Role of the cytosolic tails of Rift Valley fever virus envelope glycoproteins in viral morphogenesis
| Autor: | Marie Flamand, Felix Kreher, Xavier Carnec, Michèle Bouloy, Myriam Ermonval |
|---|---|
| Přispěvatelé: | Génétique Moléculaire des Bunyavirus, Institut Pasteur [Paris] (IP), XC was a recipient of a fellowship from the NIH grant (7-U01-AI66327) and from a Programme Transversal de Recherche from Institut Pasteur. This work was supported in part by the NIH grant and internal grant from Institut Pasteur., Institut Pasteur [Paris] |
| Jazyk: | angličtina |
| Předmět: |
Phlebovirus
Rift Valley Fever MESH: Golgi Apparatus/virology Amino Acid Motifs Mutant Golgi Apparatus MESH: Amino Acid Sequence MESH: Cytosol/virology MESH: Amino Acid Motifs Cytosol Viral Envelope Proteins Golgi MESH: Animals Viral morphogenesis Golgi localization Cytoskeleton chemistry.chemical_classification Arbovirus MESH: Rift Valley fever virus/genetics biology MESH: Rift Valley Fever/virology Golgi Targeting MESH: Viral Envelope Proteins/metabolism 3. Good health [SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitology symbols MESH: Viral Envelope Proteins/genetics Bunyaviridae MESH: Viral Envelope Proteins/chemistry Molecular Sequence Data Cell Line symbols.namesake Virology Organelle Animals Humans Amino Acid Sequence MESH: Rift Valley fever virus/metabolism MESH: Humans MESH: Molecular Sequence Data Golgi apparatus Rift Valley fever virus biology.organism_classification MESH: Cell Line chemistry Glycoprotein MESH: Rift Valley fever virus/growth & development |
| Zdroj: | Virology Virology, 2014, 448, pp.1-14. ⟨10.1016/j.virol.2013.09.023⟩ Virology, Elsevier, 2014, 448, pp.1-14. ⟨10.1016/j.virol.2013.09.023⟩ |
| ISSN: | 0042-6822 1096-0341 |
| DOI: | 10.1016/j.virol.2013.09.023 |
| Popis: | International audience; The correct folding, heterodimerization and trafficking of Gn/Gc envelope glycoproteins of Rift Valley fever virus, RVFV (Bunyaviridae and Phlebovirus genus) are essential for Golgi assembly and budding of viral particles. The Gn and Gc carboxy-terminus contain a Golgi targeting and an ER-retrieval signal, respectively. We generated RVFV-like particles with mutations in the cytosolic tails of Gn or Gc and identified regions important for release of infectious particles. The role of specific amino-acids in these regions was further investigated by creating recombinant mutant viruses by reverse-genetics. Residues outside the suspected Golgi targeting motif, i.e. the di-lysine K29-K30 motif and the N43, R44 and I46 residues of the Gn cytosolic domain, appeared important for Golgi localization and RNP packaging. Concerning the Gc tail, replacement of K2 or K3 in the di-lysine motif, had a drastic impact on Gn trafficking and induced an important organelle redistribution and cell remodeling, greatly affecting particle formation and release. |
| Databáze: | OpenAIRE |
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