Interaction of the Mouse Polyomavirus Capsid Proteins with Importins Is Required for Efficient Import of Viral DNA into the Cell Nucleus
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F18%3A10385866" target="_blank" >RIV/00216208:11310/18:10385866 - isvavai.cz</a>
Výsledek na webu
<a href="https://doi.org/10.3390/v10040165" target="_blank" >https://doi.org/10.3390/v10040165</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.3390/v10040165" target="_blank" >10.3390/v10040165</a>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Interaction of the Mouse Polyomavirus Capsid Proteins with Importins Is Required for Efficient Import of Viral DNA into the Cell Nucleus
Popis výsledku v původním jazyce
The mechanism used by mouse polyomavirus (MPyV) to overcome the crowded cytosol to reach the nucleus has not been fully elucidated. Here, we investigated the involvement of importin alpha/beta 1 mediated transport in the delivery of MPyV genomes into the nucleus. Interactions of the virus with importin beta 1 were studied by co-immunoprecipitation and proximity ligation assay. For infectivity and nucleus delivery assays, the virus and its capsid proteins mutated in the nuclear localization signals (NLSs) were prepared and produced. We found that at early times post infection, virions bound importin beta 1 in a time dependent manner with a peak of interactions at 6 h post infection. Mutation analysis revealed that only when the NLSs of both VP1 and VP2/3 were disrupted, virus did not bind efficiently to importin beta 1 and its infectivity remarkably decreased (by 80%). Nuclear targeting of capsid proteins was improved when VP1 and VP2 were co-expressed. VP1 and VP2 were effectively delivered into the nucleus, even when one of the NLS, either VP1 or VP2, was disrupted. Altogether, our results showed that MPyV virions can use VP1 and/or VP2/VP3 NLSs in concert or individually to bind importins to deliver their genomes into the cell nucleus.
Název v anglickém jazyce
Interaction of the Mouse Polyomavirus Capsid Proteins with Importins Is Required for Efficient Import of Viral DNA into the Cell Nucleus
Popis výsledku anglicky
The mechanism used by mouse polyomavirus (MPyV) to overcome the crowded cytosol to reach the nucleus has not been fully elucidated. Here, we investigated the involvement of importin alpha/beta 1 mediated transport in the delivery of MPyV genomes into the nucleus. Interactions of the virus with importin beta 1 were studied by co-immunoprecipitation and proximity ligation assay. For infectivity and nucleus delivery assays, the virus and its capsid proteins mutated in the nuclear localization signals (NLSs) were prepared and produced. We found that at early times post infection, virions bound importin beta 1 in a time dependent manner with a peak of interactions at 6 h post infection. Mutation analysis revealed that only when the NLSs of both VP1 and VP2/3 were disrupted, virus did not bind efficiently to importin beta 1 and its infectivity remarkably decreased (by 80%). Nuclear targeting of capsid proteins was improved when VP1 and VP2 were co-expressed. VP1 and VP2 were effectively delivered into the nucleus, even when one of the NLS, either VP1 or VP2, was disrupted. Altogether, our results showed that MPyV virions can use VP1 and/or VP2/VP3 NLSs in concert or individually to bind importins to deliver their genomes into the cell nucleus.
Klasifikace
Druh
J<sub>imp</sub> - Článek v periodiku v databázi Web of Science
CEP obor
—
OECD FORD obor
10607 - Virology
Návaznosti výsledku
Projekt
Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.
Návaznosti
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Ostatní
Rok uplatnění
2018
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
Viruses
ISSN
1999-4915
e-ISSN
—
Svazek periodika
10
Číslo periodika v rámci svazku
4
Stát vydavatele periodika
CH - Švýcarská konfederace
Počet stran výsledku
22
Strana od-do
—
Kód UT WoS článku
000435184400026
EID výsledku v databázi Scopus
2-s2.0-85045086349