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

Autores
Losinno, Antonella; Vissani, Maria Aldana; Sanchez, Diego; Damiani, Armando Mario
Año de publicación
2023
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
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
Fuente
Archives of Virology 168 : article number: 122 (2023)
Materia
Herpes Virus Equino
Enfermedades de los Animales
Caballos
Glicoproteínas
Experimentación in Vitro
Equine Herpesvirus
Animal Diseases
Horses
Glycoproteins
In Vitro Experimentation
Nivel de accesibilidad
acceso restringido
Condiciones de uso
http://creativecommons.org/licenses/by-nc-sa/4.0/
Repositorio
INTA Digital (INTA)
Institución
Instituto Nacional de Tecnología Agropecuaria
OAI Identificador
oai:localhost:20.500.12123/14453
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oai_identifier_str oai:localhost:20.500.12123/14453
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spelling 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 vitroLosinno, AntonellaVissani, Maria AldanaSanchez, DiegoDamiani, Armando MarioHerpes Virus EquinoEnfermedades de los AnimalesCaballosGlicoproteínasExperimentación in VitroEquine HerpesvirusAnimal DiseasesHorsesGlycoproteinsIn Vitro ExperimentationThe 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 VirologíaFil: Losinno, Antonella. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas. Instituto de Medicina y Biología Experimental de Cuyo; ArgentinaFil: Losinno, Antonella. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: 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; ArgentinaFil: Vissani, Aldana. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Sanchez, Diego. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas. Instituto de Medicina y Biología Experimental de Cuyo; ArgentinaFil: Sanchez, Diego. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Damiani, Armando Mario. Universidad Nacional de Cuyo. Facultad de Ciencias Médicas. Instituto de Medicina y Biología Experimental de Cuyo; ArgentinaFil: Damiani, Armando Mario. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaSpringer2023-04-12T14:50:51Z2023-04-12T14:50:51Z2023-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttp://hdl.handle.net/20.500.12123/14453https://link.springer.com/article/10.1007/s00705-023-05727-40304-86081432-8798https://doi.org/10.1007/s00705-023-05727-4Archives of Virology 168 : article number: 122 (2023)reponame:INTA Digital (INTA)instname:Instituto Nacional de Tecnología Agropecuariaenginfo:eu-repo/semantics/restrictedAccesshttp://creativecommons.org/licenses/by-nc-sa/4.0/Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)2025-10-16T09:31:09Zoai:localhost:20.500.12123/14453instacron:INTAInstitucionalhttp://repositorio.inta.gob.ar/Organismo científico-tecnológicoNo correspondehttp://repositorio.inta.gob.ar/oai/requesttripaldi.nicolas@inta.gob.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:l2025-10-16 09:31:09.795INTA Digital (INTA) - Instituto Nacional de Tecnología Agropecuariafalse
dc.title.none.fl_str_mv 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
spellingShingle 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
Herpes Virus Equino
Enfermedades de los Animales
Caballos
Glicoproteínas
Experimentación in Vitro
Equine Herpesvirus
Animal Diseases
Horses
Glycoproteins
In Vitro Experimentation
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_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_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
dc.creator.none.fl_str_mv Losinno, Antonella
Vissani, Maria Aldana
Sanchez, Diego
Damiani, Armando Mario
author Losinno, Antonella
author_facet Losinno, Antonella
Vissani, Maria Aldana
Sanchez, Diego
Damiani, Armando Mario
author_role author
author2 Vissani, Maria Aldana
Sanchez, Diego
Damiani, Armando Mario
author2_role author
author
author
dc.subject.none.fl_str_mv Herpes Virus Equino
Enfermedades de los Animales
Caballos
Glicoproteínas
Experimentación in Vitro
Equine Herpesvirus
Animal Diseases
Horses
Glycoproteins
In Vitro Experimentation
topic Herpes Virus Equino
Enfermedades de los Animales
Caballos
Glicoproteínas
Experimentación in Vitro
Equine Herpesvirus
Animal Diseases
Horses
Glycoproteins
In Vitro Experimentation
dc.description.none.fl_txt_mv 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
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.
publishDate 2023
dc.date.none.fl_str_mv 2023-04-12T14:50:51Z
2023-04-12T14:50:51Z
2023-04
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv 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
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
identifier_str_mv 0304-8608
1432-8798
dc.language.none.fl_str_mv eng
language eng
dc.rights.none.fl_str_mv 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)
eu_rights_str_mv restrictedAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Springer
publisher.none.fl_str_mv Springer
dc.source.none.fl_str_mv Archives of Virology 168 : article number: 122 (2023)
reponame:INTA Digital (INTA)
instname:Instituto Nacional de Tecnología Agropecuaria
reponame_str INTA Digital (INTA)
collection INTA Digital (INTA)
instname_str Instituto Nacional de Tecnología Agropecuaria
repository.name.fl_str_mv INTA Digital (INTA) - Instituto Nacional de Tecnología Agropecuaria
repository.mail.fl_str_mv tripaldi.nicolas@inta.gob.ar
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