Involvement of vacuolar proton ATPase in Junin virus multiplication
The role of vacuolar-proton ATPase (V-H+ATPAse) on Junin virus (JV) replication was evaluated by analyzing the effect of specific inhibitors of the enzyme activity on different steps of virus multiplication cycle. The presence of the macrolide antibiotics bafilomycin A1 and concanamycin A during the...
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2001
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Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03048608_v146_n2_p251_Castilla http://hdl.handle.net/20.500.12110/paper_03048608_v146_n2_p251_Castilla |
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paper:paper_03048608_v146_n2_p251_Castilla2025-07-30T18:07:40Z Involvement of vacuolar proton ATPase in Junin virus multiplication Castilla, Viviana Palermo, Laura M. Coto, Celia Esther bafilomycin cell adhesion cell vacuole concanamycin A endocytosis enzyme activity enzyme inhibition Junin virus proton transporting adenosine triphosphatase virus enzyme virus infection virus replication Adsorption Animals Anti-Bacterial Agents Cell Line Cell Survival Cercopithecus aethiops Cricetinae Enzyme Inhibitors Fluorescent Antibody Technique, Indirect Junin virus Macrolides Protein Transport Proton-Translocating ATPases Vacuolar Proton-Translocating ATPases Vero Cells Viral Proteins Virus Replication Junin virus The role of vacuolar-proton ATPase (V-H+ATPAse) on Junin virus (JV) replication was evaluated by analyzing the effect of specific inhibitors of the enzyme activity on different steps of virus multiplication cycle. The presence of the macrolide antibiotics bafilomycin A1 and concanamycin A during the first two hours of infection caused a significant reduction of extracellular infectious virus production and viral protein expression in Vero and BHK-21 cells. The inhibitory action of the compounds was mainly exerted at an early stage of the JV multiplication cycle, without affecting virus attachment to the cell but preventing virus penetration. A correlation between the inhibitory action of the compounds on intracellular compartments acidification and the reduction of JV yield was observed. The addition of concanamycin A at different times after infection indicated that the compound also interferes with the release of infectious particles to the extracellular medium. Although, intracellular transport of JV glycoproteins to the cell membrane, seems not to be affected as revealed by immunofluorescence staining. The results confirm that JV enters into the cell through the endocytic pathway as previously suggested by using lysosomotropic compounds. Fil:Castilla, V. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Palermo, L.M. 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. 2001 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03048608_v146_n2_p251_Castilla http://hdl.handle.net/20.500.12110/paper_03048608_v146_n2_p251_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 |
bafilomycin cell adhesion cell vacuole concanamycin A endocytosis enzyme activity enzyme inhibition Junin virus proton transporting adenosine triphosphatase virus enzyme virus infection virus replication Adsorption Animals Anti-Bacterial Agents Cell Line Cell Survival Cercopithecus aethiops Cricetinae Enzyme Inhibitors Fluorescent Antibody Technique, Indirect Junin virus Macrolides Protein Transport Proton-Translocating ATPases Vacuolar Proton-Translocating ATPases Vero Cells Viral Proteins Virus Replication Junin virus |
spellingShingle |
bafilomycin cell adhesion cell vacuole concanamycin A endocytosis enzyme activity enzyme inhibition Junin virus proton transporting adenosine triphosphatase virus enzyme virus infection virus replication Adsorption Animals Anti-Bacterial Agents Cell Line Cell Survival Cercopithecus aethiops Cricetinae Enzyme Inhibitors Fluorescent Antibody Technique, Indirect Junin virus Macrolides Protein Transport Proton-Translocating ATPases Vacuolar Proton-Translocating ATPases Vero Cells Viral Proteins Virus Replication Junin virus Castilla, Viviana Palermo, Laura M. Coto, Celia Esther Involvement of vacuolar proton ATPase in Junin virus multiplication |
topic_facet |
bafilomycin cell adhesion cell vacuole concanamycin A endocytosis enzyme activity enzyme inhibition Junin virus proton transporting adenosine triphosphatase virus enzyme virus infection virus replication Adsorption Animals Anti-Bacterial Agents Cell Line Cell Survival Cercopithecus aethiops Cricetinae Enzyme Inhibitors Fluorescent Antibody Technique, Indirect Junin virus Macrolides Protein Transport Proton-Translocating ATPases Vacuolar Proton-Translocating ATPases Vero Cells Viral Proteins Virus Replication Junin virus |
description |
The role of vacuolar-proton ATPase (V-H+ATPAse) on Junin virus (JV) replication was evaluated by analyzing the effect of specific inhibitors of the enzyme activity on different steps of virus multiplication cycle. The presence of the macrolide antibiotics bafilomycin A1 and concanamycin A during the first two hours of infection caused a significant reduction of extracellular infectious virus production and viral protein expression in Vero and BHK-21 cells. The inhibitory action of the compounds was mainly exerted at an early stage of the JV multiplication cycle, without affecting virus attachment to the cell but preventing virus penetration. A correlation between the inhibitory action of the compounds on intracellular compartments acidification and the reduction of JV yield was observed. The addition of concanamycin A at different times after infection indicated that the compound also interferes with the release of infectious particles to the extracellular medium. Although, intracellular transport of JV glycoproteins to the cell membrane, seems not to be affected as revealed by immunofluorescence staining. The results confirm that JV enters into the cell through the endocytic pathway as previously suggested by using lysosomotropic compounds. |
author |
Castilla, Viviana Palermo, Laura M. Coto, Celia Esther |
author_facet |
Castilla, Viviana Palermo, Laura M. Coto, Celia Esther |
author_sort |
Castilla, Viviana |
title |
Involvement of vacuolar proton ATPase in Junin virus multiplication |
title_short |
Involvement of vacuolar proton ATPase in Junin virus multiplication |
title_full |
Involvement of vacuolar proton ATPase in Junin virus multiplication |
title_fullStr |
Involvement of vacuolar proton ATPase in Junin virus multiplication |
title_full_unstemmed |
Involvement of vacuolar proton ATPase in Junin virus multiplication |
title_sort |
involvement of vacuolar proton atpase in junin virus multiplication |
publishDate |
2001 |
url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03048608_v146_n2_p251_Castilla http://hdl.handle.net/20.500.12110/paper_03048608_v146_n2_p251_Castilla |
work_keys_str_mv |
AT castillaviviana involvementofvacuolarprotonatpaseinjuninvirusmultiplication AT palermolauram involvementofvacuolarprotonatpaseinjuninvirusmultiplication AT cotoceliaesther involvementofvacuolarprotonatpaseinjuninvirusmultiplication |
_version_ |
1840326337422688256 |