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Hauptverfasser: Cui, Chuang, Liu, Hao, Zhang, Yun-Fei, Liu, Ling-Ke, Liu, Hai-Peng
Format: Artículo científico
Sprache:en
Veröffentlicht: Fish & shellfish immunology 2025
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Online-Zugang:https://pubmed.ncbi.nlm.nih.gov/40409696/
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author Cui, Chuang
Liu, Hao
Zhang, Yun-Fei
Liu, Ling-Ke
Liu, Hai-Peng
author_facet Cui, Chuang
Liu, Hao
Zhang, Yun-Fei
Liu, Ling-Ke
Liu, Hai-Peng
Cui, Chuang
Liu, Hao
Zhang, Yun-Fei
Liu, Ling-Ke
Liu, Hai-Peng
collection PubMed - marine biology
contents The PERK-eIF2α pathway of the unfolded protein response inhibits white spot syndrome virus infection by attenuating global protein translation. Cui, Chuang Liu, Hao Zhang, Yun-Fei Liu, Ling-Ke Liu, Hai-Peng Animals White spot syndrome virus 1 Unfolded Protein Response eIF-2 Kinase Eukaryotic Initiation Factor-2 Astacoidea Protein Biosynthesis Arthropod Proteins Signal Transduction Immunity, Innate As obligate intracellular pathogens, viruses rely on the endoplasmic reticulum (ER) of host cells for viral protein synthesis and processing, leading to increased ER loading, which in turn triggers ER stress and activates the unfolded protein response (UPR). And this process is intricately linked to both viral infection and the host's immune response. White spot syndrome virus (WSSV) is one of the most detrimental viral pathogens affecting farmed crustaceans such as shrimp and crayfish, but the interaction between WSSV-induced ER stress and viral infection has not been comprehensively investigated. Here, we demonstrated that WSSV infection activated all three UPR pathways, including IRE1 pathway, ATF6 pathway and PERK-eIF2α pathway in crayfish hematopoietic tissue cells. In contrast to the promoted WSSV infection by IRE1 pathway and ATF6 pathway, the activated PERK-eIF2α pathway exhibited an inhibitory effect on viral infection, which was achieved via attenuation of global protein translation of host cells mediated by phosphorylation of eIF2α. Whereas, the continuous expression of WSSV proteins appeared to bypass this translational repression. Collectively, these results emphasized the key role of the PERK-eIF2α pathway, activated by WSSV-induced ER stress, in regulating viral infection, which might constitute an important aspect of the host cell's immune response to viral infection.
format Artículo científico
id pubmed_40409696
institution PubMed
language en
publishDate 2025
publisher Fish & shellfish immunology
record_format pubmed
spellingShingle The PERK-eIF2α pathway of the unfolded protein response inhibits white spot syndrome virus infection by attenuating global protein translation.
Cui, Chuang
Liu, Hao
Zhang, Yun-Fei
Liu, Ling-Ke
Liu, Hai-Peng
Animals
White spot syndrome virus 1
Unfolded Protein Response
eIF-2 Kinase
Eukaryotic Initiation Factor-2
Astacoidea
Protein Biosynthesis
Arthropod Proteins
Signal Transduction
Immunity, Innate
The PERK-eIF2α pathway of the unfolded protein response inhibits white spot syndrome virus infection by attenuating global protein translation. Cui, Chuang Liu, Hao Zhang, Yun-Fei Liu, Ling-Ke Liu, Hai-Peng Animals White spot syndrome virus 1 Unfolded Protein Response eIF-2 Kinase Eukaryotic Initiation Factor-2 Astacoidea Protein Biosynthesis Arthropod Proteins Signal Transduction Immunity, Innate As obligate intracellular pathogens, viruses rely on the endoplasmic reticulum (ER) of host cells for viral protein synthesis and processing, leading to increased ER loading, which in turn triggers ER stress and activates the unfolded protein response (UPR). And this process is intricately linked to both viral infection and the host's immune response. White spot syndrome virus (WSSV) is one of the most detrimental viral pathogens affecting farmed crustaceans such as shrimp and crayfish, but the interaction between WSSV-induced ER stress and viral infection has not been comprehensively investigated. Here, we demonstrated that WSSV infection activated all three UPR pathways, including IRE1 pathway, ATF6 pathway and PERK-eIF2α pathway in crayfish hematopoietic tissue cells. In contrast to the promoted WSSV infection by IRE1 pathway and ATF6 pathway, the activated PERK-eIF2α pathway exhibited an inhibitory effect on viral infection, which was achieved via attenuation of global protein translation of host cells mediated by phosphorylation of eIF2α. Whereas, the continuous expression of WSSV proteins appeared to bypass this translational repression. Collectively, these results emphasized the key role of the PERK-eIF2α pathway, activated by WSSV-induced ER stress, in regulating viral infection, which might constitute an important aspect of the host cell's immune response to viral infection.
title The PERK-eIF2α pathway of the unfolded protein response inhibits white spot syndrome virus infection by attenuating global protein translation.
topic Animals
White spot syndrome virus 1
Unfolded Protein Response
eIF-2 Kinase
Eukaryotic Initiation Factor-2
Astacoidea
Protein Biosynthesis
Arthropod Proteins
Signal Transduction
Immunity, Innate
url https://pubmed.ncbi.nlm.nih.gov/40409696/