Infectious bursal disease virus hijacks endosomal membranes as the scaffolding structure for viral replication
Birnaviruses are unconventional members of the group of doublestranded RNA (dsRNA) viruses that are characterized by the lack of a transcriptionally active inner core. Instead, the birnaviral particles organize their genome in ribonucleoprotein complexes (RNPs) composed by dsRNA segments, the dsRNA-...
Guardado en:
| Publicado: |
2018
|
|---|---|
| Materias: | |
| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0022538X_v92_n11_p_Gimenez http://hdl.handle.net/20.500.12110/paper_0022538X_v92_n11_p_Gimenez |
| Aporte de: |
| id |
paper:paper_0022538X_v92_n11_p_Gimenez |
|---|---|
| record_format |
dspace |
| spelling |
paper:paper_0022538X_v92_n11_p_Gimenez2023-06-08T14:51:27Z Infectious bursal disease virus hijacks endosomal membranes as the scaffolding structure for viral replication +ssRNA Birnavirus Endosomes Gumboro disease Virus replication complex phospholipid protein VP2 protein VP3 animal cell Article cell membrane controlled study double-stranded RNA virus endosome human human cell infectious bursal disease infectious bursal disease virus nonhuman priority journal protein domain protein lipid interaction single-stranded RNA virus virus cell interaction virus replication Birnaviruses are unconventional members of the group of doublestranded RNA (dsRNA) viruses that are characterized by the lack of a transcriptionally active inner core. Instead, the birnaviral particles organize their genome in ribonucleoprotein complexes (RNPs) composed by dsRNA segments, the dsRNA-binding VP3 protein, and the virally encoded RNA-dependent RNA polymerase (RdRp). This and other structural features suggest that birnaviruses may follow a completely different replication program from that followed by members of the Reoviridae family, supporting the hypothesis that birnaviruses are the evolutionary link between single-stranded positive RNA (+ssRNA) and dsRNA viruses. Here we demonstrate that infectious bursal disease virus (IBDV), a prototypical member of the Birnaviridae family, hijacks endosomal membranes of infected cells through the interaction of a viral protein, VP3, with the phospholipids on the cytosolic leaflet of these compartments for replication. Employing a mutagenesis approach, we demonstrated that VP3 domain PATCH 2 (P2) mediates the association of VP3 with the endosomal membranes. To determine the role of VP3 P2 in the context of the virus replication cycle, we used avian cells stably overexpressing VP3 P2 for IBDV infection. Importantly, the intra- and extracellular virus yields, as well as the intracellular levels of VP2 viral capsid protein, were significantly diminished in cells stably overexpressing VP3 P2. Together, our results indicate that the association of VP3 with endosomes has a relevant role in the IBDV replication cycle. This report provides direct experimental evidence for membranous compartments such as endosomes being required by a dsRNA virus for its replication. The results also support the previously proposed role of birnaviruses as an evolutionary link between +ssRNA and dsRNA viruses. © 2018 American Society for Microbiology. 2018 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0022538X_v92_n11_p_Gimenez http://hdl.handle.net/20.500.12110/paper_0022538X_v92_n11_p_Gimenez |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
+ssRNA Birnavirus Endosomes Gumboro disease Virus replication complex phospholipid protein VP2 protein VP3 animal cell Article cell membrane controlled study double-stranded RNA virus endosome human human cell infectious bursal disease infectious bursal disease virus nonhuman priority journal protein domain protein lipid interaction single-stranded RNA virus virus cell interaction virus replication |
| spellingShingle |
+ssRNA Birnavirus Endosomes Gumboro disease Virus replication complex phospholipid protein VP2 protein VP3 animal cell Article cell membrane controlled study double-stranded RNA virus endosome human human cell infectious bursal disease infectious bursal disease virus nonhuman priority journal protein domain protein lipid interaction single-stranded RNA virus virus cell interaction virus replication Infectious bursal disease virus hijacks endosomal membranes as the scaffolding structure for viral replication |
| topic_facet |
+ssRNA Birnavirus Endosomes Gumboro disease Virus replication complex phospholipid protein VP2 protein VP3 animal cell Article cell membrane controlled study double-stranded RNA virus endosome human human cell infectious bursal disease infectious bursal disease virus nonhuman priority journal protein domain protein lipid interaction single-stranded RNA virus virus cell interaction virus replication |
| description |
Birnaviruses are unconventional members of the group of doublestranded RNA (dsRNA) viruses that are characterized by the lack of a transcriptionally active inner core. Instead, the birnaviral particles organize their genome in ribonucleoprotein complexes (RNPs) composed by dsRNA segments, the dsRNA-binding VP3 protein, and the virally encoded RNA-dependent RNA polymerase (RdRp). This and other structural features suggest that birnaviruses may follow a completely different replication program from that followed by members of the Reoviridae family, supporting the hypothesis that birnaviruses are the evolutionary link between single-stranded positive RNA (+ssRNA) and dsRNA viruses. Here we demonstrate that infectious bursal disease virus (IBDV), a prototypical member of the Birnaviridae family, hijacks endosomal membranes of infected cells through the interaction of a viral protein, VP3, with the phospholipids on the cytosolic leaflet of these compartments for replication. Employing a mutagenesis approach, we demonstrated that VP3 domain PATCH 2 (P2) mediates the association of VP3 with the endosomal membranes. To determine the role of VP3 P2 in the context of the virus replication cycle, we used avian cells stably overexpressing VP3 P2 for IBDV infection. Importantly, the intra- and extracellular virus yields, as well as the intracellular levels of VP2 viral capsid protein, were significantly diminished in cells stably overexpressing VP3 P2. Together, our results indicate that the association of VP3 with endosomes has a relevant role in the IBDV replication cycle. This report provides direct experimental evidence for membranous compartments such as endosomes being required by a dsRNA virus for its replication. The results also support the previously proposed role of birnaviruses as an evolutionary link between +ssRNA and dsRNA viruses. © 2018 American Society for Microbiology. |
| title |
Infectious bursal disease virus hijacks endosomal membranes as the scaffolding structure for viral replication |
| title_short |
Infectious bursal disease virus hijacks endosomal membranes as the scaffolding structure for viral replication |
| title_full |
Infectious bursal disease virus hijacks endosomal membranes as the scaffolding structure for viral replication |
| title_fullStr |
Infectious bursal disease virus hijacks endosomal membranes as the scaffolding structure for viral replication |
| title_full_unstemmed |
Infectious bursal disease virus hijacks endosomal membranes as the scaffolding structure for viral replication |
| title_sort |
infectious bursal disease virus hijacks endosomal membranes as the scaffolding structure for viral replication |
| publishDate |
2018 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0022538X_v92_n11_p_Gimenez http://hdl.handle.net/20.500.12110/paper_0022538X_v92_n11_p_Gimenez |
| _version_ |
1768543119277555712 |