Low stability of nucleocapsid protein in SARS virus

Biochemistry

Volumn 43, Issue 34, 2004, Pages 11103-11108

  Wang, Yulong ^a   Wu, Xiaoyu ^a   Wang, Yihua ^a   Li, Bing ^a   Zhou, Hao ^a   Yuan, Guiyong ^a   Fu, Yan ^a   Luo, Yongzhang ^a  

^a TSINGHUA UNIVERSITY   (China)

Author keywords

[No Author keywords available]

Indexed keywords

CLONING; GENES; ORGANIC ACIDS; PH EFFECTS; RNA; TITRATION; VIRUSES;

ACID TITRATION; NUCLEOCAPSID PROTEINS; SEVERE ACUTE RESPIRATORY SYNDROME (SARS); STRUCTURAL PROTEINS;

PROTEINS;

NUCLEOCAPSID PROTEIN; GUANIDINE; MONOVALENT CATION; SODIUM CHLORIDE; UREA;

ARTICLE; CIRCULAR DICHROISM; CORONAVIRUS; MOLECULAR CLONING; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN PURIFICATION; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; SARS CORONAVIRUS; TITRIMETRY; BIOSYNTHESIS; CHEMISTRY; GENETICS; HEAT; HUMAN; ISOLATION AND PURIFICATION; PH; PHYSIOLOGY; PROTEIN DENATURATION; SEVERE ACUTE RESPIRATORY SYNDROME; THERMODYNAMICS; VIROLOGY; VIRUS INACTIVATION;

CORONAVIRUS; SARS CORONAVIRUS;

CATIONS, MONOVALENT; GUANIDINE; HEAT; HUMANS; HYDROGEN-ION CONCENTRATION; NUCLEOCAPSID PROTEINS; PROTEIN DENATURATION; PROTEIN FOLDING; SARS VIRUS; SEVERE ACUTE RESPIRATORY SYNDROME; SODIUM CHLORIDE; THERMODYNAMICS; UREA; VIRUS INACTIVATION;

EID: 4644247362     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi049194b     Document Type: Article

References (32)

1. Fields, B. N., Knipe, D. M., Howley, P. M., and Griffin, D. E. (2001) Fields Virology, 4th ed., Lippincott Williams and Wilkins, Philadelphia, PA.
2. Marra, M. A., Jones, S. J., Astell, C. R., Holt, R. A., Brooks-Wilson, A., Butterfield, Y. S., Khattra, J., Asano, J. K., Barber, S. A., Chan, S. Y., Cloutier, A., Coughlin, S. M., Freeman, D., Girn, N., Griffith, O. L., Leach, S. R., Mayo, M., McDonald, H., Montgomery, S. B., Pandoh, P. K., Petrescu, A. S., Robertson, A. G., Schein, J. E., Siddiqui, A., Smailus, D. E., Stott, J. M., Yang, G. S., Plummer, F., Andonov, A., Artsob, H., Bastien, N., Bernard, K., Booth, T. F., Bowness, D., Czub, M., Drebot, M., Fernando, L., Flick, R., Garbutt, M., Gray, M., Grolla, A., Jones, S., Feldmann, H., Meyers, A., Kabani, A., Li, Y., Normand, S., Stroher, U., Tipples, G. A., Tyler, S., Vogrig, R., Ward, D., Watson, B., Brunham, R. C., Krajden, M., Petric, M., Skowronski, D. M., Upton, C., and Roper, R. L. (2003) The genome sequence of the SARS-associated coronavirus, Science 300, 1399-1404.
3. Rota, P. A., Oberste, M. S., Monroe, S. S., Nix, W. A., Campagnoli, R., Icenogle, J. P., Penaranda, S., Bankamp, B., Maher, K., Chen, M. H., Tong, S., Tamin, A., Lowe, L., Frace, M., DeRisi, J. L., Chen, Q., Wang, D., Erdman, D. D., Peret, T. C., Burns, C., Ksiazek, T. G., Rollin, P. E., Sanchez, A., Liffick, S., Holloway, B., Limor, J., McCaustland, K., Olsen-Rasmussen, M., Fouchier, R., Gunther, S., Osterhaus, A. D., Drosten, C., Pallansch, M. A., Anderson, L. J., and Bellini, W. J. (2003) Characterization of a novel coronavirus associated with severe acute respiratory syndrome, Science 300, 1394-1399.
4. Qin, E. D., Zhu, Q. Y., Yu, M., Fan, B. C., Chang, G. H., Si, B. Y., Yang, B. A., Peng, W. M., Jiang, T., Liu, B. H., Deng, Y. Q., Liu, H., Zhang, Y., Wang, C. E., Li, Y. Q., Gan, Y. H., Li, X. Y., Lü, F. H., Tan, G., Cao, W. C., and Yang, R. F. (2003) A complete sequence and comparative analysis of a SARS-associated virus (isolate BJ01), Chin. Sci. Bull. 48, 10941-10948.
5. Holmes, K. V., and Enjuanes, L. (2003) The SARS coronavirus: A postgenomic era, Science 300, 1377-1378.
6. Siddell, S. G., Ed. (1995) The Coronaviridae, Plenum, New York.
7. Chang, R. Y., and Brian, D. A. (1996) cis Requirement for N-specific protein sequence in bovine coronavirus defective interfering RNA replication, J. Virol. 70, 2201-2207.
8. Compton, S. R., Rogers, D. B., Holmes, K. V., Fertsch, D., Remenick, J., and McGowan, J. J. (1987) In vitro replication of mouse hepatitis virus strain A59, J. Virol. 61, 1814-1820.
9. Baric, R. S., Nelson, G, W., Fleming, J. O., Deans, R. J., Keck, J. G., Casteel, N., and Stohlman, S. A. (1988) Interaction between coronavirus nucleocapsid protein and viral RNAs: Implications for viral transcription, J. Virol. 62, 4280-4287.
10. Stohlman, S. A., Baric, R. S., Nelson, G. N., Soe, L. H., Welter, L. M., and Deans, R. J. (1988) Specific interaction between coronavirus leader RNA and nucleocapsid protein, J. Virol. 62, 4288-4295.
11. Ulmanen, I., Sodderlund, H., and Kaarianen, L. (1976) Forest virus capsid protein associates with 60S ribosomal subunit in infected cells, J. Virol. 20, 203-210.
12. Dimmock, N. J. (1967) Differences between the thermal inactivation of picornaviruses at "high" and "low" temperatures, Virology 31, 338-353.
13. Rombaut, B., Verheyden, B., Andries, K., and Boeyé A. (1994) Thermal inactivation of oral polio vaccine: Contribution of RNA and protein inactivation, J. Virol. 68, 6454-6457.
14. Edelhoch, H. (1967) Spectroscopic determination of tryptophan and tyrosine in proteins, Biochemistry 6, 1948-1954.
15. Li, B., Wu, X., Zhou, H., Chen, Q., and Luo, Y. (2004) Acid-induced unfolding mechanism of recombinant human endostatin, Biochemistry 43, 2550-2557.
16. Santoro, M. M., and Bolen, D. W. (1988) Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl α-chymotrypsin using different denaturants, Biochemistry 27, 8063-8068.
17. Luo, Y., and Baldwin, R. L. (1998) Trifluoroethanol stabilizes the pH 4 folding intermediate of sperm whale apomyoglobin, J. Mol. Biol. 279, 49-57.
18. Arai, M., Ikura, T., Semisotnov, G. V., Kihara, H., Amemiya, Y., and Kuwajima, K. (1998) Kinetic refolding of β-lactoglobulin. Studies by synchrotron X-ray scattering, and circular dichroism, absorption, and fluorescence spectroscopy, J. Mol. Biol. 275, 149-162.
19. Luo, Y., Kay, M. S., and Baldwin, R. L. (1997) Cooperativity of folding of the apomyoglobin pH 4 intermediate studied by glycine and proline mutations, Nat. Struct. Biol. 4, 925-930.
20. Luo, Y., and Baldwin, R. L. (1999) The 28-111 disulfide bond constrains the α-lactalbumin molten globule and weakens its cooperativity of folding, Proc. Natl. Acad. Sci. U.S.A. 96, 11283-11287.
21. Fukada, H., and Takahashi, K. (1998) Enthalpy and heat capacity changes for the proton dissociation of various buffer components in 0.1 M potassium chloride, Proteins 33, 159-166.
22. Makhatadze, G. I., Lopez, M. M., Richardson, J. M., III, and Thomas, S. T. (1998) Anion binding to the ubiquitin molecule, Protein Sci. 7, 689-697.
23. Bedell, J. L., McCrary, B. S., Edmondson, S. P., and Shriver, J. W. (2000) The acid-induced folded state of Sac7d is the native state, Protein Sci. 9, 1878-1888.
24. Sakurai, K., Oobatake, M., and Goto, Y. (2001) Salt-dependent monomer-dimer equilibrium of bovine β-lactoglobulin at pH 3, Protein Sci. 10, 2325-2335.
25. Ramos, C. H. I., and Baldwin, R. L. (2002) Sulfate anion stabilization of native ribonuclease A both by anion binding and by the Hofmeister effect, Protein Sci. 11, 1771-1778.
26. Jencks, W. P. (1987) Catalysis, in Chemistry and Enzymology, pp 358-392, Dover, Mineola, NY.
27. Goto, Y., Calciano, L. J., and Fink, A. L. (1990) Acid-induced folding of proteins, Proc. Natl. Acad. Sci. U.S.A. 87, 573-577.
28. Jané-Valbuena, J., Nibert, M. L., Spencer, S. M., Walker, S. B., Baker, T. S., Chen, Y., Centonze, V. E., and Schiff, L. A. (1999) Reovirus virion-like particles obtained by recoating infectious subvirion particles with baculovirus-expressed σ3 protein: An approach for analyzing σ3 functions during virus entry, J. Virol. 73, 2963-2973.
29. Wessner, D. R., and Fields, B. N. (1993) Isolation and genetic characterization of ethanol-resistant reovirus mutants, J. Virol. 67, 2442-2447.
30. Hooper, J. W., and Fields, B. N. (1996) Role of the μ1 protein in reovirus stability and capacity to cause chromium release from host cells, J. Virol. 70, 459-467.
31. Kumar, S., and Nussinov, R. (2001) How do thermophilic proteins deal with heat? Cell. Mol. Life Sci. 58, 1216-1233.
32. Duan, S. M., Zhao, X. S., Wen, R. F., Huang, J. J., Pi, G. H., Zhang, S. X., Han, J., Bi, S. L., Ruan, L., Dong, X. P., and SARS Research Team (2003) Stability of SARS coronavirus in human specimen and environment and its sensitivity to heating and UV irradiation, Biomed. Environ. Sci. 16, 105-111.