White spot syndrome virus IE1 protein hijacks the host pentose phosphate pathway to fuel viral replication.

Fuente: PubMed
Enregistré dans:
Détails bibliographiques
Auteurs principaux: Zhang, Jia, Lu, Kaiyu, Zhu, Jinghua, Aweya, Jude Juventus, Zhang, Yueling, Yao, Defu
Format: Artículo científico
Langue:en
Publié: PLoS pathogens 2026
Sujets:
Accès en ligne:
Tags: Ajouter un tag
Pas de tags, Soyez le premier à ajouter un tag!
_version_ 1868266095160328193
author Zhang, Jia
Lu, Kaiyu
Zhu, Jinghua
Aweya, Jude Juventus
Zhang, Yueling
Yao, Defu
author_facet Zhang, Jia
Lu, Kaiyu
Zhu, Jinghua
Aweya, Jude Juventus
Zhang, Yueling
Yao, Defu
Zhang, Jia
Lu, Kaiyu
Zhu, Jinghua
Aweya, Jude Juventus
Zhang, Yueling
Yao, Defu
collection PubMed - marine biology
contents White spot syndrome virus IE1 protein hijacks the host pentose phosphate pathway to fuel viral replication. Zhang, Jia Lu, Kaiyu Zhu, Jinghua Aweya, Jude Juventus Zhang, Yueling Yao, Defu Animals Pentose Phosphate Pathway Virus Replication White spot syndrome virus 1 Penaeidae Host-Pathogen Interactions Immediate-Early Proteins Glucosephosphate Dehydrogenase Viruses frequently reprogram host metabolism to support their replication. The pentose phosphate pathway (PPP), a key regulator of nucleotide synthesis and redox balance, is often targeted during infection. While PPP activation is well-known proviral mechanism in vertebrates, how this process occurs in invertebrate hosts remains unclear. Here, using the white spot syndrome virus (WSSV) and its penaeid shrimp host as a model, we identify a previously unrecognized viral strategy that directly reprograms the PPP through host-viral protein interaction. WSSV infection strongly induced the expression of key PPP enzymes, including glucose-6-phosphate dehydrogenase (G6PD) and transketolase-like 2 (TKTL2), and enhanced TKTL2 enzymatic activity. This activation increased the production of nicotinamide adenine dinucleotide phosphate (NADPH) and ribose-5-phosphate (R5P), two critical PPP metabolites. Functional assays confirmed that the PPP is essential for efficient WSSV replication, as knockdown or pharmacological inhibition of G6PD or TKTL2 significantly attenuated viral load and improved host survival. Mechanistically, the viral immediate-early protein IE1 was found to directly bind to the C-terminal region of TKTL2 (TKTL2-C1, residues 500-555), and enhance its enzymatic activity. This interaction promoted PPP flux, boosted NADPH and R5P biosynthesis, and suppressed reactive oxygen species (ROS) accumulation. Supplementation with NADPH, R5P, or a ROS scavenger restored viral replication defects caused by IE1 knockdown. Moreover, the IE1-binding fragment TKTL2-C1 acted as a competitive inhibitor that disrupted the IE1-TKTL2 interaction, decreased PPP flux, and reduced viral replication. Together, these findings demonstrate that WSSV IE1 directly activates host TKTL2 to rewire pentose phosphate metabolism, revealing a novel metabolic mechanism of viral pathogenesis and identifying the PPP as a potential target for antiviral intervention in aquaculture.
format Artículo científico
id pubmed_41592137
institution PubMed
language en
publishDate 2026
publisher PLoS pathogens
record_format pubmed
spellingShingle White spot syndrome virus IE1 protein hijacks the host pentose phosphate pathway to fuel viral replication.
Zhang, Jia
Lu, Kaiyu
Zhu, Jinghua
Aweya, Jude Juventus
Zhang, Yueling
Yao, Defu
Animals
Pentose Phosphate Pathway
Virus Replication
White spot syndrome virus 1
Penaeidae
Host-Pathogen Interactions
Immediate-Early Proteins
Glucosephosphate Dehydrogenase
White spot syndrome virus IE1 protein hijacks the host pentose phosphate pathway to fuel viral replication. Zhang, Jia Lu, Kaiyu Zhu, Jinghua Aweya, Jude Juventus Zhang, Yueling Yao, Defu Animals Pentose Phosphate Pathway Virus Replication White spot syndrome virus 1 Penaeidae Host-Pathogen Interactions Immediate-Early Proteins Glucosephosphate Dehydrogenase Viruses frequently reprogram host metabolism to support their replication. The pentose phosphate pathway (PPP), a key regulator of nucleotide synthesis and redox balance, is often targeted during infection. While PPP activation is well-known proviral mechanism in vertebrates, how this process occurs in invertebrate hosts remains unclear. Here, using the white spot syndrome virus (WSSV) and its penaeid shrimp host as a model, we identify a previously unrecognized viral strategy that directly reprograms the PPP through host-viral protein interaction. WSSV infection strongly induced the expression of key PPP enzymes, including glucose-6-phosphate dehydrogenase (G6PD) and transketolase-like 2 (TKTL2), and enhanced TKTL2 enzymatic activity. This activation increased the production of nicotinamide adenine dinucleotide phosphate (NADPH) and ribose-5-phosphate (R5P), two critical PPP metabolites. Functional assays confirmed that the PPP is essential for efficient WSSV replication, as knockdown or pharmacological inhibition of G6PD or TKTL2 significantly attenuated viral load and improved host survival. Mechanistically, the viral immediate-early protein IE1 was found to directly bind to the C-terminal region of TKTL2 (TKTL2-C1, residues 500-555), and enhance its enzymatic activity. This interaction promoted PPP flux, boosted NADPH and R5P biosynthesis, and suppressed reactive oxygen species (ROS) accumulation. Supplementation with NADPH, R5P, or a ROS scavenger restored viral replication defects caused by IE1 knockdown. Moreover, the IE1-binding fragment TKTL2-C1 acted as a competitive inhibitor that disrupted the IE1-TKTL2 interaction, decreased PPP flux, and reduced viral replication. Together, these findings demonstrate that WSSV IE1 directly activates host TKTL2 to rewire pentose phosphate metabolism, revealing a novel metabolic mechanism of viral pathogenesis and identifying the PPP as a potential target for antiviral intervention in aquaculture.
title White spot syndrome virus IE1 protein hijacks the host pentose phosphate pathway to fuel viral replication.
topic Animals
Pentose Phosphate Pathway
Virus Replication
White spot syndrome virus 1
Penaeidae
Host-Pathogen Interactions
Immediate-Early Proteins
Glucosephosphate Dehydrogenase
url https://pubmed.ncbi.nlm.nih.gov/41592137/