PEDV N protein capture protein translation element PABPC1 and eIF4F to promote viral replication

Zhai, Huanjie; Qin, Wenzhen; Dong, Sujie; Yang, Xinyu; Zhai, Xueying; Wu, Tong; Liu, Changlong; Zheng, Hao; Yu, Hai; Kong, Ning; Tong, Guangzhi; Shan, Tongling

doi:10.1016/j.vetmic.2023.109844

Cited by 8 publications

(5 citation statements)

References 29 publications

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“…Among the structural proteins of PEDV, PEDV M protein is an essential structural protein implicated in viral infection, replication and assembly although the precise mechanisms underlying these functions remain enigmatic ( Dong et al, 2021 ). PEDV N protein is the most abundant viral structural protein, which can be combined with viral genomic RNA to form ribonucleoprotein complexes, thereby participating in the transcription and replication of the virus ( Zhai et al, 2023 ). The spike (S) protein plays pivotal roles in PEDV attachment, receptor binding, and virus–cell membrane fusion during PEDV invasion into host cells ( Li et al, 2021 ).…”

Section: Discussionmentioning

confidence: 99%

Effect of supplementation with yeast polysaccharides on intestinal function in piglets infected with porcine epidemic diarrhea virus

Li,

Wu,

et al. 2024

Front. Microbiol.

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Porcine epidemic diarrhea virus (PEDV) has caused huge economic losses to the pig industry. Yeast polysaccharides (YP) has been used as a feed additive in recent years and poses good anti-inflammatory and antiviral effects. The present study aimed to explore the protective effect of YP on intestinal damage in PEDV-infected piglets. Eighteen 7-day-old piglets with similar body weights were randomly divided into three groups: Control group (basal diet), PEDV group (basal diet), and PEDV+YP group (basal diet +20 mg/kg BW YP), six replicates per group and one pig per replicate. Piglets in PEDV group and PEDV+YP group were orally given PEDV (dose: 1 × 106 TCID50) at 19:30 PM on the 8th day of the experiment. The control group received the same volume of PBS solution. Weight was taken on an empty stomach in the morning of the 11th day, blood was collected and then anesthetic was administered with pentobarbital sodium (50 mg/kg·BW) by intramuscular injection, and samples were slaughtered after the anesthetic was complete. The results showed that YP could alleviate the destruction of intestinal villus morphology of piglets caused by PEDV. Meanwhile, PEDV infection can reduce the activity of glutathione peroxidase, superoxide dismutase and catalase, and increase the content of malondialdehyde. YP can improve the antioxidative capacity in the serum and small intestine of PEDV-infected piglets. In addition, YP inhibited the replication of PEDV in the jejunum ileum and colon. Moreover, YP can regulate the mRNA levels of inflammatory genes (IL-1β and iNOS) and lipid metabolic genes (APOA4 and APOC3) in the small intestine. In summary, YP could inhibit virus replicates, improve intestinal morphology, enhance antioxidant capacity, relieve inflammation and regulate the metabolism of the intestine in PEDV-infected piglets.

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Section: Discussionmentioning

confidence: 99%

Effect of supplementation with yeast polysaccharides on intestinal function in piglets infected with porcine epidemic diarrhea virus

Li,

Wu,

et al. 2024

Front. Microbiol.

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“…The PEDV N protein can degrade STAT1 by inhibiting ACE2 promoter activity and preventing its phosphorylation, thus inhibiting interferon-stimulated gene expression ( 14 ). Previous studies have explored how PEDV hijects PABPC1 and eIF4F proteins related to the host transcription translation system to promote viral proliferation, and promotes cyclization of viral mRNA carried by N protein, thus promoting viral transcription and promoting viral replication ( 13 , 16 ). In this study, we explored the influence of PEDV N protein interaction with pyrimidine and purine metabolism pathway related proteins RPB2 and UPP1 on virus replication.…”

Section: Discussionmentioning

confidence: 99%

“…The PEDV N protein interacts with host p53 protein to induce S-phase arrest, thereby promoting viral replication ( 15 ). The PEDV N protein promotes the cyclization of viral mRNA carried by the N protein through interactions with PABPC1 and eIF4F proteins, thus promoting viral transcription and replication ( 13 , 16 ). However, the role of related proteins in host nucleotide metabolic pathways in regulating PEDV replication is still unknown.…”

Section: Introductionmentioning

confidence: 99%

Nucleotide metabolism-related host proteins RNA polymerase II subunit and uridine phosphorylase 1 interacting with porcine epidemic diarrhea virus N proteins affect viral replication

Xu,

Yi,

Kuang

et al. 2024

Front. Vet. Sci.

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Porcine epidemic diarrhea virus (PEDV) is a highly infectious pathogen that targets pig intestines to cause disease. It is globally widespread and causes huge economic losses to the pig industry. PEDV N protein is the protein that constitutes the core of PEDV virus particles, and most of it is expressed in the cytoplasm, and a small part can also be expressed in the nucleus. However, the role of related proteins in host nucleotide metabolic pathways in regulating PEDV replication have not been fully elucidated. In this study, PEDV-N-labeled antibodies were co-immunoprecipitated and combined with LC-MS to screen for host proteins that interact with N proteins. Bioinformatics analyses showed that the selected host proteins were mainly enriched in metabolic pathways. Moreover, co-immunoprecipitation and confocal microscopy confirmed that the second-largest subunit of RNA polymerase II (RPB2) and uridine phosphorylase 1 (UPP1) interacted with the N protein. RPB2 is the main subunit of RNA polymerase II and plays an important role in eukaryotic transcription. UPP1 is an enzyme that catalyzes reversible phosphorylation of uridine to uracil and ribo-1-phosphate to promote catabolism and bio anabolism. RPB2 overexpression significantly promoted viral replication, whereas UPP1 overexpression significantly inhibited viral replication. Studies on interactions between the PEDV N and host proteins are helpful in elucidating the pathogenesis and immune escape mechanism of PEDV.

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“…The binding of PABPC1 to the non-polyadenylated 3' untranslated region of dengue virus (DENV) RNA facilitates translation enhancement [29]. Porcine epidemic diarrhea virus (PEDV) N protein interacts with the protein translation initiation factor PABPC1 and eIF4F, which in turn promotes protein translation and viral replication [30]. We accordingly postulate that LINC01197 may serve as a sponge to sequester PABPC1, implying that LINC01197 might restrict the roles of PABPC1 in IAV replication.…”

Section: Discussionmentioning

confidence: 99%

LINC01197 inhibits Influenza A Virus replication by serving as a PABPC1 decoy

Wang,

Shi,

Zhang

et al. 2024

Preprint

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Influenza A viruses (IAVs) are known to impose a significant impact on both animal and human health due to its zoonotic potential. A growing body of evidence indicates that host long noncoding RNAs (lncRNAs) play crucial roles in regulating host-virus interactions during IAV infection. However, numerous lncRNAs associated with IAV infection have not been well-characterized. Here, we identified the LINC01197 as an antiviral host factor. LINC01197 was significantly upregulated after IAV infection which is controlled by NF-κB pathway. Functional analysis demonstrated that overexpression of LINC01197 inhibited IAV replication and virus production while knockdown of LINC01197 facilitated IAV replication. Mechanistically, LINC01197 directly interacted with poly(A) binding protein cytoplasmic 1 (PABPC1), which in turn sequesters and restricts its functions. This work demonstrates that LINC01197 functions as a protein decoy to suppress IAV replication, indicating a novel function of LINC01197 in controlling IAV replication.

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PEDV N protein capture protein translation element PABPC1 and eIF4F to promote viral replication

Cited by 8 publications

References 29 publications

Effect of supplementation with yeast polysaccharides on intestinal function in piglets infected with porcine epidemic diarrhea virus

Effect of supplementation with yeast polysaccharides on intestinal function in piglets infected with porcine epidemic diarrhea virus

Nucleotide metabolism-related host proteins RNA polymerase II subunit and uridine phosphorylase 1 interacting with porcine epidemic diarrhea virus N proteins affect viral replication

LINC01197 inhibits Influenza A Virus replication by serving as a PABPC1 decoy

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