Chemical conjugation of heterologous proteins on the surface of cowpea mosaic virus

Bioconjugate Chemistry

Volumn 15, Issue 4, 2004, Pages 807-813

  Chatterji, Anju ^a   Ochoa, Wendy ^a   Shamieh, Lara ^b   Salakian, Shant P ^a   Wong, Sek Man ^c   Clinton, Gail ^b   Ghosh, Partho ^d   Lin, Tianwei ^a   Johnson, John E ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

^b OREGON HEALTH AND SCIENCE UNIVERSITY   (United States)

^c NATIONAL UNIVERSITY OF SINGAPORE   (Singapore)

^d UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BINDING SITES; BIOACTIVITY; CROSSLINKING; ENZYME ACTIVITY; GENE EXPRESSION;

COWPEA MOSAIC VIRUS; EXPRESSION SYSTEM; HETEROLOGOUS PROTEINS; INFECTIOUS VIRIONS; INFECTIOUS VIRUS; LYSINE RESIDUES; PROPERTY; SUBUNIT GENES; SYMMETRIC DISTRIBUTIONS; VIRUS PARTICLES;

VIRUSES;

COAT PROTEIN; CYSTINE; EPIDERMAL GROWTH FACTOR RECEPTOR 2; GENE PRODUCT; HER2 TYROSINE KINASE RECEPTOR; INTERNALIN B; INTRON 8 GENE PRODUCT; LYSINE; LYSOZYME; POLYPEPTIDE; T4 LYSOZYME; UNCLASSIFIED DRUG; VIRUS PROTEIN;

ARTICLE; BINDING AFFINITY; CELL TYPE; CONJUGATION; COWPEA MOSAIC VIRUS; CROSS LINKING; DERIVATIZATION; DNA MODIFICATION; GENE EXPRESSION; GENETIC ENGINEERING; LRR DOMAIN; MOSAIC VIRUS; NONHUMAN; PROTEIN DOMAIN; PROTEIN STRUCTURE; STRUCTURE ANALYSIS; VIRION; VIRUS ADSORPTION; VIRUS CAPSID; VIRUS GENE; VIRUS PARTICLE; X RAY ANALYSIS;

COWPEA MOSAIC VIRUS;

EID: 3242816181     PISSN: 10431802     EISSN: None     Source Type: Journal    
DOI: 10.1021/bc0402888     Document Type: Article

References (45)

1. Lomonossoff, G. P., and Johnson, J. E. (1995) Viral expression system for peptides. Semin. Virol 6, 257-267.
2. Lomonossoff, G. P., and Johnson, J. E. (1996) Use of macromolecular assemblies as expression systems for peptides and synthetic vaccines. Curr. Opin. Struct. Biol. 6, 176-82.
3. Porta, C., Spall, V. E., Lin, T., Johnson, J. E., and Lomonossoff, G. P. (1996) The development of cowpea mosaic virus as a potential source of novel vaccines. Intervirology 39, 79-84.
4. Johnson, J. E., Lin, T., and Lomonossoff, G. P. (1997) Presentation of heterologous peptides on plant viruses: Genetics, structure and function. Annu. Rev. Phytopathol. 35, 67-86.
5. Porta, C., Spall, V. E., Loveland, J., Johnson, J. E., Barker, P J., and Lomonossoff, G. P. (2002) Development of cowpea mosaic virus as a high-yielding system for the presentation of foreign peptides. Virology 202, 949-55.
6. Lin, T., and Johnson, J. E. (2003) Structures of picorna like plant viruses: Implications and applications. Adv. Virus. Res. 62, 167-239.
7. Ernst, W. J., Spenger, A., Toellner, L., Katinger, H., and Grabherr, R. M. (2000) Expanding baculovirus surface display. Modification of the native coat protein gp64 of Autographa californica NPV. Eur. J. Biochem. 267, 4033-4039.
8. Gupta, A., Onda, M., Pastan, I., Adhya, S., and Chaudhary, V. (2003) High-density functional display of proteins on bacteriophage lambda. J. Mol. Biol. 334, 241-54.
9. Peabody, D. S. (2003) A Viral Platform for Chemical Modification and Multivalent Display. J. Nanobiotechnol. 1, 5-13.
10. Woiwode, T. F., Haggerty, J. E., Katz, R., Gallop, M. A., Barrett, R. W., Dower, W. J., and Cwirla, S. E. (2003) Synthetic compound libraries displayed on the surface of encoded bacteriophage. Chem. Biol. 10, 847-58.
11. Johnson, J. E., and Hollingshead, C. (1981) Crystallographic studies of cowpea mosaic virus by electron microscopy and X-ray diffraction. J. Ultrastruct. Res. 74, 223-231.
12. Porta, C., Wang, G., Cheng, H., Chen, Z., Baker, T. S., and Johnson, J. E. (1994) Direct imaging of interactions between an icosahedral virus and conjugate F(ab) fragments by cryoelectron microscopy and X-ray crystallography. Virology 204, 777-88.
13. Lin, T., Porta, C., Lomonossoff, G., and Johnson, J. E. (1996) Structure-based design of peptide presentation on a viral surface: the crystal structure of a plant/animal virus chimera at 2.8 A resolution. Fold Des. 1, 179-87.
14. Lin, T., Chen, Z., Usha, R., Stauffacher, C. V., Dai, J. B., Schmidt, T., and Johnson, J. E. (1999) The refined crystal structure of cowpea mosaic virus at 2.8 A resolution. Virology 265, 20-34.
15. Lin, T., Clark, A. J., Chen, Z., Shanks, M., Dai, J. B., Li, Y., Schmidt, T., Oxelfelt P., Lomonossoff, G. P., and Johnson, J. E. (2000) Structural fingerprinting: subgrouping of comoviruses by structural studies of red clover mottle virus to 2.4-A resolution and comparisons with other comoviruses. J. Virol. 74, 493-504.
16. Taylor, K. M., Porta, C., Lin, T., Johnson, J. E., Barker, P. J., and Lomonossoff, G. P. (1999) Position-dependent processing of peptides presented on the surface of cowpea mosaic virus. Biol. Chem. 380, 387-92.
17. Taylor, K. M., Lin, T., Porta, C., Mosser, A. G., Giesing, H. A., Lomonossoff, G. P., and Johnson, J. E. (2000) Influence of three-dimensional structure on the immunogenicity of a peptide expressed on the surface of a plant virus. J. Mol. Recognit. 13, 71-82.
18. Chatterji A., Burns, L. L., Taylor, S. S., Lomonossoff, G. P., Johnson, J. E., Lin T., and Porta, C. (2002) Cowpea mosaic virus: from the presentation of antigenic peptides to the display of active biomaterials. Intervirology 45, 362-70.
19. Porta, C., Spall, V. E., Findlay, K. C., Gergerich, R. C., Farrance, C. E., and Lomonossoff, G. P. (2003) Cowpea mosaic virus-based chimaeras. Effects of inserted peptides on the phenotype, host range, and transmissibility of the modified viruses. Virology 310, 50-63.
20. van Wezenbeek, P., Verver. J., Harmsen. J., Vos. P., and van Kammen. A. (1985) Primary structure and gene organization of the middle-component RNA of cowpea mosaic virus. EMBO J. 2,941-946.
21. Lomonossoff, G. P., and Shanks, M. (1983) The nucleotide sequence of cowpea mosaic virus B RNA. EMBO J. 2, 2253-2258.
22. Lomonossoff, G. P., and Johnson, J. E. (1991) The synthesis and structure of comovirus capsids. Prog. Biophys. Mol. Biol. 55, 107-37.
23. Chatterji A., Ochoa W., Paine, M., Ratna, B. R., Johnson, J. E., and Lin, T. (2004) New addresses on an addressable virus nanoblock: uniquely reactive lys residues on Cowpea mosaic virus. Chem. Biol., in press.
24. Wang, Q., Lin T., Johnson J. E., and Finn M. G. (2002) Natural supramolecular building blocks. Cysteine-added mutants of cowpea mosaic virus. Chem. Biol. 9, 813-819.
25. Wang Q., Kaltgrad, E., Lin, T., Johnson, J. E., and Finn M. G. (2002) Natural supramolecular building blocks. Wild-type cowpea mosaic virus. Chem. Biol. 9, 805-11.
26. Dessens, J. T., and Lomonossoff, G. P. (1993) Cauliflower mosaic virus 35S promoter controlled DNA copies of cowpea mosaic virus RNAs are infectious on plants. J. Gen. Virol. 74, 889-892.
27. Marino, M., Braun, L., Cossart, P., and Ghosh, P. (2001) Structure of the lnlB leucine-rich repeats, a domain that triggers host cell invasion by the bacterial pathogen L. monocytogenes. Mol. Cell. 4, 1063-72.
28. Doherty, J. K., Bond, C., Jardim, A., Adelman, J. P., and Clinton, G. M. (1999) The HER-2/neu receptor tyrosine kinase gene encodes a secreted autoinhibitor. Proc. Natl. Acad. Sci. U.S.A. 14, 10869-74.
29. Sulkowski, E. (1985) Purification of proteins by IMAC. Trends Biotechnol. 3, 1-7.
30. Hermanson, T. G. (1996) Bioconjugate techniques, Academic Press, San Diego, California.
31. Ausubel, F. M., Brent, R., Kingston, R. E., Moore, D. D., Seidman, J. G., Smith, J. A., and Struhl, K. (1999) Short Protocols on Molecular Biology, 4th ed., John Wiley and Sons, New York.
32. Shughar, D. (1952) The measuremnt of lysozyme activity and the ultraviolet inactivation of lysozyme. Biochem. Biophys. Acta 8, 302-309.
33. Frank J., Radermacher, M., Penczek, P., Zhu, J., Li, Y., Ladjadj, M., and Leith, A. (1996) SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields. J. Struct. Biol. 116, 190-199.
34. Jones, T. A., and Liljas, L. (1984) Crystallographic refinement of macromolecules having noncrystallographic symmetry. Acta Crystallogr. A 40, 50-57.
35. Esnouf, R. M. (1997) An extensively modified version of MolScript that includes greatly enhanced coloring capabilities. J. Mol. Graphics 15, 132-134.
36. Bierne H., and Cossart P. (2002) InlB, a surface protein of Listeria monocytogenes that behaves as an invasion and a growth factor. J. Cell Sci. 115, 3357-67.
37. Machner, M. P., Frese, S., Schubert, W. D., Orian-Rousseau, V., Gherardi, E., Wehland, J., Niemann, H. H., and Heinz, D. W. (2003) Aromatic amino acids at the surface of InlB are essential for host cell invasion by Listeria monocytogenes. Mol. Microbiol. 48, 1525-36.
38. Marino, M., Banerjee, M., Jonquieres, R., Cossart, P., and Ghosh, P. (2002) GW domains of the Listeria monocytogenes invasion protein InlB are SH3-like and mediate binding to host ligands. EMBO J. 121, 5623-34.
39. Shen, Y., Naujokas, M., Park, M., and Ireton, K. (2000) InIB-dependent internalization of Listeria is mediated by the Met receptor tyrosine kinase. Cell 103, 501-10.
40. Schubert, W. D., Gobel, G., Diepholz, M., Darji, A., Kloer, D., Hain, T., Chakraborty, T., Wehland, J., Domann, E., and Heinz, D. W. (2001) Internalins from the human pathogen Listeria monocytogenes combine three distinct folds into a contiguous internalin domain. J. Mol. Biol. 312, 783-94.
41. Azios, N. G., Romero, F. J., Denton, M. C., Doherty, J. K., and Clinton, G. M. (2001) Expression of herstatin, an autoinhibitor of HER-2/neu, inhibits transactivation of HER-3 by HER-2 and blocks EGF activation of the EGF receptor. Oncogene 20, 5199-209.
42. Molina, M. A., Saez, R., Ramsey, E. E., Garcia-Barchino, M. J., Rojo, F., Evans, A. J., Albanell, J., Keenan, E. J., Lluch, A., Garcia-Conde, J., Baselga, J., and Clinton, G. M. (2002) NH(2)-terminal truncated HER-2 protein but not full-length receptor is associated with nodal metastasis in human breast cancer. Clin. Cancer Res. 8, 347-53.
43. Justman, Q. A., and Clinton, G. M. (2003) Herstatin, an autoinhibitor of the human epidermal growth factor receptor2 Tyrosine kinase, modulates epidermal growth factor signaling pathways resulting in growth arrest. J. Biol. Chem. 277, 20618-20624.
44. Sia, S. K., and Kim, P. S. (2003) Protein grafting of an HIV-1-inhibiting epitope. Proc. Natl. Acad. Sci. U.S.A. 100, 9756-61.
45. Ye, Y., Shealy, S., Lee, H. W., Torshin, I., Harrison, R., and Yang, J. J. (2003) A grafting approach to obtain site-specific metal-binding properties of EF-hand proteins. Protein Eng. 16, 429-34.