ArticleProceedings of the National Academy of Sciences of the United States of America2016
Bunyamwera orthobunyavirus glycoprotein precursor is processed by cellular signal peptidase and signal peptide peptidase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 49 citations in OpenAlex.
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- A positive-sense single-stranded RNA virus acquired a negative-sense open reading frame through recombination.PLoS pathogens · 2025Article
- NSm is a critical determinant for bunyavirus transmission between vertebrate and mosquito hosts.Nature communications · 2025Article
- Oropouche Virus: An Emerging Orthobunyavirus.The Journal of general virology · 2024Review
- A reporter Oropouche virus expressing ZsGreen from the M segment enables pathogenesis studies in mice.Journal of virology · 2024Article
- Do NSm Virulence Factors in theViruses · 2024Article
- OROPOUCHE VIRUS: MORE QUESTIONS THAN ANSWERS.Zoonoses (Shannon, Ireland) · 2024Article
- Differential role of NSs genes in the neurovirulence of two genogroups of Akabane virus causing postnatal encephalomyelitis.Archives of virology · 2023Article
- Oropouche Virus Glycoprotein Topology and Cellular Requirements for Glycoprotein Secretion.Journal of virology · 2023Article
- Signal peptide peptidase: a potential therapeutic target for parasitic and viral infections.Expert opinion on therapeutic targets · 2022Review
- Evaluation and Designing of Epitopic-Peptide Vaccine AgainstInternational journal of peptide research and therapeutics · 2022Article
- Hepatitis C virus modulates signal peptide peptidase to alter host protein processing.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Review
- Recent Advances in Bunyavirus Glycoprotein Research: Precursor Processing, Receptor Binding and Structure.Viruses · 2021Review
- A Look intoViruses · 2021Review
- Physiological functions of SPP/SPPL intramembrane proteases.Cellular and molecular life sciences : CMLS · 2020Review
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
The M genome segment of Bunyamwera virus (BUNV)-the prototype of both the Bunyaviridae family and the Orthobunyavirus genus-encodes the glycoprotein precursor (GPC) that is proteolytically cleaved to yield two viral structural glycoproteins, Gn and Gc, and a nonstructural protein, NSm. The cleavage mechanism of orthobunyavirus GPCs and the host proteases involved have not been clarified. In this study, we investigated the processing of BUNV GPC and found that both NSm and Gc proteins were cleaved at their own internal signal peptides (SPs), in which NSm domain I functions as SP(NSm) and NSm domain V as SP(Gc) Moreover, the domain I was further processed by a host intramembrane-cleaving protease, signal peptide peptidase, and is required for cell fusion activities. Meanwhile, the NSm domain V (SP(Gc)) remains integral to NSm, rendering the NSm topology as a two-membrane-spanning integral membrane protein. We defined the cleavage sites and boundaries between the processed proteins as follows: Gn, from residue 17-312 or nearby residues; NSm, 332-477; and Gc, 478-1433. Our data clarified the mechanism of the precursor cleavage process, which is important for our understanding of viral glycoprotein biogenesis in the genus Orthobunyavirus and thus presents a useful target for intervention strategies.
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