Malaria epitopes expressed on the surface of recombinant tobacco mosaic virus

Bio/Technology

Volumn 13, Issue 1, 1995, Pages 53-57

  Turpen, Thomas H ^a   Reinl, Stephen J ^a   Charoenvit, Yupin ^b   Hoffman, Stephen L ^b   Fallarme, Victoria ^b   Grill, Laurence K ^a  

^a Biosource Technologies Inc   (United States)

^b NAVAL MEDICAL RESEARCH INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

COAT PROTEIN; EPITOPE; HYBRID PROTEIN;

ANTIGENICITY; ARTICLE; B LYMPHOCYTE; CARBOXY TERMINAL SEQUENCE; COST EFFECTIVENESS ANALYSIS; ENZYME LINKED IMMUNOSORBENT ASSAY; GENE EXPRESSION; IMMUNE SYSTEM; MALARIA; OPEN READING FRAME; RECOMBINANT DNA TECHNOLOGY; TOBACCO MOSAIC VIRUS;

AMINO ACID SEQUENCE; ANIMAL; ANTIGENS, PROTOZOAN; BASE SEQUENCE; EPITOPES; ESCHERICHIA COLI; GENE EXPRESSION; MALARIA VACCINES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PLANTS, TOXIC; PLASMODIUM; PROTEIN STRUCTURE, SECONDARY; SUPPORT, U.S. GOV'T, NON-P.H.S.; TOBACCO; TOBAMOVIRUS; VIRAL PROTEINS;

EID: 0028851280     PISSN: 0733222X     EISSN: None     Source Type: Journal    
DOI: 10.1038/nbt0195-53     Document Type: Article

References (33)

1. Arnon, R. and Van Regenmortel, M. H. V. 1992. Structural basis of antigenic specificity and design of new vaccines. FASEB J. 6:3265-3274.
2. Oaks, S. C. Jr., Mitchell, V. S., Pearson, G. W., Carpenter, C. C. J. (Eds.). 1991. Vaccines, p. 169-210. In: Malaria-Obstacles and Opportunities. National Academy Press, Washington, D. C.
3. Haynes, J. R., Cunningham, J., Von Seefried, A., Lennick, M., Garvin, R. T. and Shen, S.-H. 1986. Development of genetically-engineered, candidate polio vaccine employing the self-assembling properties of the tobacco mosaic virus coat protein. Bio/Technology 4:637-641.
4. Usha, R., Rohll, J. B., Spall, V. E., Shanks, M., Maule, A. J., Johnson, J. E. and Lomonossoff, G. P. 1993. Expression of an animal virus antigenic site on the surface of a plant virus particle. Virology 197:366-374.
5. Dawson, W. O. 1992. Tobamovirus-plant interactions. Virology 186:359-367.
6. Kumagai, M. H., Turpen, T. H., Weinzettl, N., della-Cioppa, G., Turpen, A. M., Donson, J., Hilf, M. E., Grantham, G. L., Dawson, W. O., Chow, T. P., Piatak, M. Jr. and Grill, L. K. 1993. Rapid, high-level expression of biologically active α-trichosanthin in transfected plants by an RNA viral vector. Proc. Natl. Acad. Sci. USA 90:427-430.
7. Namba, K., Pattanayek, R. and Stubbs, G. 1989. Visualization of protein-nucleic acid interactions in a virus. Refined structure of intact tobacco mosaic virus at 2.9 Xresolution by X-ray fiber diffraction. J. Mol. Biol. 208:307-325.
8. Culver, J. N., Lindbeck, A. G. C. and Dawson, W. O. 1991. Virus-host interactions: Induction of chlorotic and necrotic responses in plants by tobamoviruses. Annu. Rev. Phytopathology 29:193-217.
9. Takamatsu, N., Watanabe, Y., Yanagi, H, Mcshi, T., Shiba, T. and Okada, Y. 1990. Production of enkephalin in tobacco protoplasts using tobacco mosaic vims RNA vector. FEBS Lett. 269:73-76.
10. Pelham, H.R.B. 1978. Leaky UAG termination codon in tobacco mosaic virus RNA. Nature 272:469-471.
11. Skuzeski, J. M., Nichols, L. M., Gesteland, R. F. and Atkins, J. F. 1991. The signal for a leaky UAG stop codon in several plant viruses includes the two downstream codons. J. Mol. Biol. 218:365-373.
12. Zerfass, K. and Beier. H. 1992. Pseudouridine in the anticodon G*A of plant cytoplasmic tRNATïr is required for UAG and UAA suppression in the TMV-specific context. Nuc. Ac. Res. 20:5911-5918.
13. Hamamoto, H., Sugiyama, Y., Nakagawa, N., Hashida, E., Matsunaga, Y, Takemoto, S., Watanabe, Y. and Okada, Y. 1993. A new tobacco mosaic virus vector and its use for the systemic production of angiotensin-I-converting enzyme inhibitor in transgenic tobacco and tomato. Bio/Technology 11:930-932.
14. Charoenvit, Y, Mellouk, S., Cole, C, Bechara, R., Leef, M. F., Sedegah, M., Yuan, L. F., Robey, F. A., Beaudoin, R. L. and Hoffman, S. L. 1991. Monoclonal, but not polyclonal, antibodies protect against Plasmodium yoelii sporo-zoites. J. Immunol. 146:1020-1025.
15. Charoenvit, Y., Collins, W. E., Jones, T. R., Millet, P., Yuan, L, Campbell, G. H., Beaudoin, R. L., Broderson, J. R. and Hoffman, S. L. 1991. Inability of malaria vaccine to induce antibodies to a protective epitope within its sequence. Science 251:668-671.
16. Gooding, G. V. Jr. and Hebert, T. T. 1967. A simple technique for purification of tobacco mosaic virus in large quantities. Phytopathology 57:1285.
17. Rappaport, I. 1965. The antigenic structure of tobacco mosaic virus. Adv. Virus Res. 11:223-275.
18. Valenzuela, P., Coit, D., Medina-Selby, M. A., Kuo, C. H., Van Nest, G., Burke, R. L., Bull, P., Urdea, M. C. and Graves, P. V. 1985. Antigen engineering in yeast: Synthesis and assembly of hybrid hepatitis B surface antigen-herpes simplex 1 gD particles. Bio/Technology 3:323-326.
19. Westhof, E., Altschuh, D., Moras, D., Bloomer, A. C, Mondragon, A., Klug, A. and Van Regenmortel, M. H. V. 1984. Correlation between segmental mobility and the location of antigenic determinants in proteins. Nature 311:123126.
20. Namba, K. and Stubbs, G. 1986. Structure of tobacco mosaic virus at 3.6 À resolution: Implications for assembly. Science 231:1401-1406.
21. Van Regenmortel, M. H. V. 1986. Tobacco mosaic virus. Antigenic structure, p. 79-104. In: The Plant Viruses. The Rod-Shaped Plant Viruses (Van Regenmortel, M. H. V, Fraenkel-Conrat, H.) (Eds.). Plenum Press, New York.
22. Dawson, W. O. 1991. The pathogenicity of tobacco mosaic virus. Sem. Virol. 2:131-137.
23. Lindbeck, A. G. C, Lewandowski, D. J., Culver, J. N., Thomson, W. W. and Dawson, W. O. 1992. Mutant coat protein of tobacco mosaic virus induces acute chlorosis in expanded and developing tobacco leaves. Mol. Plant-Microbe Interact. 5:235-241.
24. Kearney, C. M., Donson, J, Jones, G. E. and Dawson, W. O. 1993. Low level of genetic drift in foreign sequences replicating in an RNA virus in plants. Virology 192:11-17.
25. Mason, H. S., Lam, D. M-K. and Arntzen, C. J. 1992. Expression of hepatitis B surface antigen in transgenic plants. Proc. Natl. Acad. Sci. USA 89:1174511749.
26. Sambrook, J., Fritsch, E. F. and Maniatis, T. 1989. Molecular Cloning: A Laboratory Manual, 2nd Ed., Cold Spring Harbor Laboratory, Cold Spring Harbor, New York.
27. Yanisch-Perron, C, Vieira, J. and Messing, J. 1985. Improved M13 cloning vectors and host strains: nucleotide sequences of the M13mpl8 and pUC19 vectors. Gene 33:103-119.
28. Goelet, P., Lomonossoff, G. P., Butler, P. J. G., Akam, M. E., Gait, M. J. and Karn, J. 1982. Nucleotide sequence of tobacco mosaic virus RNA. Proc. Natl, Acad Sci. USA 79:5818-5822.
29. Kraulis, P. J. 1991. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24:946-950.
30. Saiki, R. K., Scharf, S., Faloona, F. A., Muliis, K. B., Horn, G. T., Erlich, H. A. and Amheim, N. 1985. Enzymatic amplification of 0-globin genomic sequences and restriction site analysis for diagnosis of sickle cell anemia. Science 230:1350-1354.
31. Sanger, F., Nicklen, S. and Coulson, A. R. 1977. DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. USA 74:5463-5467.
32. Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
33. Towbin, H., Staehelin, T. and Gordon, J. 1979. Electrophoretic transfer of proteins from Polyacrylamide gels to nitrocellulose sheets: Procedure and some applications. Proc. Natl. Acad. Sci. USA 76:4350-4354.