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Article

ELAVL1 Promotes Proliferation and Inhibits Apoptosis of the Marek’s Disease Virus (MDV)-Transformed Cell Line MSB1 via the COX-2/PGE2 Pathway

by
Lei He
1,2,†,
Dong-Mei Zhan
1,2,†,
Hui Peng
1,2,
Meng-Ru Gao
1,2,
Jian Chen
1,2,
Yan-Yan Jia
1,2,
Cheng-Shui Liao
1,2,
Song-Biao Chen
1,2,
Ke Ding
1,2,3,* and
Zu-Hua Yu
1,2,*
1
Laboratory of Functional Microbiology and Animal Health, College of Animal Science and Technology, Henan University of Science and Technology, Luoyang 471023, China
2
Luoyang Key Laboratory of Live Carrier Biomaterial and Animal Disease Prevention and Control, Henan University of Science and Technology, Luoyang 471023, China
3
College of Animal Science and Veterinary Medicine, Henan Institute of Science and Technology, Xingxiang 453003, China
*
Authors to whom correspondence should be addressed.
†
These authors contributed equally to this work.
Animals 2026, 16(5), 843; https://doi.org/10.3390/ani16050843
Submission received: 15 January 2026 / Revised: 26 February 2026 / Accepted: 4 March 2026 / Published: 7 March 2026
(This article belongs to the Special Issue Pathogenesis, Immunology and Epidemiology of Veterinary Viruses—2nd Edition)
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Simple Summary

Marek’s disease virus (MDV) causes lymphoproliferative tumors in chickens. Although the RNA-binding protein ELAVL1 is implicated in tumorigenesis, its role in MDV-induced oncogenesis remains unclear. This study investigated the role of ELAVL1 in the MDV-transformed MSB1 cell line, specifically in the COX-2/PGE2 pathway. Overexpression of ELAVL1 significantly enhanced cell proliferation, promoted G1-to-S/G2 phase cell cycle progression, and reduced apoptosis. These changes were accompanied by upregulated transcription and expression of COX-2 and PGE2. Conversely, siRNA-mediated knockdown of ELAVL1 inhibited cell proliferation, induced G1 phase arrest, and decreased COX-2 and PGE2 expression. The findings suggest that the RNA-binding protein ELAVL1 enhances the oncogenic properties of MDV-transformed lymphocytes by activating the COX-2/PGE2 signaling pathway, unraveling the potential mechanism through which MDV induces oncogenesis.

Abstract

Marek’s disease (MD), caused by the oncogenic Marek’s disease virus (MDV), is a highly contagious avian infection that induces lymphoproliferative tumors. The RNA-binding protein ELAVL1 is known to regulate tumor cell proliferation and apoptosis, but its role in MDV-induced oncogenesis remains unclear. This study investigated whether ELAVL1 modulates proliferation and apoptosis in the MDV-transformed MSB1 cell line and whether its effects involve the cyclooxygenase-2 (COX-2)/prostaglandin E2 (PGE2) pathway. MSB1 cells were transiently transfected with ELAVL1-overexpressing plasmids (pEGFP-C-ELAVL1) or ELAVL1-specific siRNA, with expression confirmed by real-time PCR (qRT-PCR). Cell proliferation was assessed using the CCK-8 assay, while cell cycle distribution and apoptosis rates were analyzed by flow cytometry. COX-2 and PGE2 expression levels were determined by qRT-PCR, Western blotting, and ELISA. Overexpression of ELAVL1 significantly promoted the proliferation of MSB1 cells, decreased transition into the G1 phase, increased the proportions of S and G2 phase cells, and suppressed apoptosis. Correspondingly, both mRNA and protein levels of COX-2 and PGE2 were significantly elevated. Conversely, ELAVL1 knockdown significantly inhibited proliferation, induced G1 phase arrest, decreased S phase cells, and significantly decreased COX-2 and PGE2 expression. These findings indicate that ELAVL1 promotes proliferation and inhibits apoptosis in MDV-transformed MSB1 cells, potentially via the COX-2/PGE2 signaling pathway.

1. Introduction

RNA-binding proteins (RBPs) are central regulators of post-transcriptional gene expression, RNA splicing, stability, localization, and translation [1]. By binding to specific elements in the 5′ or 3′ untranslated regions (UTRs) of target messenger RNAs (mRNAs), RBPs modulate mRNA fate and are critical for development, cellular homeostasis, and neoplastic disease progression [2,3,4,5]. Embryonic lethal abnormal vision-like 1 (ELAVL1), also known as human antigen R (HuR), is a key member of this family and has been strongly implicated in oncogenesis. Under normal conditions, ELAVL1 is primarily localized in the nucleus; however, it translocates to the cytoplasm in response to stimuli such as cellular stress or inflammation. In the cytoplasm, ELAVL1 binds to AU-rich elements (AREs) within the 3′UTRs of target mRNAs, enhancing their stability and translation [6,7]. Through this mechanism, ELAVL1 upregulates the expression of numerous proteins involved in cell proliferation, survival, angiogenesis, and metastasis [8]. Cyclooxygenase-2 (COX-2), an inducible enzyme that plays a significant role in inflammation and cancer progression, is a well-characterized downstream target of ELAVL1 [9,10]. Specifically, ELAVL1 increases COX-2 expression, which in turn promotes tumor cell growth and inhibits apoptosis by directly binding to and stabilizing the 3′UTR of COX-2 mRNA [11,12]. This regulatory axis also contributes to tumor-associated neovascularization [13,14,15], where prostaglandin E2 (PGE2), the main enzymatic product of COX-2, is a potent mediator of tumor progression [10,16,17,18]. Thus, the ELAVL1-mediated regulation of COX-2 is a significant axis in oncogenesis [15,19,20,21].
Studies indicate that several herpesviruses manipulate the post-transcriptional regulatory network of host cells to promote viral persistence and tumorigenesis by targeting ELAVL1. For example, proteins encoded by Epstein–Barr virus (EBV) regulate ELAVL1 activity in human tumors [22]. Similarly, Kaposi’s sarcoma-associated herpesvirus (KSHV) exploits ELAVL1 to enhance viral gene expression. Notably, Kaposin-B stabilizes PROX1 mRNA during KSHV-mediated lymphatic reprogramming of vascular endothelial cells [23].
The ELAVL1 protein and its mammalian orthologs are highly conserved in chickens, suggesting they may perform similar functions in avian species. Marek’s disease virus (MDV; Gallid herpesvirus 2) is a highly oncogenic alpha-herpesvirus that can establish latent infections in lymphocytes, leading to transformation and the development of Marek’s disease (MD), which is primarily characterized by the proliferation of lymphocytes in the infected chickens. As a major economic burden to the global poultry industry, MD underscores the need for a deeper understanding of the molecular mechanisms underlying its pathogenesis. MDV infection has been shown to activate the COX-2/PGE2 pathway, which may promote tumorigenesis by suppressing the antiviral CD4+ T-cell response [24]. However, the upstream molecular mechanism underlying MDV-mediated activation of the COX-2/PGE2 pathway remains poorly understood. In mammalian systems, ELAVL1 is a key post-transcriptional regulator of COX-2 expression, and both ELAVL1 and COX-2 have been extensively studied in human and other mammalian cancers [25,26,27,28,29,30,31]. However, their functional interplay has not been systematically explored in avian viruses, particularly in models of MDV-induced tumorigenesis.
Accordingly, we propose the following hypothesis: ELAVL1 expression and/or activity are dysregulated in MDV-transformed T cells. This stabilizes COX-2 and other pro-survival and pro-inflammatory mRNAs, thereby driving cell proliferation, inhibiting apoptosis, and possibly promoting tumor development through PGE2-mediated immunosuppression.
In the present study, ELAVL1 expression was modulated via plasmid-mediated overexpression and siRNA-mediated knockdown in the MDV-transformed avian CD4+ T-cell line MSB1. The effects of ELAVL1 on MSB1 cell proliferation, cell cycle distribution, and apoptosis were investigated to determine whether ELAVL1 exerts a pro-tumorigenic effect and whether these phenotypic changes are associated with alterations in the COX-2/PGE2 pathway. These findings provide insight into the role of ELAVL1 in MDV-driven tumorigenesis and explore its potential as a therapeutic target for this economically important avian disease.

2. Materials and Methods

2.1. Cell Culture and Transfection with Plasmids and siRNA

MSB1 cells, an MDV-transformed chicken lymphoblastoid line, were maintained in complete RPMI 1640 medium (Gibco, Waltham, MA, USA) supplemented with 10% fetal bovine serum (Gibco, USA), 10% tryptose phosphate broth (Sigma, St. Louis, MO, USA), and 1% penicillin-streptomycin (HyClone, Logan, UT, USA) at 37 °C under 5% CO2. For transfection experiments, MSB1 cells were seeded in 6-well plates at a density of 1 × 106 per well (n = 3 per group). Cells were transfected with a plasmid overexpressing ELAVL1 (pEGFP-C-ELAVL1) or the corresponding empty vector control (pEGFP-C) using the riboFECT™ CP kit (C10511-05, RiboBio, Guangzhou, China), according to the manufacturer’s instructions. For gene silencing, MSB1 cells were transfected with ELAVL1-specific siRNA (siELAVL1: 5′-GUGUCCUGCAACUUUGUCCTT-3′) or a non-targeting control siRNA (siNC: 5′-CCAUGACCAACUACGAUGA-3′) (100 nM, RiboBio, China).

2.2. Quantitative RT-PCR (qRT-PCR)

The mRNA expression levels of ELAVL1, COX-2, and PGE2 were quantified by quantitative RT-PCR (qRT-PCR), as outlined previously [32]. Briefly, total RNA was extracted from MSB1 cells in each group at 48 h post-transfection using TRIzol (15596018CN, Invitrogen, Carlsbad, CA, USA) and quantified with a NanoDrop ND-2000 spectrophotometer (Thermo Scientific, Waltham, MA, USA). cDNA was synthesized from 1 µg of total RNA using the PrimeScript™ RT Master Mix kit (RR036A, TaKaRa Bio, Shiga, Japan). qRT-PCR was subsequently performed for ELAVL1, COX-2, and PGE2 using the SYBR® Premix Ex Taq™ II (RR820A, TaKaRa Bio, Japan) on an ABI 7500 Real-Time PCR System (Applied Biosystems, Foster City, CA, USA). Each 20 µL PCR reaction contained 1 μL of cDNA, 0.4 μL (10 µM) of each specific primer, 10 μL SYBR Premix Ex Taq II, 0.4 μL ROX Reference Dye II (50×), and 7.8 μL sterile water. The cycling conditions were 95 °C for 30 s, followed by 40 cycles of 95 °C for 30 s and 60 °C for 30 s. Gene expression levels were calculated using the comparative 2−ΔΔCt method, with β-actin as the endogenous control. Results are expressed as fold change relative to the control group (set to 1). Primer sequences are listed in Table 1.

2.3. Western Blotting Analysis

The protein expression levels of ELAVL1 and COX were measured as follows: 1 × 106 MSB1 cells per well were cultured in 6-well plates (n = 3 per group), and lysed 48 h post-transfection using ice-cold RIPA buffer (R0010, Servicebio, Wuhan, China) supplemented with protease and phosphatase inhibitors. Protein concentrations were determined using a Bradford assay kit (G2001, Servicebio, China). Equal amounts of total protein (20 µg per sample) were separated by 10% SDS-PAGE and transferred onto a polyvinylidene difluoride (PVDF) membrane (G6047, Servicebio, China). Membranes were blocked with 5% bovine serum albumin (BSA) (GC305006, Servicebio, China) for 30 min at room temperature and incubated overnight at 4 °C with the following primary antibodies: anti-ELAVL1 (1:1000; 11910-1-AP, Proteintech, Rosemont, IL, USA), anti-COX-2 (1:1000; 123751-1-AP, Proteintech), and anti-β-actin (1:1000; ab8226, Abcam, Waltham, MA, USA). Subsequently, membranes were incubated for two hours with the corresponding horseradish peroxidase (HRP)-conjugated secondary antibodies: anti-rabbit IgG (1:1000; A0208, Beyotime, Shanghai, China) for ELAVL1 and COX-2, and anti-mouse IgG (1:1000; SA00001-1, Proteintech) for β-actin. Protein bands were visualized using the Bio-Rad Clarity Western ECL substrate (Bio-Rad Laboratories, Inc., Hercules, CA, USA), and chemiluminescent signals were captured. Band intensities were quantified using ImageJ (version 1.53, National Institutes of Health, Bethesda, MD, USA). The gray value of ELAVL1 or COX-2 protein was first normalized to that of β-actin, then expressed as a ratio relative to the control group.

2.4. ELISA Assays

PGE2 levels in MSB1 cell lysates were measured using ELISA. Briefly, MSB1 cells (1 × 106 per well) were cultured in 6-well plates (n = 3 per group), and culture supernatants (2 mL per well) were collected 48 h post-transfection. Supernatants were centrifuged at 12,000 r/min for 10 min to remove cell debris, concentrated, and stored at −80 °C until analysis. PGE2 concentrations were measured using a commercially available ELISA kit (EU2554, Wuhan Fine Biotech Co., Ltd., Wuhan, China), following the manufacturer’s instructions. The PGE2 concentrations in the supernatant were extrapolated from the standard curve and ultimately normalized to total protein, with results presented as pg PGE2/μg protein.

2.5. Cell Viability Assays

Cell proliferation was assessed using the Cell Counting Kit-8 (CCK-8; C0037, Beyotime, China), according to the manufacturer’s instructions. MSB1 cells were harvested post-transfection and seeded in triplicate into 96-well plates at a density of 4000 cells per well. The CCK-8 reagent (10 µL) was added to each well at 0, 24, 48, and 72 h of culture, followed by a 2-h incubation at 37 °C. Optical density (OD) was measured at 450 nm using a microplate reader (Thermo Fisher Scientific, Waltham, MA, USA).

2.6. Cell Cycle Assay

The distribution of cell cycle phases was analyzed using a commercial Cell Cycle Detection Kit (KGA512, KeyGen, Changchun, China) according to the manufacturer’s instructions. Briefly, cells were harvested 48 h post-transfection, washed twice with ice-cold PBS, and fixed in 70% ethanol on ice for 2 h at 4 °C. Fixed cells were washed twice with cold PBS and resuspended in a staining solution containing 50 µg/mL propidium iodide (PI) and 50 µg/mL RNase A. After incubation in the dark at 4 °C for 30 min, cell cycle distribution was analyzed by flow cytometry (CytoFLEX, Beckman Coulter, Brea, CA, USA).

2.7. AnnexinV-APC/7-AAD Staining

Cell apoptosis was evaluated by flow cytometry (CytoFLEX, Beckman Coulter, USA) using Annexin V-APC and 7-AAD staining. At 48 h post-transfection, MSB1 cells were harvested, washed twice with ice-cold PBS, and processed using an Annexin V-APC/7-AAD Apoptosis Detection Kit (A213, Vazyme, Nanjing, China) following the manufacturer’s instructions. Cells were resuspended in 500 µL of 1× binding buffer and stained with 5 µL of Annexin V-APC and 7-AAD for 15 min at room temperature in the dark. Flow cytometric analysis was then performed, and the proportions of early apoptotic (Annexin V+/7-AAD−) and late apoptotic (Annexin V+/7-AAD+) cells were quantified.

2.8. Statistical Analysis

All experiments were performed with three independent biological replicates (n = 3). For RT-qPCR, CCK-8, and Western blotting, each biological replicate was assayed in technical triplicate. Data are presented as the mean ± SD. Statistical analyses were performed using SPSS 20.0 (IBM Corp., Armonk, NY, USA) and GraphPad Prism 9.0 (GraphPad Software, Boston, MA, USA). Differences between the two groups were analyzed using a two-tailed Student’s t-test or a Welch’s t-test when variances were unequal. Comparisons among multiple groups were performed using a one-way ANOVA followed by Dunnett’s post hoc test. A p value less than 0.05 was considered statistically significant (* p < 0.05, ** p < 0.01), with ns denoting no significant difference.

3. Results

3.1. ELAVL1 Overexpression and Knockdown in MSB1 Cells

To investigate the functional role of ELAVL1 in MSB1 cells, overexpression and knockdown models were established by transfecting MSB1 cells with pEGFP-C1-ELAVL1 or siELAVL1, respectively. qRT-PCR analysis confirmed that ELAVL1 mRNA levels were markedly upregulated following pEGFP-C1-ELAVL1 transfection and significantly downregulated upon siELAVL1 treatment (Figure 1). This differential expression system provided a reliable experimental platform for subsequent functional studies.

3.2. ELAVL1 Expression Plays a Key Role in the Cell Viability and Cycle Progression of MSB1 Cells

CCK-8 assays were performed to examine whether ELAVL1 regulates MSB1 cell proliferation. Overexpression of ELAVL 1 significantly increased the cell viability, whereas its knockdown suppressed it (Figure 2). Flow cytometric analysis revealed that ELAVL1 overexpression accelerated the G1/S transition, as evidenced by a decreased proportion of cells in G1 and increased proportions in S and G2 phases. Conversely, ELAVL1 knockdown induced G1 arrest, with accumulation of cells in the G1 phase and a concomitant reduction in the S phase. No significant change in the G2 phase distribution was observed upon ELAVL1 knockdown (Figure 3). These results demonstrate that ELAVL1 promotes MSB1 cell proliferation, at least in part, by facilitating the G1/S phase progression.

3.3. Overexpression of ELAVL1 Inhibits the Apoptosis of MSB1 Cells

Next, we examined whether ELAVL1 influences apoptosis in MSB1 cells. Overexpression of ELAVL1 significantly reduced the apoptotic rate, whereas ELAVL1 knockdown markedly increased apoptosis (Figure 4). These results indicate that ELAVL1 protects MSB1 cells from apoptotic cell death, consistent with its pro-survival role suggested by proliferation and cell cycle analyses.

3.4. ELAVL1 Regulates the Expression of COX-2/PGE2 in MSB1 Cells

To further investigate the effect of ELAVL1 on the COX-2/PGE2 pathway, we analyzed the mRNA transcription and protein expression of ELAVL1, COX-2, and PGE2. Overexpression of ELAVL1 significantly upregulated both the mRNA and protein levels of COX-2, whereas ELAVL1 knockdown markedly suppressed COX-2 expression (Figure 5A,B). Similarly, PGE2, a key downstream effector of COX-2, was elevated upon ELAVL1 overexpression and reduced following ELAVL1 knockdown (Figure 5D,E). These results demonstrate that ELAVL1 positively regulates the COX-2/PGE2 pathway at both the transcriptional and translational levels.

4. Discussion

The biological functions of ELAVL1 and its role in the pathogenesis of neoplastic diseases have attracted considerable scientific interest [33,34]. Studies have shown that ELAVL1 expression is significantly upregulated in the cytoplasm of various tumor tissues [35,36], where it regulates tumor cell proliferation, invasion, lymphangiogenesis, and angiogenesis across multiple cancer types [37,38,39,40,41]. Consequently, ELAVL1 has been proposed as a potential therapeutic target for chemotherapy and for slowing down tumor progression [42,43,44,45]. However, most research on ELAVL1 has focused on human cancers, and its functions and underlying mechanisms in avian neoplastic diseases remain largely unexplored.
Uncontrolled cell division, dysregulated cell cycle progression, and abnormal proliferation are hallmarks of cancer. Activation of cyclins, which in turn activate cyclin-dependent kinases (CDKs), is a key driver of cell cycle progression [46]. ELAVL1 can bind to the 3′UTR of cyclin D1 and cyclin E1 mRNAs, enhancing their stability and promoting their expression. The resulting activation of cyclin D1 and E1 stimulates CDK4, CDK6, and CDK2, thereby facilitating the transition from the G1 to the S phase while promoting cell proliferation [43,47]. This study investigated the effects of ELAVL1 on proliferation, cell cycle distribution, and apoptosis in MSB1 cells using overexpression and knockdown approaches. The results revealed a consistent trend: ELAVL1 overexpression significantly enhanced cell viability, accelerated cell cycle progression, and inhibited apoptosis in MSB1 cells, whereas ELAVL1 knockdown exerted the opposite effect, including inducing G1 phase arrest, delaying progression to S phase, reducing cell viability, and enhancing apoptosis. These findings indicate that ELAVL1 promotes proliferation and inhibits apoptosis in MSB1 tumor cells, supporting previous reports in other tumors [38,48,49,50].
Studies have shown that COX-2 and its enzymatic product PGE2 play key roles in tumor cell proliferation and apoptosis [51,52]. In normal cells, COX-2 expression is tightly regulated by ARE-binding proteins. However, during tumorigenesis, this regulatory capacity is often compromised, leading to sustained COX-2 overexpression [53]. Elevated COX-2 expression in cancer cells has been linked to ELAVL1, which interacts with COX-2 mRNA, and ELAVL1 expression levels positively correlate with COX-2 levels. Thus, silencing ELAVL1 reduces COX-2 protein expression [12,15,53]. Inhibition of the COX-2/PGE2 signaling pathway has been shown to suppress the proliferation, migration, and invasion of cancer cells while inducing apoptosis, confirming its role in tumor growth and survival [54,55]. In the present study, modulation of ELAVL1 expression in MSB1 cells affected cell cycle progression and positively correlated with COX-2 and PGE2 levels. Conversely, ELAVL1 knockdown suppressed the expression of these two proteins, accompanied by cell cycle arrest and reduced proliferation. These findings suggest that ELAVL1 regulates proliferation and apoptosis in MSB1 cells, possibly through the COX-2/PGE2 pathway.
Future studies should include additional MDV-induced tumor cell lines or tumor samples to validate the broader relevance of these findings. Although this study examined the correlation between ELAVL1 and COX-2/PGE2 levels in vitro, the specific regulatory relationship remains to be further investigated. Techniques such as RNA immunoprecipitation (RIP) or 3′UTR luciferase reporter assays could clarify whether avian ELAVL1 directly interacts with COX-2 mRNA. Inhibition of COX-2 and PGE2, followed by assessment of proliferation and apoptosis in MDV-induced tumor cells, would further clarify the mechanisms by which ELAVL1 and COX-2/PGE2 regulate the proliferation and apoptosis of MDV-induced tumor cells. Moreover, in vivo studies of MDV infection are warranted to elucidate the mechanistic role of ELAVL1 in viral oncogenesis and to provide a more comprehensive assessment of the COX/PGE2 pathway as a viable therapeutic target.

5. Conclusions

In this study, we investigated the function of ELAVL1 in MSB1 cells, an MDV-induced model of avian T-cell lymphoma. The results demonstrate that ELAVL1 promotes proliferation, accelerates cell cycle progression, and inhibits apoptosis. Notably, ELAVL1 overexpression was associated with increased COX-2 expression and PG2 production, suggesting a functional link between ELAVL1 and the COX-2/PGE2 axis. These findings identify ELAVL1 as a candidate therapeutic target for this economically important avian disease and highlight the need for further investigation into its downstream mechanisms.

Author Contributions

Conceptualization, Z.-H.Y. and K.D.; methodology, L.H., D.-M.Z. and H.P.; software, M.-R.G. and H.P.; validation, J.C., Y.-Y.J. and S.-B.C.; data curation, M.-R.G., L.H. and D.-M.Z.; formal analysis, J.C., C.-S.L. and Y.-Y.J.; writing—original draft preparation, L.H. and D.-M.Z.; supervision, K.D., S.-B.C. and C.-S.L.; project administration, K.D. and Z.-H.Y.; funding acquisition, Z.-H.Y. All authors have read and agreed to the published version of the manuscript.

Funding

This research was supported by the National Natural Science Foundation of China (grant number 32472990), and the APC was funded by 32472990.

Institutional Review Board Statement

Ethical review and approval were waived for this study, as this study was conducted exclusively using established, commercially available cell lines, and it is not classified as human or animal subject research.

Informed Consent Statement

Not applicable.

Data Availability Statement

The data supporting the findings of this study are included within the article. Further inquiries can be directed to the corresponding authors.

Acknowledgments

We acknowledge the financial support from the National Natural Science Foundation of China for this work.

Conflicts of Interest

The authors declare no conflicts of interest.

Abbreviations

The following abbreviations are used in this manuscript:
MDMarek’s disease
MDVMarek’s disease virus
ELAVL1Embryonic lethal abnormal vision-like 1
HuRHuman antigen R
RBPRNA-binding proteins
DMSODimethyl sulfoxide
FBSFetal bovine serum
TPBTryptose phosphate broth
qRT-PCRQuantitative Real-time Polymerase Chain Reaction
SDS-PAGESodium dodecyl sulfate polyacrylamide gel electrophoresis
UTRUntranslated region
COX-2Cyclooxygenase-2
PGE2Prostaglandin E2
CDKCyclin-dependent kinases
ODOptical density

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Animals 16 00843 g001
Figure 1. Expression of ELAVL1 in MSB1 cells following transfection with pEGFP-C1-ELAVL1, pEGFP-C1, siELAVL1, or siNC. β-Actin was used as the control. Gene expression was normalized to the Control group. Each biological replicate was assayed in technical triplicate. Data are presented as mean ± SD from three independent biological replicates (n = 3). Comparisons between two groups were performed using a two-tailed Student’s t-test or Welch’s t-test when variances were unequal. ** p < 0.01 indicates a significant difference compared with the corresponding control group.
Figure 1. Expression of ELAVL1 in MSB1 cells following transfection with pEGFP-C1-ELAVL1, pEGFP-C1, siELAVL1, or siNC. β-Actin was used as the control. Gene expression was normalized to the Control group. Each biological replicate was assayed in technical triplicate. Data are presented as mean ± SD from three independent biological replicates (n = 3). Comparisons between two groups were performed using a two-tailed Student’s t-test or Welch’s t-test when variances were unequal. ** p < 0.01 indicates a significant difference compared with the corresponding control group.
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Animals 16 00843 g002
Figure 2. Cell viability of MSB1 cells after transfection with pEGFP-C1, pEGFP-C1-ELAVL1, siNC, or siELAVL1. Each biological replicate was assayed in technical triplicate. Data are presented as mean ± SD from three independent biological replicates (n = 3). Comparisons among multiple groups were performed using one-way ANOVA followed by Dunnett’s post hoc test to compare each treatment group with its corresponding control. (* p < 0.05, ** p < 0.01).
Figure 2. Cell viability of MSB1 cells after transfection with pEGFP-C1, pEGFP-C1-ELAVL1, siNC, or siELAVL1. Each biological replicate was assayed in technical triplicate. Data are presented as mean ± SD from three independent biological replicates (n = 3). Comparisons among multiple groups were performed using one-way ANOVA followed by Dunnett’s post hoc test to compare each treatment group with its corresponding control. (* p < 0.05, ** p < 0.01).
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Animals 16 00843 g003
Figure 3. Flow cytometry analysis of the cell cycle in MSB1 cells following transfection with (A) pEGFP-C1; (B) pEGFP-C1-ELAVL1; (C) siNC; or (D) pEGFP-C1-siELAVL1; (E) Cell cycle distribution across experimental groups. G1: pre-DNA synthesis phase; S: DNA synthesis phase; G2: post-DNA synthesis phase. Data are presented as mean ± SD from three independent biological replicates (n = 3). Comparisons among multiple groups were performed using one-way ANOVA followed by Dunnett’s post hoc test to compare each treatment group with its corresponding control. (* p < 0.05, ** p < 0.01, ns, not significant).
Figure 3. Flow cytometry analysis of the cell cycle in MSB1 cells following transfection with (A) pEGFP-C1; (B) pEGFP-C1-ELAVL1; (C) siNC; or (D) pEGFP-C1-siELAVL1; (E) Cell cycle distribution across experimental groups. G1: pre-DNA synthesis phase; S: DNA synthesis phase; G2: post-DNA synthesis phase. Data are presented as mean ± SD from three independent biological replicates (n = 3). Comparisons among multiple groups were performed using one-way ANOVA followed by Dunnett’s post hoc test to compare each treatment group with its corresponding control. (* p < 0.05, ** p < 0.01, ns, not significant).
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Figure 4. Flow cytometric results for the apoptosis rate of MSB1 cells following modulation of ELAVL1 expression. Representative plots are shown for (A) pEGFP-C1 group, (B) pEGFP-C1-ELAVL1 group, (C) siNC group, and (D) pEGFP-C1-siELAVL1 group; (E) The proportion of apoptotic cells in the different experimental groups. Data are presented as mean ± SD from three independent biological replicates (n = 3). Comparisons between two groups were performed using a two-tailed Welch’s t-test. (** p < 0.01).
Figure 4. Flow cytometric results for the apoptosis rate of MSB1 cells following modulation of ELAVL1 expression. Representative plots are shown for (A) pEGFP-C1 group, (B) pEGFP-C1-ELAVL1 group, (C) siNC group, and (D) pEGFP-C1-siELAVL1 group; (E) The proportion of apoptotic cells in the different experimental groups. Data are presented as mean ± SD from three independent biological replicates (n = 3). Comparisons between two groups were performed using a two-tailed Welch’s t-test. (** p < 0.01).
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Figure 5. The effect of ELAVL1 on the expression of COX-2 and PGE2. (A,B) Relative mRNA levels of COX-2 and PGE2 in MSB1 cells transfected with pEGFP-C1-ELAVL1, pEGFP-C1-siELAVL1, or siNC, with β-actin as the loading control; (C) PGE2 concentration in cell culture supernatant, quantified using ELISA; (D) Representative Western blot images showing ELAVL1 and COX-2 protein levels; (E,F) Densitometric quantification of ELAVL1 and COX-2 protein levels normalized to β-actin. Each biological replicate was assayed in technical triplicate. Data are presented as mean ± SD from three independent biological replicates (n = 3). Comparisons between two groups were performed using a two-tailed Student’s t-test or Welch’s t-test when variances were unequal. (* p < 0.05, ** p < 0.01).
Figure 5. The effect of ELAVL1 on the expression of COX-2 and PGE2. (A,B) Relative mRNA levels of COX-2 and PGE2 in MSB1 cells transfected with pEGFP-C1-ELAVL1, pEGFP-C1-siELAVL1, or siNC, with β-actin as the loading control; (C) PGE2 concentration in cell culture supernatant, quantified using ELISA; (D) Representative Western blot images showing ELAVL1 and COX-2 protein levels; (E,F) Densitometric quantification of ELAVL1 and COX-2 protein levels normalized to β-actin. Each biological replicate was assayed in technical triplicate. Data are presented as mean ± SD from three independent biological replicates (n = 3). Comparisons between two groups were performed using a two-tailed Student’s t-test or Welch’s t-test when variances were unequal. (* p < 0.05, ** p < 0.01).
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Table 1. Sequences of primers used for qRT-PCR assays detecting the mRNA expression levels of ELAVL1, COX-2, and PGE2 in MSB1 cells.
Table 1. Sequences of primers used for qRT-PCR assays detecting the mRNA expression levels of ELAVL1, COX-2, and PGE2 in MSB1 cells.
NamePrimer Sequences (5′ → 3′)Size (bp)
gga β-actin Forward primerTCAACACCCCAGCCATGTAT244
gga β-actin Reverse primerATTTCTCTCTCGGCTGTGGT
ELAVL1 Forward primerTACCTCCCCCAGAACATGAC220
ELAVL1 Reverse primerTTGGACGAGCATAGGAAACC
COX-2 Forward primerGAACCATCCTACCCGCTATTGT246
COX-2 Reverse primerCTATGGGGATTACAATGCGATG
PGE2 Forward primerCAACAAGTTCAGCCAGAGCGA200
PGE2 Reverse primerCCAGCTTTGTTTTTGCAGAGGT
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MDPI and ACS Style

He, L.; Zhan, D.-M.; Peng, H.; Gao, M.-R.; Chen, J.; Jia, Y.-Y.; Liao, C.-S.; Chen, S.-B.; Ding, K.; Yu, Z.-H. ELAVL1 Promotes Proliferation and Inhibits Apoptosis of the Marek’s Disease Virus (MDV)-Transformed Cell Line MSB1 via the COX-2/PGE2 Pathway. Animals 2026, 16, 843. https://doi.org/10.3390/ani16050843

AMA Style

He L, Zhan D-M, Peng H, Gao M-R, Chen J, Jia Y-Y, Liao C-S, Chen S-B, Ding K, Yu Z-H. ELAVL1 Promotes Proliferation and Inhibits Apoptosis of the Marek’s Disease Virus (MDV)-Transformed Cell Line MSB1 via the COX-2/PGE2 Pathway. Animals. 2026; 16(5):843. https://doi.org/10.3390/ani16050843

Chicago/Turabian Style

He, Lei, Dong-Mei Zhan, Hui Peng, Meng-Ru Gao, Jian Chen, Yan-Yan Jia, Cheng-Shui Liao, Song-Biao Chen, Ke Ding, and Zu-Hua Yu. 2026. "ELAVL1 Promotes Proliferation and Inhibits Apoptosis of the Marek’s Disease Virus (MDV)-Transformed Cell Line MSB1 via the COX-2/PGE2 Pathway" Animals 16, no. 5: 843. https://doi.org/10.3390/ani16050843

APA Style

He, L., Zhan, D.-M., Peng, H., Gao, M.-R., Chen, J., Jia, Y.-Y., Liao, C.-S., Chen, S.-B., Ding, K., & Yu, Z.-H. (2026). ELAVL1 Promotes Proliferation and Inhibits Apoptosis of the Marek’s Disease Virus (MDV)-Transformed Cell Line MSB1 via the COX-2/PGE2 Pathway. Animals, 16(5), 843. https://doi.org/10.3390/ani16050843

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