Glycoprotein-mediated biological properties of a host range mutant of Junin virus

The biological properties mediated by the main envelope glycoprotein (GP1) of a mouse-attenuated mutant of Junin virus, named Cl67, were investigated in comparison with its parental strain XJCl3. In contrast to the parental strain, this mutant was unable to multiply in primary cultures of mouse embr...

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Autores principales:	Scolaro, L.A., Damonte, E.B.
Formato:	JOUR
Materias:	Antigenicity Attenuation Binding Fusion Glycoprotein GP1 Host-range mutant Junin virus glycoprotein antigenicity article controlled study nonhuman priority journal protein analysis Vero cell virus mutant
Acceso en línea:	http://hdl.handle.net/20.500.12110/paper_09232516_v148_n5_p323_Scolaro
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	todo:paper_09232516_v148_n5_p323_Scolaro
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spelling	todo:paper_09232516_v148_n5_p323_Scolaro2023-10-03T15:45:53Z Glycoprotein-mediated biological properties of a host range mutant of Junin virus Scolaro, L.A. Damonte, E.B. Antigenicity Attenuation Binding Fusion Glycoprotein GP1 Host-range mutant Junin virus glycoprotein antigenicity article controlled study Junin virus nonhuman priority journal protein analysis Vero cell virus mutant Junin virus The biological properties mediated by the main envelope glycoprotein (GP1) of a mouse-attenuated mutant of Junin virus, named Cl67, were investigated in comparison with its parental strain XJCl3. In contrast to the parental strain, this mutant was unable to multiply in primary cultures of mouse embryo fibroblasts (MEFs). Impairment of Cl67 multiplication was associated with a lack of virus binding to MEF, probably due to an altered interaction between GP1 and cellular receptors. Antigenic and immunogenic characterization of GP1, performed by neutralization assays, demonstrated that, under certain conditions, polyclonal and monoclonal antibodies exhibited differential affinity and specificity for each virus. Cl67-infected Vero cells showed a marked pH-dependent fusion capability, suggesting more efficient tow pH triggering of fusion by mutant virus GP1 In comparison with the parental strain. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_09232516_v148_n5_p323_Scolaro
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	Antigenicity Attenuation Binding Fusion Glycoprotein GP1 Host-range mutant Junin virus glycoprotein antigenicity article controlled study Junin virus nonhuman priority journal protein analysis Vero cell virus mutant Junin virus
spellingShingle	Antigenicity Attenuation Binding Fusion Glycoprotein GP1 Host-range mutant Junin virus glycoprotein antigenicity article controlled study Junin virus nonhuman priority journal protein analysis Vero cell virus mutant Junin virus Scolaro, L.A. Damonte, E.B. Glycoprotein-mediated biological properties of a host range mutant of Junin virus
topic_facet	Antigenicity Attenuation Binding Fusion Glycoprotein GP1 Host-range mutant Junin virus glycoprotein antigenicity article controlled study Junin virus nonhuman priority journal protein analysis Vero cell virus mutant Junin virus
description	The biological properties mediated by the main envelope glycoprotein (GP1) of a mouse-attenuated mutant of Junin virus, named Cl67, were investigated in comparison with its parental strain XJCl3. In contrast to the parental strain, this mutant was unable to multiply in primary cultures of mouse embryo fibroblasts (MEFs). Impairment of Cl67 multiplication was associated with a lack of virus binding to MEF, probably due to an altered interaction between GP1 and cellular receptors. Antigenic and immunogenic characterization of GP1, performed by neutralization assays, demonstrated that, under certain conditions, polyclonal and monoclonal antibodies exhibited differential affinity and specificity for each virus. Cl67-infected Vero cells showed a marked pH-dependent fusion capability, suggesting more efficient tow pH triggering of fusion by mutant virus GP1 In comparison with the parental strain.
format	JOUR
author	Scolaro, L.A. Damonte, E.B.
author_facet	Scolaro, L.A. Damonte, E.B.
author_sort	Scolaro, L.A.
title	Glycoprotein-mediated biological properties of a host range mutant of Junin virus
title_short	Glycoprotein-mediated biological properties of a host range mutant of Junin virus
title_full	Glycoprotein-mediated biological properties of a host range mutant of Junin virus
title_fullStr	Glycoprotein-mediated biological properties of a host range mutant of Junin virus
title_full_unstemmed	Glycoprotein-mediated biological properties of a host range mutant of Junin virus
title_sort	glycoprotein-mediated biological properties of a host range mutant of junin virus
url	http://hdl.handle.net/20.500.12110/paper_09232516_v148_n5_p323_Scolaro
work_keys_str_mv	AT scolarola glycoproteinmediatedbiologicalpropertiesofahostrangemutantofjuninvirus AT damonteeb glycoproteinmediatedbiologicalpropertiesofahostrangemutantofjuninvirus
_version_	1807318898850136064

Glycoprotein-mediated biological properties of a host range mutant of Junin virus

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