ArticleProceedings of the National Academy of Sciences of the United States of America1993
Flavivirus premembrane protein cleavage and spike heterodimer secretion require the function of the viral proteinase NS3.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.
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Who cites it
70 citing papers in PubMed, 140 citations in OpenAlex.
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- DENV2 Pseudoviral Particles with Unprocessed Capsid Protein Are Assembled and Infectious.Viruses · 2019Article
- Role of Capsid Anchor in the Morphogenesis of Zika Virus.Journal of virology · 2018Article
- Recent Advances in Zika Virus Vaccines.Viruses · 2018Review
- Early Events in Japanese Encephalitis Virus Infection: Viral Entry.Pathogens (Basel, Switzerland) · 2018Review
- Biochemistry and Molecular Biology of Flaviviruses.Chemical reviews · 2018Review
- The Multiples Fates of the Flavivirus RNA Genome During Pathogenesis.Frontiers in genetics · 2018Review
- Investigating Tick-borne Flaviviral-like Particles as a Delivery System for Gene Therapy.Current therapeutic research, clinical and experimental · 2018Article
- Organization of the Flavivirus RNA replicase complex.Wiley interdisciplinary reviews. RNA · 2017Review
10 more citing papers are in PubMed but not listed here.
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Flavivirus protein biosynthesis involves the proteolytic processing of a single polyprotein precursor by host- and virus-encoded proteinases. In this study, the requirement for the proteolytic function of the viral proteinase NS3 for correct processing of a polyprotein segment encompassing the Murray Valley encephalitis virus structural proteins is shown. The NS3-mediated cleavage in the structural polyprotein region presumably releases the capsid protein from its membrane anchor and triggers the appearance of the premembrane (prM) protein. This suggests that cleavage of prM by signal peptidase in the lumen of the endoplasmic reticulum is under control of a cytoplasmic cleavage catalyzed by a viral proteinase. The function of the viral proteinase is also essential for secretion of flaviviral spike proteins when expressed from cDNA via vaccinia virus recombinants or in COS cell transfections. This has important implications for the design of flavivirus subunit vaccines.
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