HSP70 plays an ambiguous role during viral infections in plants

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61389030%3A_____%2F21%3A00546748" target="_blank" >RIV/61389030:_____/21:00546748 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00216208:11310/21:10436875

Výsledek na webu

<a href="http://doi.org/10.32615/bp.2021.001" target="_blank" >http://doi.org/10.32615/bp.2021.001</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.32615/bp.2021.001" target="_blank" >10.32615/bp.2021.001</a>

Jazyk výsledku

angličtina

Název v původním jazyce

HSP70 plays an ambiguous role during viral infections in plants

Popis výsledku v původním jazyce

Heat shock and almost all types of stresses associated with oxidative stress are accompanied by heat shock protein (HSP) expression. HSPs are involved in refolding denatured proteins and directing unrepairable proteins for degradation. Thus, under stress conditions, HSPs help to restore cellular balance. However, in virus-infected plants, HSP70 can have both positive and negative effects because viruses usually recruit HSP70. HSP70 can promote the replication and translation of the viral genome, the formation of viral replication complexes, and the propagation of viral particles from cell to cell and throughout the plant. HSP gene silencing in various virus-host plants systems and the comparison of susceptible and resistant species have shown that HSPs70 accelerate the development of infection. Conversely, during the process known as thermotherapy, the temperature increase inhibits viral replication in some host and virus systems. The success of thermotherapy depends not only on the temperature and treatment period or duration but also on the plant species and viral strain. In this review, we discuss the ambiguous role that HSPs70 play during viral infections in plants towards weighing the balance between their positive and negative functions.

Název v anglickém jazyce

HSP70 plays an ambiguous role during viral infections in plants

Popis výsledku anglicky

Heat shock and almost all types of stresses associated with oxidative stress are accompanied by heat shock protein (HSP) expression. HSPs are involved in refolding denatured proteins and directing unrepairable proteins for degradation. Thus, under stress conditions, HSPs help to restore cellular balance. However, in virus-infected plants, HSP70 can have both positive and negative effects because viruses usually recruit HSP70. HSP70 can promote the replication and translation of the viral genome, the formation of viral replication complexes, and the propagation of viral particles from cell to cell and throughout the plant. HSP gene silencing in various virus-host plants systems and the comparison of susceptible and resistant species have shown that HSPs70 accelerate the development of infection. Conversely, during the process known as thermotherapy, the temperature increase inhibits viral replication in some host and virus systems. The success of thermotherapy depends not only on the temperature and treatment period or duration but also on the plant species and viral strain. In this review, we discuss the ambiguous role that HSPs70 play during viral infections in plants towards weighing the balance between their positive and negative functions.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10611 - Plant sciences, botany

Projekt

<a href="/cs/project/EF16_019%2F0000738" target="_blank" >EF16_019/0000738: Centrum experimentální biologie rostlin</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2021

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Biologia Plantarum

ISSN

0006-3134

e-ISSN

1573-8264

Svazek periodika

65

Číslo periodika v rámci svazku

Online volume

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

12

Strana od-do

68-79

Kód UT WoS článku

000640332300002

EID výsledku v databázi Scopus

2-s2.0-85122281210