The interplay between viperin antiviral activity, lipid droplets and Junín mammarenavirus multiplication
Junín arenavirus infections are associated with high levels of interferons in both severe and fatal cases. Upon Junín virus (JUNV) infection a cell signaling cascade initiates, that ultimately attempts to limit viral replication and prevent infection progression through the expression of host antivi...
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2018
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00426822_v514_n_p216_PenaCarcamo http://hdl.handle.net/20.500.12110/paper_00426822_v514_n_p216_PenaCarcamo |
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paper:paper_00426822_v514_n_p216_PenaCarcamo2023-06-08T15:04:52Z The interplay between viperin antiviral activity, lipid droplets and Junín mammarenavirus multiplication Junín virus Lipids droplets Viperin alpha interferon fat droplet viper venom viral protein fat droplet interferon nucleoprotein protein RSAD2 protein, human animal cell antiviral activity Argentine hemorrhagic fever Article bioinformatics cell structure confocal microscopy controlled study disease association drug mechanism drug protein binding gene overexpression gene silencing human human cell immunomodulation innate immunity Junin virus lipid level nonhuman priority journal protein function protein interaction signal transduction virogenesis American hemorrhagic fever chemistry genetics immunology Junin virus physiology protein domain virology virus replication Hemorrhagic Fever, American Humans Interferons Junin virus Lipid Droplets Nucleoproteins Protein Domains Proteins Virus Replication Junín arenavirus infections are associated with high levels of interferons in both severe and fatal cases. Upon Junín virus (JUNV) infection a cell signaling cascade initiates, that ultimately attempts to limit viral replication and prevent infection progression through the expression of host antiviral proteins. The interferon stimulated gene (ISG) viperin has drawn our attention as it has been highlighted as an important antiviral protein against several viral infections. The studies of the mechanistic actions of viperin have described important functional domains relating its antiviral and immune-modulating actions through cellular lipid structures. In line with this, through silencing and overexpression approaches, we have identified viperin as an antiviral ISG against JUNV. In addition, we found that lipid droplet structures are modulated during JUNV infection, suggesting its relevance for proper virus multiplication. Furthermore, our confocal microscopy images, bioinformatics and functional results also revealed viperin-JUNV protein interactions that might be participating in this antiviral pathway at lipid droplet level. Altogether, these results will help to better understand the factors mediating innate immunity in arenavirus infection and may lead to the development of pharmacological agents that can boost their effectiveness thereby leading to new treatments for this viral disease. © 2017 Elsevier Inc. 2018 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00426822_v514_n_p216_PenaCarcamo http://hdl.handle.net/20.500.12110/paper_00426822_v514_n_p216_PenaCarcamo |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Junín virus Lipids droplets Viperin alpha interferon fat droplet viper venom viral protein fat droplet interferon nucleoprotein protein RSAD2 protein, human animal cell antiviral activity Argentine hemorrhagic fever Article bioinformatics cell structure confocal microscopy controlled study disease association drug mechanism drug protein binding gene overexpression gene silencing human human cell immunomodulation innate immunity Junin virus lipid level nonhuman priority journal protein function protein interaction signal transduction virogenesis American hemorrhagic fever chemistry genetics immunology Junin virus physiology protein domain virology virus replication Hemorrhagic Fever, American Humans Interferons Junin virus Lipid Droplets Nucleoproteins Protein Domains Proteins Virus Replication |
| spellingShingle |
Junín virus Lipids droplets Viperin alpha interferon fat droplet viper venom viral protein fat droplet interferon nucleoprotein protein RSAD2 protein, human animal cell antiviral activity Argentine hemorrhagic fever Article bioinformatics cell structure confocal microscopy controlled study disease association drug mechanism drug protein binding gene overexpression gene silencing human human cell immunomodulation innate immunity Junin virus lipid level nonhuman priority journal protein function protein interaction signal transduction virogenesis American hemorrhagic fever chemistry genetics immunology Junin virus physiology protein domain virology virus replication Hemorrhagic Fever, American Humans Interferons Junin virus Lipid Droplets Nucleoproteins Protein Domains Proteins Virus Replication The interplay between viperin antiviral activity, lipid droplets and Junín mammarenavirus multiplication |
| topic_facet |
Junín virus Lipids droplets Viperin alpha interferon fat droplet viper venom viral protein fat droplet interferon nucleoprotein protein RSAD2 protein, human animal cell antiviral activity Argentine hemorrhagic fever Article bioinformatics cell structure confocal microscopy controlled study disease association drug mechanism drug protein binding gene overexpression gene silencing human human cell immunomodulation innate immunity Junin virus lipid level nonhuman priority journal protein function protein interaction signal transduction virogenesis American hemorrhagic fever chemistry genetics immunology Junin virus physiology protein domain virology virus replication Hemorrhagic Fever, American Humans Interferons Junin virus Lipid Droplets Nucleoproteins Protein Domains Proteins Virus Replication |
| description |
Junín arenavirus infections are associated with high levels of interferons in both severe and fatal cases. Upon Junín virus (JUNV) infection a cell signaling cascade initiates, that ultimately attempts to limit viral replication and prevent infection progression through the expression of host antiviral proteins. The interferon stimulated gene (ISG) viperin has drawn our attention as it has been highlighted as an important antiviral protein against several viral infections. The studies of the mechanistic actions of viperin have described important functional domains relating its antiviral and immune-modulating actions through cellular lipid structures. In line with this, through silencing and overexpression approaches, we have identified viperin as an antiviral ISG against JUNV. In addition, we found that lipid droplet structures are modulated during JUNV infection, suggesting its relevance for proper virus multiplication. Furthermore, our confocal microscopy images, bioinformatics and functional results also revealed viperin-JUNV protein interactions that might be participating in this antiviral pathway at lipid droplet level. Altogether, these results will help to better understand the factors mediating innate immunity in arenavirus infection and may lead to the development of pharmacological agents that can boost their effectiveness thereby leading to new treatments for this viral disease. © 2017 Elsevier Inc. |
| title |
The interplay between viperin antiviral activity, lipid droplets and Junín mammarenavirus multiplication |
| title_short |
The interplay between viperin antiviral activity, lipid droplets and Junín mammarenavirus multiplication |
| title_full |
The interplay between viperin antiviral activity, lipid droplets and Junín mammarenavirus multiplication |
| title_fullStr |
The interplay between viperin antiviral activity, lipid droplets and Junín mammarenavirus multiplication |
| title_full_unstemmed |
The interplay between viperin antiviral activity, lipid droplets and Junín mammarenavirus multiplication |
| title_sort |
interplay between viperin antiviral activity, lipid droplets and junín mammarenavirus multiplication |
| publishDate |
2018 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00426822_v514_n_p216_PenaCarcamo http://hdl.handle.net/20.500.12110/paper_00426822_v514_n_p216_PenaCarcamo |
| _version_ |
1768543076335222784 |