ArticleJournal of virology1998
Signal peptidase cleavage at the flavivirus C-prM junction: dependence on the viral NS2B-3 protease for efficient processing requires determinants in C, the signal peptide, and prM.
Article in Journal of virology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.
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Who cites it
77 citing papers in PubMed, 144 citations in OpenAlex.
- Signal peptidase complex mediates rotavirus VP7 processing and virion assembly.PLoS pathogens · 2026Article
- mRNA Vaccine Against Japanese Encephalitis Virus Genotype IV Protects Against Lethal Infection.Viruses · 2026Article
- In vitro synthesis of active recombinant orthoflavivirus nonstructural polyproteins in detergent micelles for biochemical analysis.Npj viruses · 2026Article
- Signal peptidase complex mediates rotavirus VP7 processing and virion assembly.bioRxiv : the preprint server for biology · 2025Article
- Pan-serotype dengue virus inhibitor JNJ-A07 targets NS4A-2K-NS4B interaction with NS2B/NS3 and blocks replication organelle formation.Nature communications · 2024Article
- Development of a novel virus-like particle-based vaccine for preventing tick-borne encephalitis virus infection.Virologica Sinica · 2023Article
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- An optimized messenger RNA vaccine candidate protects non-human primates from Zika virus infection.NPJ vaccines · 2023Article
- Assembly-defective Tembusu virus ectopically expressing capsid protein is an approach for live-attenuated flavivirus vaccine development.NPJ vaccines · 2022Article
- SPCS1-Dependent E2-p7 processing determines HCV Assembly efficiency.PLoS pathogens · 2022Article
- A mutation-mediated evolutionary adaptation of Zika virus in mosquito and mammalian host.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Review
- The EViruses · 2021Article
- Downstream Sequences Control the Processing of the Pestivirus EJournal of virology · 2020Article
- The role of capsid in the flaviviral life cycle and perspectives for vaccine development.Vaccine · 2020Review
- Review
- Development of a potent Zika virus vaccine using self-amplifying messenger RNA.Science advances · 2020Article
- DENV2 Pseudoviral Particles with Unprocessed Capsid Protein Are Assembled and Infectious.Viruses · 2019Article
- Formation of Virus-Like Particles of the Dengue Virus Serotype 2 Expressed in Silkworm Larvae.Molecular biotechnology · 2019Article
- Zika Virus NS2A-Mediated Virion Assembly.mBio · 2019Article
17 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Signal peptidase cleavage at the C-prM junction in the flavivirus structural polyprotein is inefficient in the absence of the cytoplasmic viral protease, which catalyzes cleavage at the COOH terminus of the C protein. The signal peptidase cleavage occurs efficiently in circumstances where the C protein is deleted or if the viral protease complex is present. In this study, we used cDNA of Murray Valley encephalitis virus (MVE) to examine features of the structural polyprotein which allow this regulation of a luminal cleavage by a cytoplasmic protease. We found that the inefficiency of signal peptidase cleavage in the absence of the viral protease is not attributable solely to features of the C protein. Inhibition of cleavage still occurred when charged residues in C were mutated to uncharged residues or when an unrelated protein sequence (that of ubiquitin) was substituted for C. Also, fusion of the C protein did not inhibit processing of an alternative adjacent signal sequence. The cleavage region of the flavivirus prM translocation signal is unusually hydrophobic, and we established that altering this characteristic by making three point mutations near the signal peptidase cleavage site in MVE prM dramatically increased the extent of cleavage without requiring removal of the C protein. In addition, we demonstrated that luminal sequences downstream from the signal peptidase cleavage site contributed to the inefficiency of cleavage.
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