Internal cleavages of hepatitis C virus NS3 induced by P1 mutations at the NS3/4A cleavage site

Virology

Volumn 383, Issue 2, 2009, Pages 271-278

  Hou, Xiaohong ^a   Yang, Wengang ^a   Zhao, Yongsen ^a   Agarwal, Atul ^a   Huang, Mingjun ^a  

^a Achillion Pharmaceuticals   (United States)

Author keywords

Alternative cleavage; cis cleavage; NS3; Polyprotein processing

Indexed keywords

NONSTRUCTURAL PROTEIN 3; NONSTRUCTURAL PROTEIN 4A; PROTEINASE INHIBITOR;

ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; GENE MUTATION; HEPATITIS C VIRUS; HEPATOMA CELL; HUMAN; HUMAN CELL; NONHUMAN; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN PROCESSING; PROTEIN PROTEIN INTERACTION;

CARRIER PROTEINS; HEPACIVIRUS; MODELS, MOLECULAR; MUTATION, MISSENSE; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN STRUCTURE, TERTIARY; VIRAL NONSTRUCTURAL PROTEINS; VIRAL PROTEINS;

HEPATITIS C VIRUS;

EID: 58149107260     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2008.10.037     Document Type: Article

References (35)

1. Bartenschlager R., Ahlborn-Laake L., Mous J., and Jacobsen H. Nonstructural protein 3 of the hepatitis C virus encodes a serine-type proteinase required for cleavage at the NS3/4 and NS4/5 junctions. J. Virol. 67 7 (1993) 3835-3844
2. Bartenschlager R., Ahlborn-Laake L., Mous J., and Jacobsen H. Kinetic and structural analyses of hepatitis C virus polyprotein processing. J. Virol. 68 8 (1994) 5045-5055
3. Bartenschlager R., Ahlborn-Laake L., Yasargil K., Mous J., and Jacobsen H. Substrate determinants for cleavage in cis and in trans by the hepatitis C virus NS3 proteinase. J. Virol. 69 1 (1995) 198-205
4. Brass V., Berke J.M., Montserret R., Blum H.E., Penin F., and Moradpour D. Structural determinants for membrane association and dynamic organization of the hepatitis C virus NS3-4A complex. Proc. Natl. Acad. Sci. U. S. A. 105 38 (2008) 14545-14550
5. Choo Q.L., Richman K.H., Han J.H., Berger K., Lee C., Dong C., Gallegos C., Coit D., Medina-Selby R., Barr P.J., et al. Genetic organization and diversity of the hepatitis C virus. Proc. Natl. Acad. Sci. U. S. A. 88 6 (1991) 2451-2455
6. Choo Q., Kuo G., Weiner A., Overby L., Bradley D., and Houghton M. Isolation of a cDNA clone derived from a blood-borne non-A, non-B viral hepatitis genome [Science 1989;244:359-362]. J. Hepatol. 36 5 (2002) 582-585
7. Dubuisson J. Hepatitis C virus proteins. World J. Gastroenterol. 13 17 (2007) 2406-2415
8. Failla C., Tomei L., and De Francesco R. Both NS3 and NS4A are required for proteolytic processing of hepatitis C virus nonstructural proteins. J. Virol. 68 6 (1994) 3753-3760
9. Gallinari P., Paolini C., Brennan D., Nardi C., Steinkuhler C., and De Francesco R. Modulation of hepatitis C virus NS3 protease and helicase activities through the interaction with NS4A. Biochemistry 38 17 (1999) 5620-5632
10. Grakoui A., McCourt D.W., Wychowski C., Feinstone S.M., and Rice C.M. Characterization of the hepatitis C virus-encoded serine proteinase: determination of proteinase-dependent polyprotein cleavage sites. J. Virol. 67 5 (1993) 2832-2843
11. Hijikata M., Mizushima H., Akagi T., Mori S., Kakiuchi N., Kato N., Tanaka T., Kimura K., and Shimotohno K. Two distinct proteinase activities required for the processing of a putative nonstructural precursor protein of hepatitis C virus. J. Virol. 67 8 (1993) 4665-4675
12. Ho S.N., Hunt H.D., Horton R.M., Pullen J.K., and Pease L.R. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77 1 (1989) 51-59
13. Kim D.W., Gwack Y., Han J.H., and Choe J. C-terminal domain of the hepatitis C virus NS3 protein contains an RNA helicase activity. Biochem. Biophys. Res. Commun. 215 1 (1995) 160-166
14. Kim J.L., Morgenstern K.A., Lin C., Fox T., Dwyer M.D., Landro J.A., Chambers S.P., Markland W., Lepre C.A., O'Malley E.T., Harbeson S.L., Rice C.M., Murcko M.A., Caron P.R., and Thomson J.A. Crystal structure of the hepatitis C virus NS3 protease domain complexed with a synthetic NS4A cofactor peptide. Cell 87 2 (1996) 343-355
15. Kolykhalov A.A., Agapov E.V., and Rice C.M. Specificity of the hepatitis C virus NS3 serine protease: effects of substitutions at the 3/4A, 4A/4B, 4B/5A, and 5A/5B cleavage sites on polyprotein processing. J. Virol. 68 11 (1994) 7525-7533
16. Kou Y.H., Chang M.F., Wang Y.M., Hong T.M., and Chang S.C. Differential requirements of NS4A for the internal NS3 cleavage and polyprotein processing of hepatitis C virus. J. Virol. 23 (2007) 23
17. Kraut J. Serine proteases: structure and mechanism of catalysis. Annu. Rev. Biochem. 46 (1977) 331-358
18. Leinbach S.S., Bhat R.A., Xia S.M., Hum W.T., Stauffer B., Davis A.R., Hung P.P., and Mizutani S. Substrate specificity of the NS3 serine proteinase of hepatitis C virus as determined by mutagenesis at the NS3/NS4A junction. Virology 204 1 (1994) 163-169
19. Lin C., Pragai B.M., Grakoui A., Xu J., and Rice C.M. Hepatitis C virus NS3 serine proteinase: trans-cleavage requirements and processing kinetics. J. Virol. 68 12 (1994) 8147-8157
20. Lohmann V., Korner F., Koch J., Herian U., Theilmann L., and Bartenschlager R. Replication of subgenomic hepatitis C virus RNAs in a hepatoma cell line. Science 285 5424 (1999) 110-113
21. Lorenz I.C., Marcotrigiano J., Dentzer T.G., and Rice C.M. Structure of the catalytic domain of the hepatitis C virus NS2-3 protease. Nature 442 7104 (2006) 831-835
22. Love R.A., Parge H.E., Wickersham J.A., Hostomsky Z., Habuka N., Moomaw E.W., Adachi T., and Hostomska Z. The crystal structure of hepatitis C virus NS3 proteinase reveals a trypsin-like fold and a structural zinc binding site. Cell 87 2 (1996) 331-342
23. Schechter I., and Berger A. On the size of the active site in proteases. I. Papain. Biochem. Biophys. Res. Commun. 27 2 (1967) 157-162
24. Shoji I., Suzuki T., Sato M., Aizaki H., Chiba T., Matsuura Y., and Miyamura T. Internal processing of hepatitis C virus NS3 protein. Virology 254 2 (1999) 315-323
25. Sikora B., Chen Y., Lichti C.F., Harrison M.K., Jennings T.A., Tang Y., Tackett A.J., Jordan J.B., Sakon J., Cameron C.E., and Raney K.D. Hepatitis C virus NS3 helicase forms oligomeric structures that exhibit optimal DNA unwinding activity in vitro. J. Biol. Chem. 283 17 (2008) 11516-11525
26. Takamizawa A., Mori C., Fuke I., Manabe S., Murakami S., Fujita J., Onishi E., Andoh T., Yoshida I., and Okayama H. Structure and organization of the hepatitis C virus genome isolated from human carriers. J. Virol. 65 3 (1991) 1105-1113
27. Tellinghuisen T.L., Marcotrigiano J., and Rice C.M. Structure of the zinc-binding domain of an essential component of the hepatitis C virus replicase. Nature 435 7040 (2005) 374-379
28. Varaklioti A., Vassilaki N., Georgopoulou U., and Mavromara P. Alternate translation occurs within the core coding region of the hepatitis C viral genome. J. Biol. Chem. 277 20 (2002) 17713-17721
29. Vrolijk J.M., Kaul A., Hansen B.E., Lohmann V., Haagmans B.L., Schalm S.W., and Bartenschlager R. A replicon-based bioassay for the measurement of interferons in patients with chronic hepatitis C. J. Virol. Methods 110 2 (2003) 201-209
30. Walewski J.L., Keller T.R., Stump D.D., and Branch A.D. Evidence for a new hepatitis C virus antigen encoded in an overlapping reading frame. RNA 7 5 (2001) 710-721
31. Wolk B., Sansonno D., Krausslich H.G., Dammacco F., Rice C.M., Blum H.E., and Moradpour D. Subcellular localization, stability, and trans-cleavage competence of the hepatitis C virus NS3-NS4A complex expressed in tetracycline-regulated cell lines. J. Virol. 74 5 (2000) 2293-2304
32. Xu Z., Choi J., Lu W., and Ou J.H. Hepatitis C virus F protein is a short-lived protein associated with the endoplasmic reticulum. J. Virol. 77 2 (2003) 1578-1583
33. Yan Y., Li Y., Munshi S., Sardana V., Cole J.L., Sardana M., Steinkuehler C., Tomei L., De Francesco R., Kuo L.C., and Chen Z. Complex of NS3 protease and NS4A peptide of BK strain hepatitis C virus: a 2.2 A resolution structure in a hexagonal crystal form. Protein Sci. 7 4 (1998) 837-847
34. Yang S.H., Lee C.G., Song M.K., and Sung Y.C. Internal cleavage of hepatitis C virus NS3 protein is dependent on the activity of NS34A protease. Virology 268 1 (2000) 132-140
35. Yao N., Reichert P., Taremi S.S., Prosise W.W., and Weber P.C. Molecular views of viral polyprotein processing revealed by the crystal structure of the hepatitis C virus bifunctional protease-helicase. Structure 7 11 (1999) 1353-1363