. 1994;30-35 Springer-Verlag, Berlin, Heidelberg, New York.
16. Clarke B.E., Newton S.E., Carroll A.R., Francis M.J., Appleyard G., Syred A.D., Highfield P.E., Rowlands D.J., Brown F. Improved immunogenicity of a peptide epitope after fusion to hepatitis B core protein. Nature. 330:1987;381-384.
17. Newton S.E., Clarke B.E., Appleyard G., Francis M.J., Carroll A.R., Rowlands D.J., Skehel J., Brown F. Novel antigen presentation via vaccinia. Chanock R.M., Lerner R.A., Brown F., Ginsberg H. Modern approaches to new vaccines. 1987;Vaccine 87 Cold Spring Harbor Laboratory, New York.
18. Meloen R.H., Casal J.I., Dalsgaard K., Langevels J.P.M. Synthetic peptide vaccines: success at last. Gregoriadis G., McCormack B., Allison A.C. Vaccines: new generation immunological adjuvants. 1995;127-133 Plenum, New York.
19. Jennings PA, Bills M, Irving DD, Matlick JS. Fimbrie of bacteroids nodosus: protein engineering of the structural subunit for the production of an exogenous peptide. Prot Engin 1989;2(5):365-369.
20. Bona C., Brumeanu T.D., Zaghouani H. Immunogenicity of microbial peptides grafted in self immunoglobulin molecules. Cell. Mol. Biol. 40:(Suppl. I):1994;21-30.
21. Kurz C., Forss C., Kupper H. Nucleotide sequence and corresponding amino acid sequence of the gene for the major antigen of foot-and-mouth disease virus. Nucl. Acids. Res. 9:1981;1919-1931.
22. Haberman A.M., Moller C., McGreedy D., Gerhard W.V. A large degree of functional diversity exists among helper T cells specific for the same antigenic site of influenza hemagglutinin. J. Immunol. 145:1990;3087-3094.
23. Zaghouani H., Krystal M., Kuzu H., Moran T., Shah H., Kuzu Y., Schulman J., Bona C. Cells expressing an H chain Ig gene carrying a viral T cell epitope are lysed by specific cytotoxic T cells. J. Immunol. 148:(11):1992;3604-3609.
24. Zaghouani H., Anderson S.A., Sperber K.E., Daian C., Kennedy R.C., Mayer L., Bona C.A. Induction of antibodies to the human immunodeficiency virus type I by immunization of baboons with immunoglobulin molecules carrying the principal neutralising determinant of the envelope protein. Proc. Natl. Acad. Sci. 92:1995;631-635.
25. Peppel K., Crawford D., Beutler B. A tumor necrosis factor (TNF) receptor-IgG heavy chain chimeric protein as a bivalent antagonist of TNF activity. J. Exp. Med. 74:1991;1483-1489.
26. Kacskovics I., Sun J., Butler J.E. Five putative subclasses of swine IgG identified from the cDNA sequences of a single animal. J. Immunol. 153:1994;3565-3573.
27. Porath J., Carlsson J., Olsson I., Belfrage G. Metal chelate affinity chromatography, a new approach to protein fractionation. Nature. 258:1975;598-599.
28. Hammes B.D., Rickwood D. Gel electrophoresis of proteins. 1981;IRL Press, Oxford.
29. Ferris N.F., Donalson A.I., Barnett I.T.R., Osbore R.W. Inactivation, purification and stability of 146s antigen of foot-and-mouth disease virus for as reagents in the complement fixation test. Rev. Sci. Tech. vol. 2:1984;339-350 Office International des. Epizooties, Paris.
30. Mulcahy G., Pullen L.A., Gale C., DiMarchi R.D., Doel T.R. Mouse protection test as a predictor of the protective capacity of synthetic foot-and-mouth disease vaccines. Vaccine. 9:1991;19-24.
31. Capon D.J., Chamow S.M., Mordenti J., Marsters S.A., Gregory T., Mitsuya H., Byrn R.A., Lucas C., Wurm F.M., Groopman J.E., Broder S., Smith D.H. Designing CD4 immunoadhesins for AIDS therapy. Nature. 337:1989;525-530.
32. Brumeanu T.D., Swiggard W.J., Steinman R.M., Bona C.A., Zaghouani H. Efficient loading of identical viral peptide onto class II molecules by antigenized immunoglobulin and influenza virus. J. Exp. Med. 178:1993;1795-1799.
33. Zaghouani H., Steinman R., Nonacs R., Shah H., Gerhard W., Bona C. Presentation of a viral T cell epitope expressed in the CDR3 region of a self immunoglobulin molecule. Science. 259:1993;224-227.
34. Guise A.D., West S.M., Chaudhuri J.B. Protein folding in vivo and renaturation of recombinant proteins from inclusion bodies. Mol. Biotech. 6:1996;53-64.
35. Chapman H.A. Endosomal proteolysis and MHC class II function. Curr. Opin. Immunol. 10:1998;93-102.
36. Collen T., Pullen L., Doel T.R. T cell dependent induction of antibody against foot-and-mouth disease virus in a mouse model. Virology. 70:1989;395-403.
37. Rothel J.S., Wood P.R., Seow H.F., Lightowlers M.W. Urea/DTT solubilization of a recombinant Taenia ovis antigen, 45W, expressed as a GST fusion protein results in enhanced protective immune response to the 45W moiety. Vaccine. 15:1997;469-472.