Expression of virus-encoded proteinases: functional and structural similarities with cellular enzymes
- PMID: 8302216
- PMCID: PMC372939
- DOI: 10.1128/mr.57.4.781-822.1993
Expression of virus-encoded proteinases: functional and structural similarities with cellular enzymes
Abstract
Many viruses express their genome, or part of their genome, initially as a polyprotein precursor that undergoes proteolytic processing. Molecular genetic analyses of viral gene expression have revealed that many of these processing events are mediated by virus-encoded proteinases. Biochemical activity studies and structural analyses of these viral enzymes reveal that they have remarkable similarities to cellular proteinases. However, the viral proteinases have evolved unique features that permit them to function in a cellular environment. In this article, the current status of plant and animal virus proteinases is described along with their role in the viral replication cycle. The reactions catalyzed by viral proteinases are not simple enzyme-substrate interactions; rather, the processing steps are highly regulated, are coordinated with other viral processes, and frequently involve the participation of other factors.
Similar articles
-
Viral proteinases--possible targets of antiviral drugs.Acta Virol. 2002;46(3):131-40. Acta Virol. 2002. PMID: 12580374 Review.
-
The 35-kDa protein from the N-terminus of the potyviral polyprotein functions as a third virus-encoded proteinase.Virology. 1991 Dec;185(2):527-35. doi: 10.1016/0042-6822(91)90522-d. Virology. 1991. PMID: 1962435
-
The role of proteolytic processing in the morphogenesis of virus particles.Experientia. 1992 Feb 15;48(2):201-15. doi: 10.1007/BF01923512. Experientia. 1992. PMID: 1740191 Free PMC article. Review.
-
Effects of site-directed mutagenesis on the presumed catalytic triad and substrate-binding pocket of grapevine fanleaf nepovirus 24-kDa proteinase.Virology. 1992 Oct;190(2):884-8. doi: 10.1016/0042-6822(92)90931-e. Virology. 1992. PMID: 1519363
-
[A study of the complex of proteolytic enzymes and their protein inhibitors in embryogenesis of the silkworm].Ontogenez. 2001 Jul-Aug;32(4):269-76. Ontogenez. 2001. PMID: 11573423 Russian.
Cited by
-
An in silico approach for identification of novel inhibitors as potential therapeutics targeting COVID-19 main protease.J Biomol Struct Dyn. 2021 Aug;39(12):4304-4315. doi: 10.1080/07391102.2020.1776158. Epub 2020 Jun 16. J Biomol Struct Dyn. 2021. PMID: 32544024 Free PMC article.
-
First generation inhibitors of the adenovirus proteinase.FEBS Lett. 2013 Aug 2;587(15):2332-9. doi: 10.1016/j.febslet.2013.05.033. Epub 2013 May 24. FEBS Lett. 2013. PMID: 23711373 Free PMC article.
-
Functional analysis of the interaction between VPg-proteinase (NIa) and RNA polymerase (NIb) of tobacco etch potyvirus, using conditional and suppressor mutants.J Virol. 1999 Oct;73(10):8732-40. doi: 10.1128/JVI.73.10.8732-8740.1999. J Virol. 1999. PMID: 10482627 Free PMC article.
-
Arterivirus subgenomic mRNA synthesis and virion biogenesis depend on the multifunctional nsp1 autoprotease.J Virol. 2007 Oct;81(19):10496-505. doi: 10.1128/JVI.00683-07. Epub 2007 Jul 11. J Virol. 2007. PMID: 17626105 Free PMC article.
-
The coronavirus replicase.Curr Top Microbiol Immunol. 2005;287:57-94. doi: 10.1007/3-540-26765-4_3. Curr Top Microbiol Immunol. 2005. PMID: 15609509 Free PMC article. Review.
References
Publication types
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Full Text Sources
Other Literature Sources