Myristoylation of the poliovirus polyprotein is required for proteolytic processing of the capsid and for viral infectivity.
作者： H G Kräusslich , C Hölscher , Q Reuer , J Harber , E Wimmer
DOI: 10.1128/JVI.64.5.2433-2436.1990
关键词: Viral replication 、 RNA 、 Poliovirus 、 Biology 、 Protein biosynthesis 、 Mutant 、 Myristic acid 、 Molecular biology 、 Myristoylation 、 Capsid
摘要: The poliovirus polyprotein is cotranslationally linked to myristic acid at its amino-terminal glycine residue. We investigated the role of myristoylation in viral replication cycle by site-directed mutagenesis this codon. Synthetic full-length RNA transcripts carrying a Gly-to-Ala mutation (G4002A) gave no infectious virus on transfection into permissive cells (HeLa). However, mutant was replicated transfected cells, albeit reduced level. virus-specific polypeptide P1, precursor for capsid proteins, found HeLa with wild-type or RNA, but only P1 myristoylated; G4002A not myristoylated. also introduced an vitro transcription-translation vector encoding precursor. Processing poliovirus-infected cell lysate (providing 3Cpro and 3CDpro activities) severely inhibited, whereas normally inefficient cleavage purified affected. These results suggest that moiety may be required efficient processing 3CDpro. Images
sci-hub.st 参考文章(23)
A J Dorner, L F Dorner, G R Larsen, E Wimmer, C W Anderson, Identification of the initiation site of poliovirus polyprotein synthesis. Journal of Virology. ,vol. 42, pp. 1017- 1028 ,(1982) , 10.1128/JVI.42.3.1017-1028.1982
P V Pallai, F Burkhardt, M Skoog, K Schreiner, P Bax, K A Cohen, G Hansen, D E H Palladino, K S Harris, M J Nicklin, E Wimmer, Cleavage of synthetic peptides by purified poliovirus 3C proteinase. Journal of Biological Chemistry. ,vol. 264, pp. 9738- 9741 ,(1989) , 10.1016/S0021-9258(18)81718-5
M J Nicklin, K S Harris, P V Pallai, E Wimmer, Poliovirus proteinase 3C: large-scale expression, purification, and specific cleavage activity on natural and synthetic substrates in vitro. Journal of Virology. ,vol. 62, pp. 4586- 4593 ,(1988) , 10.1128/JVI.62.12.4586-4593.1988
D. J. Filman, R. Syed, M. Chow, A. J. Macadam, P. D. Minor, J. M. Hogle, Structural factors that control conformational transitions and serotype specificity in type 3 poliovirus The EMBO Journal. ,vol. 8, pp. 1567- 1579 ,(1989) , 10.1002/J.1460-2075.1989.TB03541.X
Emilio A. Emini, William A. Schleif, Richard J. Colonno, Eckard Wimmer, Antigenic conservation and divergence between the viral-specific proteins of poliovirus type 1 and various picornaviruses Virology. ,vol. 140, pp. 13- 20 ,(1985) , 10.1016/0042-6822(85)90441-6
Mary Frances Ypma-Wong, Bert L. Semler, in vitro molecular genetics as a tool for determining the differential cleavage specificities of the polivirus 3C proteinase Nucleic Acids Research. ,vol. 15, pp. 2069- 2088 ,(1987) , 10.1093/NAR/15.5.2069
M. J. Nicklin, H. G. Krausslich, H. Toyoda, J. J. Dunn, E. Wimmer, Poliovirus polypeptide precursors: expression in vitro and processing by exogenous 3C and 2A proteinases. Proceedings of the National Academy of Sciences of the United States of America. ,vol. 84, pp. 4002- 4006 ,(1987) , 10.1073/PNAS.84.12.4002
Tsutomu Takegami, Bert L. Semler, Carl W. Anderson, Eckard Wimmer, Membrane fractions active in poliovirus RNA replication contain VPg precursor polypeptides. Virology. ,vol. 128, pp. 33- 47 ,(1983) , 10.1016/0042-6822(83)90316-1
A. V. Paul, A. Schultz, S. E. Pincus, S. Oroszlan, E. Wimmer, Capsid protein VP4 of poliovirus is N-myristoylated. Proceedings of the National Academy of Sciences of the United States of America. ,vol. 84, pp. 7827- 7831 ,(1987) , 10.1073/PNAS.84.22.7827
J. Jore, B. De Geus, R. J. Jackson, P. H. Pouwels, B. E. Enger-Valk, Poliovirus protein 3CD is the active protease for processing of the precursor protein P1 in vitro. Journal of General Virology. ,vol. 69, pp. 1627- 1636 ,(1988) , 10.1099/0022-1317-69-7-1627