Autocatalytic activity and substrate specificity of the pestivirus N-terminal protease Npro

Virology

Volumn 452-453, Issue , 2014, Pages 303-309

  Gottipati, Keerthi ^a   Acholi, Sudheer ^a   Ruggli, Nicolas ^b   Choi, Kyung H ^a  

^a University of Texas Medical Branch School of Medicine   (United States)

^b INSTITUTE OF VIROLOGY AND IMMUNOLOGY   (Switzerland)

Author keywords

Autoprotease; Classical swine fever virus; Cysteine protease; Mass spectrometry; Pestivirus; Self cleavage; Substrate specificity

Indexed keywords

GREEN FLUORESCENT PROTEIN; NUCLEOPHILE; PROTEINASE;

AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME SPECIFICITY; IN VITRO STUDY; NONHUMAN; PESTIVIRUS; PRIORITY JOURNAL; PROTEIN CLEAVAGE; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN STABILITY;

AUTOPROTEASE; CLASSICAL SWINE FEVER VIRUS; CYSTEINE PROTEASE; MASS SPECTROMETRY; N-TERMINAL PROTEASE N(PRO); PESTIVIRUS; SELF-CLEAVAGE; SUBSTRATE SPECIFICITY;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; BIOCATALYSIS; CATALYTIC DOMAIN; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PESTIVIRUS; SERINE ENDOPEPTIDASES; SUBSTRATE SPECIFICITY; VIRAL PROTEINS;

EID: 84896278871     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2014.01.026     Document Type: Article

References (21)

1. Achmuller C., Kaar W., Ahrer K., Wechner P., Hahn R., Werther F., Schmidinger H., Cserjan-Puschmann M., Clementschitsch F., Striedner G., Bayer K., Jungbauer A., Auer B. N(pro) fusion technology to produce proteins with authentic N termini in E. coli. Nat. Methods 2007, 4:1037-1043.
2. Bauhofer O., Summerfield A., Sakoda Y., Tratschin J.D., Hofmann M.A., Ruggli N. Classical swine fever virus Npro interacts with interferon regulatory factor 3 and induces its proteasomal degradation. J. Virol. 2007, 81:3087-3096.
3. Chen Z., Rijnbrand R., Jangra R.K., Devaraj S.G., Qu L., Ma Y., Lemon S.M., Li K. Ubiquitination and proteasomal degradation of interferon regulatory factor-3 induced by Npro from a cytopathic bovine viral diarrhea virus. Virology 2007, 366:277-292.
4. Crameri A., Whitehorn E.A., Tate E., Stemmer W.P. Improved green fluorescent protein by molecular evolution using DNA shuffling. Nat. Biotechnol. 1996, 14:315-319.
5. Fukuda H., Arai M., Kuwajima K. Folding of green fluorescent protein and the cycle3 mutant. Biochemistry 2000, 39:12025-12032.
6. Gil L.H., Ansari I.H., Vassilev V., Liang D., Lai V.C., Zhong W., Hong Z., Dubovi E.J., Donis R.O. The amino-terminal domain of bovine viral diarrhea virus Npro protein is necessary for alpha/beta interferon antagonism. J. Virol. 2006, 80:900-911.
7. Gottipati K., Ruggli N., Gerber M., Tratschin J.D., Benning M., Bellamy H., Choi K.H. The structure of classical swine fever virus N(pro): A novel cysteine autoprotease and zinc-binding protein involved in subversion of type I interferon induction. PLoS Pathog. 2013, 9:e1003704.
8. Hilton L., Moganeradj K., Zhang G., Chen Y.H., Randall R.E., McCauley J.W., Goodbourn S. The NPro product of bovine viral diarrhea virus inhibits DNA binding by interferon regulatory factor 3 and targets it for proteasomal degradation. J. Virol. 2006, 80:11723-11732.
9. Lawson M.A., Semler B.L. Poliovirus thiol proteinase 3C can utilize a serine nucleophile within the putative catalytic triad. Proc. Natl. Acad. Sci. USA 1991, 88:9919-9923.
10. Lindenbach B.D., Thiel H.J., Rice C.M. Flaviviridae: the viruses and their replication. Fields Virology 5th ed. 2007, 1101-1152. Lippincott-Raven Publishers, Philadelphia, PA. D.M. Knipe, P.M. Howley (Eds.).
11. Meyers G., Thiel H.J. Molecular characterization of pestiviruses. Adv. Virus Res. 1996, 47:53-118.
12. Rawlings N.D., Barrett A.J., Bateman A. MEROPS: the database of proteolytic enzymes, their substrates and inhibitors. Nucl. Acids Res. 2012, 40:D343-350.
13. Ruggli N., Summerfield A., Fiebach A.R., Guzylack-Piriou L., Bauhofer O., Lamm C.G., Waltersperger S., Matsuno K., Liu L., Gerber M., Choi K.H., Hofmann M.A., Sakoda Y., Tratschin J.D. Classical swine fever virus can remain virulent after specific elimination of the interferon regulatory factor 3-degrading function of Npro. J. Virol. 2009, 83:817-829.
14. Ruggli N., Tratschin J.D., Schweizer M., McCullough K.C., Hofmann M.A., Summerfield A. Classical swine fever virus interferes with cellular antiviral defense: evidence for a novel function of N(pro). J. Virol. 2003, 77:7645-7654.
15. Rumenapf T., Stark R., Heimann M., Thiel H.J. N-terminal protease of pestiviruses: identification of putative catalytic residues by site-directed mutagenesis. J. Virol. 1998, 72:2544-2547.
16. Schechter I., Berger A. On the size of the active site in proteases. I. Papain. Biochem. Biophys. Res. Commun. 1967, 27:157-162.
17. Stark R., Meyers G., Rumenapf T., Thiel H.J. Processing of pestivirus polyprotein: cleavage site between autoprotease and nucleocapsid protein of classical swine fever virus. J. Virol. 1993, 67:7088-7095.
18. Szymanski M.R., Fiebach A.R., Tratschin J.D., Gut M., Ramanujam V.M., Gottipati K., Patel P., Ye M., Ruggli N., Choi K.H. Zinc binding in pestivirus N(pro) is required for interferon regulatory factor 3 interaction and degradation. J. Mol. Biol. 2009, 391:438-449.
19. Tratschin J.D., Moser C., Ruggli N., Hofmann M.A. Classical swine fever virus leader proteinase Npro is not required for viral replication in cell culture. J, Virol, 1998, 72:7681-7684.
20. Wiskerchen M., Belzer S.K., Collett M.S. Pestivirus gene expression: the first protein product of the bovine viral diarrhea virus large open reading frame, p20, possesses proteolytic activity. J, Virol, 1991, 65:4508-4514.
21. Zogg T., Sponring M., Schindler S., Koll M., Schneider R., Brandstetter H., Auer B. Crystal structures of the viral protease npro imply distinct roles for the catalytic water in catalysis. Structure 2013, 21:929-938.