Infectious bursal disease virus uptake involves macropinocytosis and trafficking to early endosomes in a Rab5-dependent manner
ARTÍCULO PUBLICADO EN REVISTA EXTERNA. Infectious bursal disease virus (IBDV) internalization is sparsely known in terms of molecular components of the pathway involved. To describe the cell biological features of IBDV endocytosis, we employed perturbants of endocytic pathways such as pharmacol...
Autores principales: | , , , |
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Formato: | Artículo Científico |
Lenguaje: | Inglés |
Publicado: |
Comité editorial Cellular Microbiology
2020
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Acceso en línea: | http://repositorio.umaza.edu.ar//handle/00261/1816 https://onlinelibrary.wiley.com/doi/full/10.1111/cmi.12415 |
Aporte de: |
id |
I56-R16200261-1816 |
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record_format |
dspace |
institution |
Universidad Juan Agustín MAZA |
institution_str |
I-56 |
repository_str |
R-162 |
collection |
UMAZA Digital (Universidad MAZA - Mendoza) |
language |
Inglés |
orig_language_str_mv |
eng |
description |
ARTÍCULO PUBLICADO EN REVISTA EXTERNA. Infectious bursal disease virus (IBDV) internalization
is sparsely known in terms of molecular components
of the pathway involved. To describe
the cell biological features of IBDV endocytosis,
we employed perturbants of endocytic pathways
such as pharmacological inhibitors and overexpression
of dominant-negative mutants. Internalization
analysis was performed quantifying
infected cells by immunofluorescence and
Western blot detection of the viral protein VP3 at
12 h post-infection reinforced by the analysis of
the capsid protein VP2 localization after virus
uptake at 1 h post-infection. We compared IBDV
infection to the internalization of well-established
ligands with defined endocytic pathways: transferrin,
cholera-toxin subunit B and dextran. To
describe virus endocytosis at the morphological
level, we performed ultrastructural studies of
viral internalization kinetics in control and actin
dynamics-blocked cells. Our results indicate that
IBDV endocytic internalization was clathrin- and
dynamin-independent, and that IBDV uses macropinocytosis
as the primary entry mechanism. After uptake, virus traffics to early endosomes
and requires exposure to the low endocytic pH as
well as a functional endocytic pathway to complete
its replication cycle. Moreover, our results
indicate that the GTPase Rab5 is crucial for IBDV
entry supporting the participation of the early
endosomal pathway in IBDV internalization and
infection of susceptible cells. Sitio de la revista: https://onlinelibrary.wiley.com/doi/full/10.1111/cmi.12415 |
format |
Artículo Científico |
author |
Gimenez, María Cecilia Rodríguez Aguirre, José Francisco Colombo, María Isabel Delgui, Laura Ruth |
spellingShingle |
Gimenez, María Cecilia Rodríguez Aguirre, José Francisco Colombo, María Isabel Delgui, Laura Ruth Infectious bursal disease virus uptake involves macropinocytosis and trafficking to early endosomes in a Rab5-dependent manner |
author_facet |
Gimenez, María Cecilia Rodríguez Aguirre, José Francisco Colombo, María Isabel Delgui, Laura Ruth |
author_sort |
Gimenez, María Cecilia |
title |
Infectious bursal disease virus uptake involves macropinocytosis and trafficking to early endosomes in a Rab5-dependent manner |
title_short |
Infectious bursal disease virus uptake involves macropinocytosis and trafficking to early endosomes in a Rab5-dependent manner |
title_full |
Infectious bursal disease virus uptake involves macropinocytosis and trafficking to early endosomes in a Rab5-dependent manner |
title_fullStr |
Infectious bursal disease virus uptake involves macropinocytosis and trafficking to early endosomes in a Rab5-dependent manner |
title_full_unstemmed |
Infectious bursal disease virus uptake involves macropinocytosis and trafficking to early endosomes in a Rab5-dependent manner |
title_sort |
infectious bursal disease virus uptake involves macropinocytosis and trafficking to early endosomes in a rab5-dependent manner |
publisher |
Comité editorial Cellular Microbiology |
publishDate |
2020 |
url |
http://repositorio.umaza.edu.ar//handle/00261/1816 https://onlinelibrary.wiley.com/doi/full/10.1111/cmi.12415 |
work_keys_str_mv |
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bdutipo_str |
Repositorios |
_version_ |
1764820541856808960 |