Minor envelope proteins from GP2a to GP4 contribute to the spread pattern and yield of type 2 PRRSV in MARC-145 cells

Bai, Yuan-Zhe; Sun, Yue; Liu, Yong-Gang; Zhang, Hong-Liang; An, Tong-Qing; Wang, Qian; Tian, Zhi-Jun; Qiao, Xinyuan; Cai, Xue-Hui; Tang, Yan-Dong

doi:10.3389/fcimb.2024.1376725

Cited by 5 publications

(1 citation statement)

References 26 publications

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“…HEK293T cells were transfected with 2 μg of plasmids encoding wild-type S, N652Q, or N661Q variants, respectively. After 48 h, the cells were lysed and subjected to Western blot analysis using a previously described procedure outlined in our previous publications (19)(20)(21)(22)(23)(24).…”

Section: Western Blottingmentioning

confidence: 99%

The N-glycosylation at positions 652 and 661 of viral spike protein negatively modulates porcine deltacoronavirus entry

Wang,

Qiao,

Liu

et al. 2024

Front. Vet. Sci.

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N-glycosylation is a highly conserved glycan modification that plays crucial roles in various physiological processes, including protein folding, trafficking, and signal transduction. Porcine deltacoronavirus (PDCoV) poses a newly emerging threat to the global porcine industry. The spike protein of PDCoV exhibits a high level of N-glycosylation; however, its role in viral infection remains poorly understood. In this study, we applied a lentivirus-based entry reporter system to investigate the role of N-glycosylation on the viral spike protein during PDCoV entry stage. Our findings demonstrate that N-glycosylation at positions 652 and 661 of the viral spike protein significantly reduces the infectivity of PDCoV pseudotyped virus. Overall, our results unveil a novel function of N-glycosylation in PDCoV infection, highlighting its potential for facilitating the development of antiviral strategies.

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Section: Western Blottingmentioning

confidence: 99%

The N-glycosylation at positions 652 and 661 of viral spike protein negatively modulates porcine deltacoronavirus entry

Wang,

Qiao,

Liu

et al. 2024

Front. Vet. Sci.

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Prevalence and genetic diversity of PRRSV in Sichuan province of China from 2021 to 2023: Evidence of an ongoing epidemic transition

Huang,

Xu,

Luo

et al. 2024

Virology

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The full-length nsp2 replicase contributes to viral assembly in highly pathogenic PRRSV-2

Bai,

Wang,

Sun

et al. 2024

J Virol

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Porcine reproductive and respiratory syndrome viruses (PRRSVs) are significant pathogens that affect the global swine industry. Its virions consist of a central core composed of nucleocapsid (N) protein, surrounded by multiple distinct viral envelope proteins. However, the mechanisms underlying the recognition and packaging of N protein by viral envelope proteins remain elusive. In this study, we elucidated the role of nonstructural protein 2 (nsp2) from highly pathogenic PRRSV-2 (HP-PRRSV-2) in viral assembly. Firstly, among all the tested envelope proteins, only glycoprotein 5 (GP5) exhibits limited interaction with N protein. Interestingly, we demonstrated that full-length nsp2 co-immunoprecipitates (Co-IPs) with the N protein and all tested viral envelope proteins. In the presence of full-length nsp2, the N protein interacts with distinct viral envelope proteins. Moreover, upon viral infection, Co-IP experiments using nsp2-specific antibodies or N-specific antibodies revealed the formation of a complex between N and nsp2 with the M protein, GP2a, and GP5. However, neither of the two short forms of nsp2—namely nsp2TF nor nsp2N—participates in this process as they fail to interact with the N protein. Finally, our results demonstrate that this process occurs in the endoplasmic reticulum (ER) and the ER-Golgi intermediate compartment (ERGIC). Overall, our findings unveil a novel functional role for full-length nsp2 of HP-PRRSV-2 in facilitating the assembly of the N protein with viral envelope proteins. IMPORTANCE The virus assembly process of arteriviruses remains largely elusive, including the direct interaction between N protein and viral envelope proteins or the potential requirement for additional proteins in facilitating assembly. Moreover, where the N protein assembles with viral envelope proteins during the virus lifecycle remains unclear. This study reveals a novel role for nonstructural protein 2 (nsp2) in highly pathogenic porcine reproductive and respiratory syndrome virus type 2 (HP-PRRSV-2), highlighting its involvement in HP-PRRSV-2 assembly. These findings provide crucial insights into HP-PRRSV-2 assembly and enhance our understanding of their lifecycle. Overall, this study offers an alternative approach to developing a new antiviral strategy targeting PRRSV-2 assembly.

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Minor envelope proteins from GP2a to GP4 contribute to the spread pattern and yield of type 2 PRRSV in MARC-145 cells

Cited by 5 publications

References 26 publications

The N-glycosylation at positions 652 and 661 of viral spike protein negatively modulates porcine deltacoronavirus entry

The N-glycosylation at positions 652 and 661 of viral spike protein negatively modulates porcine deltacoronavirus entry

Prevalence and genetic diversity of PRRSV in Sichuan province of China from 2021 to 2023: Evidence of an ongoing epidemic transition

The full-length nsp2 replicase contributes to viral assembly in highly pathogenic PRRSV-2

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