Equid herpesvirus type 3 infection produces membrane-associated and secreted forms of glycoprotein G that are not required for efficient cell-to-cell spread of the virus in vitro
The ORF 70 gene of equid alphaherpesvirus type 3 (EHV-3) encodes glycoprotein G (gG), which is conserved in the majority of alphaherpesviruses. This glycoprotein is located in the viral envelope and has the characteristic of being secreted into the culture medium after proteolytic processing. It mod...
| Autores principales: | , , , |
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| Formato: | info:ar-repo/semantics/artículo |
| Lenguaje: | Inglés |
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Springer
2023
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| Materias: | |
| Acceso en línea: | http://hdl.handle.net/20.500.12123/14453 https://link.springer.com/article/10.1007/s00705-023-05727-4 https://doi.org/10.1007/s00705-023-05727-4 |
| _version_ | 1855037119708266496 |
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| author | Losinno, Antonella Vissani, Maria Aldana Sanchez, Diego Damiani, Armando Mario |
| author_browse | Damiani, Armando Mario Losinno, Antonella Sanchez, Diego Vissani, Maria Aldana |
| author_facet | Losinno, Antonella Vissani, Maria Aldana Sanchez, Diego Damiani, Armando Mario |
| author_sort | Losinno, Antonella |
| collection | INTA Digital |
| description | The ORF 70 gene of equid alphaherpesvirus type 3 (EHV-3) encodes glycoprotein G (gG), which is conserved in the majority of alphaherpesviruses. This glycoprotein is located in the viral envelope and has the characteristic of being secreted into the culture medium after proteolytic processing. It modulates the antiviral immune response of the host by interacting with chemokines. The aim of this study was to identify and characterize EHV-3 gG. By constructing viruses with HA-tagged gG, it was possible to detect gG in lysates of infected cells, their supernatants, and purified virions. A 100-, 60-, and 17-kDa form of the protein were detected in viral particles, while a 60-kDa form was identified in supernatants of infected cells. The role of EHV-3 gG in the viral infection cycle was assessed by the construction of a gG-minus EHV-3 mutant and its gG-positive revertant. When growth characteristics in an equine dermal fibroblast cell line were compared, the plaque size and the growth kinetics of the gG-minus mutant were similar to those of the revertant virus, suggesting that EHV-3 gG does not play a role in direct cell-to-cell transmission or virus proliferation of EHV-3 in tissue culture. The identification and characterization of EHV-3 gG described here provide a solid background for further studies to assess whether this glycoprotein has a function in modulating the host immune response. |
| format | info:ar-repo/semantics/artículo |
| id | INTA14453 |
| institution | Instituto Nacional de Tecnología Agropecuaria (INTA -Argentina) |
| language | Inglés |
| publishDate | 2023 |
| publishDateRange | 2023 |
| publishDateSort | 2023 |
| publisher | Springer |
| publisherStr | Springer |
| record_format | dspace |
| spelling | INTA144532023-04-12T14:53:16Z Equid herpesvirus type 3 infection produces membrane-associated and secreted forms of glycoprotein G that are not required for efficient cell-to-cell spread of the virus in vitro Losinno, Antonella Vissani, Maria Aldana Sanchez, Diego Damiani, Armando Mario Herpes Virus Equino Enfermedades de los Animales Caballos Glicoproteínas Experimentación in Vitro Equine Herpesvirus Animal Diseases Horses Glycoproteins In Vitro Experimentation The ORF 70 gene of equid alphaherpesvirus type 3 (EHV-3) encodes glycoprotein G (gG), which is conserved in the majority of alphaherpesviruses. This glycoprotein is located in the viral envelope and has the characteristic of being secreted into the culture medium after proteolytic processing. It modulates the antiviral immune response of the host by interacting with chemokines. The aim of this study was to identify and characterize EHV-3 gG. By constructing viruses with HA-tagged gG, it was possible to detect gG in lysates of infected cells, their supernatants, and purified virions. A 100-, 60-, and 17-kDa form of the protein were detected in viral particles, while a 60-kDa form was identified in supernatants of infected cells. The role of EHV-3 gG in the viral infection cycle was assessed by the construction of a gG-minus EHV-3 mutant and its gG-positive revertant. When growth characteristics in an equine dermal fibroblast cell line were compared, the plaque size and the growth kinetics of the gG-minus mutant were similar to those of the revertant virus, suggesting that EHV-3 gG does not play a role in direct cell-to-cell transmission or virus proliferation of EHV-3 in tissue culture. The identification and characterization of EHV-3 gG described here provide a solid background for further studies to assess whether this glycoprotein has a function in modulating the host immune response. Instituto de Virología Fil: Losinno, Antonella. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas. Instituto de Medicina y Biología Experimental de Cuyo; Argentina Fil: Losinno, Antonella. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina Fil: Vissani, Aldana. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Virología: Argentina. Fil: Vissani, Aldana. Universidad del Salvador. Escuela de Veterinaria. Cátedra de Enfermedades Infecciosas; Argentina Fil: Vissani, Aldana. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina Fil: Sanchez, Diego. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas. Instituto de Medicina y Biología Experimental de Cuyo; Argentina Fil: Sanchez, Diego. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina Fil: Damiani, Armando Mario. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas. Instituto de Medicina y Biología Experimental de Cuyo; Argentina Fil: Damiani, Armando Mario. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina 2023-04-12T14:50:51Z 2023-04-12T14:50:51Z 2023-04 info:ar-repo/semantics/artículo info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://hdl.handle.net/20.500.12123/14453 https://link.springer.com/article/10.1007/s00705-023-05727-4 0304-8608 1432-8798 https://doi.org/10.1007/s00705-023-05727-4 eng info:eu-repo/semantics/restrictedAccess http://creativecommons.org/licenses/by-nc-sa/4.0/ Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0) application/pdf Springer Archives of Virology 168 : article number: 122 (2023) |
| spellingShingle | Herpes Virus Equino Enfermedades de los Animales Caballos Glicoproteínas Experimentación in Vitro Equine Herpesvirus Animal Diseases Horses Glycoproteins In Vitro Experimentation Losinno, Antonella Vissani, Maria Aldana Sanchez, Diego Damiani, Armando Mario Equid herpesvirus type 3 infection produces membrane-associated and secreted forms of glycoprotein G that are not required for efficient cell-to-cell spread of the virus in vitro |
| title | Equid herpesvirus type 3 infection produces membrane-associated and secreted forms of glycoprotein G that are not required for efficient cell-to-cell spread of the virus in vitro |
| title_full | Equid herpesvirus type 3 infection produces membrane-associated and secreted forms of glycoprotein G that are not required for efficient cell-to-cell spread of the virus in vitro |
| title_fullStr | Equid herpesvirus type 3 infection produces membrane-associated and secreted forms of glycoprotein G that are not required for efficient cell-to-cell spread of the virus in vitro |
| title_full_unstemmed | Equid herpesvirus type 3 infection produces membrane-associated and secreted forms of glycoprotein G that are not required for efficient cell-to-cell spread of the virus in vitro |
| title_short | Equid herpesvirus type 3 infection produces membrane-associated and secreted forms of glycoprotein G that are not required for efficient cell-to-cell spread of the virus in vitro |
| title_sort | equid herpesvirus type 3 infection produces membrane associated and secreted forms of glycoprotein g that are not required for efficient cell to cell spread of the virus in vitro |
| topic | Herpes Virus Equino Enfermedades de los Animales Caballos Glicoproteínas Experimentación in Vitro Equine Herpesvirus Animal Diseases Horses Glycoproteins In Vitro Experimentation |
| url | http://hdl.handle.net/20.500.12123/14453 https://link.springer.com/article/10.1007/s00705-023-05727-4 https://doi.org/10.1007/s00705-023-05727-4 |
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