Processing Determinants and Functions of Cleavage Products of Picornavirus Polyproteins

作者: Louis E.-C. Leong , Christopher T. Cornell , Bert L. Semler

DOI: 10.1128/9781555817916.CH16

关键词:

摘要: Picornaviruses employ a number of unique intracellular mechanisms and novel processes during their infectious cycles resulting in being among the most successful viral pathogens. This chapter begins with discussion features proteinases, continues an outline functions both precursor mature polypeptides present picornaviral infection, concludes brief summary nonviral substrates cleaved by proteinases. Viral proteinases including L protein, 2A proteinase 3C have been discussed chapter. The aphthoviruses cardioviruses code for protein at N terminus polyproteins. cleavage activity from foot-and-mouth disease virus (FMDV), aphthovirus, has well characterized. carries out majority proteolytic processing polyprotein. evolution picornaviruses might dictate that P1 to PN substrate positions be identical or similar optimize polyprotein maximize generation proteins. In vitro synthesized RNAs containing large inframe deletions within region are self-replicating cultured cells, suggesting proteins required RNA replication located primarily P2 P3 (nonstructural) regions genome. Since utilize mechanism translation is cap independent, it advantageous inhibit nonessential cap-dependent cellular translation.

参考文章(134)
M E Piccone, M Zellner, T F Kumosinski, P W Mason, M J Grubman, Identification of the active-site residues of the L proteinase of foot-and-mouth disease virus. Journal of Virology. ,vol. 69, pp. 4950- 4956 ,(1995) , 10.1128/JVI.69.8.4950-4956.1995
Alexander E. Gorbalenya, Alexei P. Donchenko, Vladimir M. Blinov, Eugene V. Koonin, Cysteine proteases of positive strand RNA viruses and chymotrypsin-like serine proteases. A distinct protein superfamily with a common structural fold. FEBS Letters. ,vol. 243, pp. 103- 114 ,(1989) , 10.1016/0014-5793(89)80109-7
K S Harris, S R Reddigari, M J Nicklin, T Hämmerle, E Wimmer, Purification and characterization of poliovirus polypeptide 3CD, a proteinase and a precursor for RNA polymerase. Journal of Virology. ,vol. 66, pp. 7481- 7489 ,(1992) , 10.1128/JVI.66.12.7481-7489.1992
K Strebel, E Beck, A second protease of foot-and-mouth disease virus. Journal of Virology. ,vol. 58, pp. 893- 899 ,(1986) , 10.1128/JVI.58.3.893-899.1986
R. Andino, G.E. Rieckhof, P.L. Achacoso, D. Baltimore, Poliovirus RNA synthesis utilizes an RNP complex formed around the 5'-end of viral RNA. The EMBO Journal. ,vol. 12, pp. 3587- 3598 ,(1993) , 10.1002/J.1460-2075.1993.TB06032.X
W A Charini, S Todd, G A Gutman, B L Semler, Transduction of a human RNA sequence by poliovirus. Journal of Virology. ,vol. 68, pp. 6547- 6552 ,(1994) , 10.1128/JVI.68.10.6547-6552.1994