Processing and localization of Dengue virus type 2 polyprotein precursor NS3-NS4A-NS4B-NS5
- PMID: 1433530
- PMCID: PMC240467
- DOI: 10.1128/JVI.66.12.7549-7554.1992
Processing and localization of Dengue virus type 2 polyprotein precursor NS3-NS4A-NS4B-NS5
Abstract
Processing of dengue virus type 2 polyprotein precursor NS3-NS4A-NS4B-NS5 could be mediated by the catalytically active NS3 protease domain and NS2B in trans at the dibasic sites NS3-NS4A and NS4B-NS5. Subcellular localization of the unprocessed precursor NS3-NS4A-NS4B-NS5 showed that it was confined to a distinct subcellular organelle in the cytoplasm, which was distinct from the distribution of the mature NS5.
Similar articles
-
Cleavage of the dengue virus polyprotein at the NS3/NS4A and NS4B/NS5 junctions is mediated by viral protease NS2B-NS3, whereas NS4A/NS4B may be processed by a cellular protease.J Virol. 1992 Mar;66(3):1535-42. doi: 10.1128/JVI.66.3.1535-1542.1992. J Virol. 1992. PMID: 1531368 Free PMC article.
-
Role of protein conformation in the processing of dengue virus type 2 nonstructural polyprotein precursor.Gene. 1993 Jul 30;129(2):197-205. doi: 10.1016/0378-1119(93)90269-9. Gene. 1993. PMID: 8325506
-
Both nonstructural proteins NS2B and NS3 are required for the proteolytic processing of dengue virus nonstructural proteins.J Virol. 1991 May;65(5):2467-75. doi: 10.1128/JVI.65.5.2467-2475.1991. J Virol. 1991. PMID: 2016768 Free PMC article.
-
The Dengue Virus Replication Complex: From RNA Replication to Protein-Protein Interactions to Evasion of Innate Immunity.Adv Exp Med Biol. 2018;1062:115-129. doi: 10.1007/978-981-10-8727-1_9. Adv Exp Med Biol. 2018. PMID: 29845529 Review.
-
Dengue virus NS2 and NS4: Minor proteins, mammoth roles.Biochem Pharmacol. 2018 Aug;154:54-63. doi: 10.1016/j.bcp.2018.04.008. Epub 2018 Apr 17. Biochem Pharmacol. 2018. PMID: 29674002 Review.
Cited by
-
Structures and Dynamics of Dengue Virus Nonstructural Membrane Proteins.Membranes (Basel). 2022 Feb 17;12(2):231. doi: 10.3390/membranes12020231. Membranes (Basel). 2022. PMID: 35207152 Free PMC article. Review.
-
Dynamics and binding interactions of peptide inhibitors of dengue virus entry.J Biol Phys. 2019 Mar;45(1):63-76. doi: 10.1007/s10867-018-9515-6. Epub 2019 Jan 24. J Biol Phys. 2019. PMID: 30680580 Free PMC article.
-
Autocatalytic activation of a malarial egress protease is druggable and requires a protein cofactor.EMBO J. 2021 Jun 1;40(11):e107226. doi: 10.15252/embj.2020107226. Epub 2021 May 1. EMBO J. 2021. PMID: 33932049 Free PMC article.
-
Design, structure-based focusing and in silico screening of combinatorial library of peptidomimetic inhibitors of Dengue virus NS2B-NS3 protease.J Comput Aided Mol Des. 2010 Mar;24(3):195-212. doi: 10.1007/s10822-010-9326-8. Epub 2010 Mar 21. J Comput Aided Mol Des. 2010. PMID: 20306283
-
Functional interplay among the flavivirus NS3 protease, helicase, and cofactors.Virol Sin. 2014 Apr;29(2):74-85. doi: 10.1007/s12250-014-3438-6. Epub 2014 Mar 26. Virol Sin. 2014. PMID: 24691778 Free PMC article. Review.
References
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Research Materials