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Do NSm Virulence Factors in the Bunyavirales Viral Order Originate from Gn Gene Duplication?
Open accessPublished version of a preprint
Abstract
One-third of the nine WHO shortlisted pathogens prioritized for research and development in public health emergencies belong to the Bunyavirales order. Several Bunyavirales species carry an NSm protein that acts as a virulence factor. We predicted the structures of these NSm proteins and unexpectedly found that in two families, their cytosolic domain was inferred to have a similar fold to that of the cytosolic domain of the viral envelope-forming glycoprotein N (Gncyto) encoded on the same genome fragment. We show that although the sequence identity between the NSmcyto and the Gncyto domains is low, the conservation of the two zinc finger-forming CysCysHisCys motifs explains the predicted structural conservation. Importantly, our predictions provide a first glimpse into the long-unknown structure of NSm. Also, these predictions suggest that NSm is the result of a gene duplication event in the Bunyavirales Nairoviridae and Peribunyaviridae families and that such events may be common in the recent evolutionary history of RNA viruses.
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Highly accurate protein structure prediction with AlphaFold
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Metadata
- Authors
- Lefebvre, V., Leon Foun Lin, R., Cole, L., Cosset, F.-L., Fogeron, M.-L., & Böckmann, A.
- Affiliations
- Lyon 1 Université (FR)
- MMSB—Molecular Microbiology and Structural Biochemistry, Université de Lyon 1, CNRS UMR 5086, F-69367 Lyon, France
- Corresponding author
- Fogeron, Marie-Laure
- Böckmann, Anja
- Venue
- Viruses
- Publisher
- MDPI AG
- Published
- 2024-01-05
- Volume
- 16
- Issue
- 1
- Pages
- 90
- ISSN
- 1999-4915 (ISSN-L)
- PMC
- PMC10819786
- OpenAlex
- W4390617771
- Cited by
- 3
- References
- 1
- Citations by year
- 2026: 2 · 2024: 1
- FWCI
- 1.03
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Viruses (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- HAL (submittedVersion, other-oa)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- Agence Nationale de la Recherche (ANRS ECTZ 205074, ECTZ 158948, ANR-11-LABX-0048, ANR-11-IDEX-0007)
- RESPOND program of the LabEx Ecofect of the “Université de Lyon” (ANRS ECTZ 205074, ECTZ 158948, ANR-11-LABX-0048, ANR-11-IDEX-0007)
- program “Investissements d’Avenir” operated by the French National Research Agency (ANR) (ANRS ECTZ 205074, ECTZ 158948, ANR-11-LABX-0048, ANR-11-IDEX-0007)
- API-2022 MMSB (ANRS ECTZ 205074, ECTZ 158948, ANR-11-LABX-0048, ANR-11-IDEX-0007)
- Topics
- Health Sciences › Medicine › Infectious Diseases › Viral Infections and Vectors
- Health Sciences › Medicine › Epidemiology › Virology and Viral Diseases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- Bunyaviridae, viral virulence factors, gene duplication, Gn glycoprotein, zinc finger, protein structure prediction, Nairoviridae, Peribunyaviridae, RNA virus evolution, cytosolic domain
- MeSH terms
- Biological Evolution, Humans, Public Health, RNA Viruses, Viral Envelope Proteins, Gene Duplication, Virulence Factors
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