2022
DOI: 10.1016/j.virusres.2022.198916
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Up-regulated 60S ribosomal protein L18 in PEDV N protein-induced S-phase arrested host cells promotes viral replication

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Cited by 5 publications
(5 citation statements)
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“…The identification of this RL11_human in this analysis, along with its alignment with the variation profile of the antigen antibody group from the antibody testing, suggests relevance to previous reports [18][19][20]. According to the report by Q. Zhu et al [19], they propose the potential to create a conducive cellular environment that significantly facilitates cell replication and promotes a favorable context for virus replication. They have elucidated that the expression of 60S Ribosomal protein RPL18 notably increases following Covid-19 infection.…”
Section: Results and Discusstionssupporting
confidence: 67%
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“…The identification of this RL11_human in this analysis, along with its alignment with the variation profile of the antigen antibody group from the antibody testing, suggests relevance to previous reports [18][19][20]. According to the report by Q. Zhu et al [19], they propose the potential to create a conducive cellular environment that significantly facilitates cell replication and promotes a favorable context for virus replication. They have elucidated that the expression of 60S Ribosomal protein RPL18 notably increases following Covid-19 infection.…”
Section: Results and Discusstionssupporting
confidence: 67%
“…Investigation into this phenomenon revealed previous reports of a similar significant increase in the expression of this 60S Ribosomal protein after Covid-19 infection. Z. Khalid et al have previously reported that 60S Ribosomal protein L29 (RPL29) was highly expressed across all COVID-19 infection groups [18][19][20]. The screened 60S ribosomal protein L11 (RL11_human) in this analysis is a component of the 60S ribosomal subunit, a central part of the ribosome, with several important functions: Ribosome conformation: RL11_human plays a crucial role in the conformation and maturation of ribosomes.…”
Section: Results and Discusstionsmentioning
confidence: 93%
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“…Since RPS18 protein expression is not different for normal and infected cells it had to be silenced with siRNA to look for its effects 45 but it was found that RPS18 forms an important cluster of NS1 targetting proteins. It was found that DENV infection results in relocation of RPS18 protein to the perinuclear position and indeed it is found to have profound effect in virus replication 47 . Involvement of RPS18 protein in DENV replication can also be suggested by its high amount of presence in nucleus compartment (Fig: 8).…”
Section: Resultmentioning
confidence: 99%
“…Mechanistically, the N protein interacts with p53 in the nucleus via the N S171-N194 motif, maintaining a high level of p53 and activating the p53-DREAM signaling pathway to inhibit the expression of cyclin A, and subsequently inducing S phase arrest [65]. A subsequent proteomic study showed that 60S ribosomal protein L18 (RPL18) was significantly increased in S phase arrested cells induced by N protein expression or PEDV infection [127]. In contrast, a recent study found that the N protein virus bound to constitutively photomorphogenic 1 (COP1) via its N-terminal domain (1-124 aa) and inhibited COP1 degradation, thereby promoting the COP1-mediated ubiquitination and degradation of p53, abolishing the antiviral activity of p53 [66].…”
Section: N Proteinmentioning
confidence: 99%