Both nonstructural proteins NS2B and NS3 are required for the proteolytic processing of dengue virus nonstructural proteins - PubMed (original) (raw)
Both nonstructural proteins NS2B and NS3 are required for the proteolytic processing of dengue virus nonstructural proteins
B Falgout et al. J Virol. 1991 May.
Abstract
The cleavages at the junctions of the flavivirus nonstructural (NS) proteins NS2A/NS2B, NS2B/NS3, NS3/NS4A, and NS4B/NS5 share an amino acid sequence motif and are presumably catalyzed by a virus-encoded protease. We constructed recombinant vaccinia viruses expressing various portions of the NS region of the dengue virus type 4 polyprotein. By analyzing immune precipitates of 35S-labeled lysates of recombinant virus-infected cells, we could monitor the NS2A/NS2B, NS2B/NS3, and NS3/NS4A cleavages. A polyprotein composed of NS2A, NS2B, and the N-terminal 184 amino acids of NS3 was cleaved at the NS2A/NS2B and NS2B/NS3 junctions, whereas a similar polyprotein containing only the first 77 amino acids of NS3 was not cleaved. This finding is consistent with the proposal that the N-terminal 180 amino acids of NS3 constitute a protease domain. Polyproteins containing NS2A and NS3 with large in-frame deletions of NS2B were not cleaved at the NS2A/NS2B or NS2B/NS3 junctions. Coinfection with a recombinant expressing NS2B complemented these NS2B deletions for NS2B/NS3 cleavage and probably also for NS2A/NS2B cleavage. Thus, NS2B is also required for the NS2A/NS2B and NS2B/NS3 cleavages and can act in trans. Other experiments showed that NS2B was needed, apparently in cis, for NS3/NS4A cleavage and for a series of internal cleavages in NS3. Indirect evidence that NS3 can also act in trans was obtained. Models are discussed for a two-component protease activity requiring both NS2B and NS3.
Similar articles
- Processing of Japanese encephalitis virus non-structural proteins: NS2B-NS3 complex and heterologous proteases.
Jan LR, Yang CS, Trent DW, Falgout B, Lai CJ. Jan LR, et al. J Gen Virol. 1995 Mar;76 ( Pt 3):573-80. doi: 10.1099/0022-1317-76-3-573. J Gen Virol. 1995. PMID: 7897348 - Role of protein conformation in the processing of dengue virus type 2 nonstructural polyprotein precursor.
Zhang L, Padmanabhan R. Zhang L, et al. Gene. 1993 Jul 30;129(2):197-205. doi: 10.1016/0378-1119(93)90269-9. Gene. 1993. PMID: 8325506 - The flavivirus NS2B-NS3 protease-helicase as a target for antiviral drug development.
Luo D, Vasudevan SG, Lescar J. Luo D, et al. Antiviral Res. 2015 Jun;118:148-58. doi: 10.1016/j.antiviral.2015.03.014. Epub 2015 Apr 2. Antiviral Res. 2015. PMID: 25842996 Review. - Towards the design of antiviral inhibitors against flaviviruses: the case for the multifunctional NS3 protein from Dengue virus as a target.
Lescar J, Luo D, Xu T, Sampath A, Lim SP, Canard B, Vasudevan SG. Lescar J, et al. Antiviral Res. 2008 Nov;80(2):94-101. doi: 10.1016/j.antiviral.2008.07.001. Epub 2008 Jul 30. Antiviral Res. 2008. PMID: 18674567 Review.
Cited by
- Erp57 facilitates ZIKV-induced DNA damage via NS2B/NS3 complex formation.
Wang Y, Song D, Li Y, Qin L, Wan Q, Hu H, Wu M, Feng Y, Schang L, Weiss R, He ML. Wang Y, et al. Emerg Microbes Infect. 2024 Dec;13(1):2417864. doi: 10.1080/22221751.2024.2417864. Epub 2024 Oct 28. Emerg Microbes Infect. 2024. PMID: 39404735 Free PMC article. - Natural products and derivatives as Japanese encephalitis virus antivirals.
Mi Y, Guo Y, Luo X, Bai Y, Chen H, Wang M, Wang Y, Guo J. Mi Y, et al. Pathog Dis. 2024 Feb 7;82:ftae022. doi: 10.1093/femspd/ftae022. Pathog Dis. 2024. PMID: 39317665 Free PMC article. Review. - Membrane Retention of West Nile Virus NS5 Depends on NS1 or NS3 for Enzymatic Activity.
Tseng AC, Nerurkar VR, Neupane KR, Kae H, Kaufusi PH. Tseng AC, et al. Viruses. 2024 Aug 16;16(8):1303. doi: 10.3390/v16081303. Viruses. 2024. PMID: 39205277 Free PMC article. - Pan-serotype dengue virus inhibitor JNJ-A07 targets NS4A-2K-NS4B interaction with NS2B/NS3 and blocks replication organelle formation.
Kiemel D, Kroell AH, Denolly S, Haselmann U, Bonfanti JF, Andres JI, Ghosh B, Geluykens P, Kaptein SJF, Wilken L, Scaturro P, Neyts J, Van Loock M, Goethals O, Bartenschlager R. Kiemel D, et al. Nat Commun. 2024 Jul 19;15(1):6080. doi: 10.1038/s41467-024-50437-3. Nat Commun. 2024. PMID: 39030239 Free PMC article. - Dengue virus non-structural protein 3 inhibits mitochondrial respiration by impairing complex I function.
Sousa BG, Mebus-Antunes NC, Fernandes-Siqueira LO, Caruso MB, Saraiva GN, Carvalho CF, Neves-Martins TC, Galina A, Zingali RB, Zeidler JD, Da Poian AT. Sousa BG, et al. mSphere. 2024 Jul 30;9(7):e0040624. doi: 10.1128/msphere.00406-24. Epub 2024 Jul 9. mSphere. 2024. PMID: 38980068 Free PMC article.
References
- J Gen Virol. 1974 Apr;23(1):91-6 - PubMed
- Virus Genes. 1990 Sep;4(3):197-213 - PubMed
- Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463-7 - PubMed
- J Virol. 1978 Feb;25(2):535-45 - PubMed
- Virology. 1978 Sep;89(2):423-37 - PubMed
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Research Materials
Miscellaneous