In vitro anti-Junin virus activity of a peptide isolated from Melia azedarach L. leaves

Meliacine, a peptide isolated from leaves of Melia azedarach L. inhibited the multiplication of Junin virus in Vero cells treated with the compound before infection (pre-treatment) or immediately after virus adsorption. Analysis of early events following infection demonstrated that meliacine blocks...

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Autores principales:	Castilla, Viviana, Barquero, Andrea Alejandra, Mersich, Susana E., Coto, Celia Esther
Publicado:	1998
Materias:	Antiviral peptide Arenaviruses Junin virus Meliacine Membrane fusion antivirus agent meliacine plant extract unclassified drug virus glycoprotein animal cell antiviral activity article cell fusion concentration response controlled study in vitro study intracellular transport junin virus nonhuman plant leaf priority journal vero cell virus adsorption Animals Antiviral Agents Cercopithecus aethiops Dose-Response Relationship, Drug Fluorescent Antibody Technique, Indirect Giant Cells Humans Membrane Fusion Peptides, Cyclic Plant Extracts Plant Leaves Time Factors Vero Cells
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_09248579_v10_n1_p67_Castilla http://hdl.handle.net/20.500.12110/paper_09248579_v10_n1_p67_Castilla
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	paper:paper_09248579_v10_n1_p67_Castilla
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spelling	paper:paper_09248579_v10_n1_p67_Castilla2023-06-08T15:51:08Z In vitro anti-Junin virus activity of a peptide isolated from Melia azedarach L. leaves Castilla, Viviana Barquero, Andrea Alejandra Mersich, Susana E. Coto, Celia Esther Antiviral peptide Arenaviruses Junin virus Meliacine Membrane fusion antivirus agent meliacine plant extract unclassified drug virus glycoprotein animal cell antiviral activity article cell fusion concentration response controlled study in vitro study intracellular transport junin virus nonhuman plant leaf priority journal vero cell virus adsorption Animals Antiviral Agents Cercopithecus aethiops Dose-Response Relationship, Drug Fluorescent Antibody Technique, Indirect Giant Cells Humans Junin virus Membrane Fusion Peptides, Cyclic Plant Extracts Plant Leaves Time Factors Vero Cells Meliacine, a peptide isolated from leaves of Melia azedarach L. inhibited the multiplication of Junin virus in Vero cells treated with the compound before infection (pre-treatment) or immediately after virus adsorption. Analysis of early events following infection demonstrated that meliacine blocks virus penetration by preventing the uncoating step. The addition of meliacine at different times after infection indicated that meliacine also interferes with the release of infectious particles to the extracellular medium and inhibits the low-pH-induced fusion of infected cells. Intracellular transport of viral glycoproteins to the cell membrane was not affected by meliacine, as revealed by immunofluorescence staining. Taken together, these results suggest that meliacine affects two events of the virus replicative cycle that require membrane fusion: uncoating and budding. Fil:Castilla, V. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Barquero, A.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Mersich, S.E. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Coto, C.E. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 1998 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_09248579_v10_n1_p67_Castilla http://hdl.handle.net/20.500.12110/paper_09248579_v10_n1_p67_Castilla
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	Antiviral peptide Arenaviruses Junin virus Meliacine Membrane fusion antivirus agent meliacine plant extract unclassified drug virus glycoprotein animal cell antiviral activity article cell fusion concentration response controlled study in vitro study intracellular transport junin virus nonhuman plant leaf priority journal vero cell virus adsorption Animals Antiviral Agents Cercopithecus aethiops Dose-Response Relationship, Drug Fluorescent Antibody Technique, Indirect Giant Cells Humans Junin virus Membrane Fusion Peptides, Cyclic Plant Extracts Plant Leaves Time Factors Vero Cells
spellingShingle	Antiviral peptide Arenaviruses Junin virus Meliacine Membrane fusion antivirus agent meliacine plant extract unclassified drug virus glycoprotein animal cell antiviral activity article cell fusion concentration response controlled study in vitro study intracellular transport junin virus nonhuman plant leaf priority journal vero cell virus adsorption Animals Antiviral Agents Cercopithecus aethiops Dose-Response Relationship, Drug Fluorescent Antibody Technique, Indirect Giant Cells Humans Junin virus Membrane Fusion Peptides, Cyclic Plant Extracts Plant Leaves Time Factors Vero Cells Castilla, Viviana Barquero, Andrea Alejandra Mersich, Susana E. Coto, Celia Esther In vitro anti-Junin virus activity of a peptide isolated from Melia azedarach L. leaves
topic_facet	Antiviral peptide Arenaviruses Junin virus Meliacine Membrane fusion antivirus agent meliacine plant extract unclassified drug virus glycoprotein animal cell antiviral activity article cell fusion concentration response controlled study in vitro study intracellular transport junin virus nonhuman plant leaf priority journal vero cell virus adsorption Animals Antiviral Agents Cercopithecus aethiops Dose-Response Relationship, Drug Fluorescent Antibody Technique, Indirect Giant Cells Humans Junin virus Membrane Fusion Peptides, Cyclic Plant Extracts Plant Leaves Time Factors Vero Cells
description	Meliacine, a peptide isolated from leaves of Melia azedarach L. inhibited the multiplication of Junin virus in Vero cells treated with the compound before infection (pre-treatment) or immediately after virus adsorption. Analysis of early events following infection demonstrated that meliacine blocks virus penetration by preventing the uncoating step. The addition of meliacine at different times after infection indicated that meliacine also interferes with the release of infectious particles to the extracellular medium and inhibits the low-pH-induced fusion of infected cells. Intracellular transport of viral glycoproteins to the cell membrane was not affected by meliacine, as revealed by immunofluorescence staining. Taken together, these results suggest that meliacine affects two events of the virus replicative cycle that require membrane fusion: uncoating and budding.
author	Castilla, Viviana Barquero, Andrea Alejandra Mersich, Susana E. Coto, Celia Esther
author_facet	Castilla, Viviana Barquero, Andrea Alejandra Mersich, Susana E. Coto, Celia Esther
author_sort	Castilla, Viviana
title	In vitro anti-Junin virus activity of a peptide isolated from Melia azedarach L. leaves
title_short	In vitro anti-Junin virus activity of a peptide isolated from Melia azedarach L. leaves
title_full	In vitro anti-Junin virus activity of a peptide isolated from Melia azedarach L. leaves
title_fullStr	In vitro anti-Junin virus activity of a peptide isolated from Melia azedarach L. leaves
title_full_unstemmed	In vitro anti-Junin virus activity of a peptide isolated from Melia azedarach L. leaves
title_sort	in vitro anti-junin virus activity of a peptide isolated from melia azedarach l. leaves
publishDate	1998
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_09248579_v10_n1_p67_Castilla http://hdl.handle.net/20.500.12110/paper_09248579_v10_n1_p67_Castilla
work_keys_str_mv	AT castillaviviana invitroantijuninvirusactivityofapeptideisolatedfrommeliaazedarachlleaves AT barqueroandreaalejandra invitroantijuninvirusactivityofapeptideisolatedfrommeliaazedarachlleaves AT mersichsusanae invitroantijuninvirusactivityofapeptideisolatedfrommeliaazedarachlleaves AT cotoceliaesther invitroantijuninvirusactivityofapeptideisolatedfrommeliaazedarachlleaves
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In vitro anti-Junin virus activity of a peptide isolated from Melia azedarach L. leaves

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