Proteomic and phosphoproteomic analyses reveal several events involved in the early stages of bovine herpesvirus 1 infection

Magalhães-Júnior, Marcos Jorge de; Baracat‐Pereira, Maria Cristina; Pereira, Lorena; Vital, Camilo Elber; Santos, Marcelo Rocha dos; Cunha, Pricila S.; Fernandes, Kenner Morais; Bressan, Gustavo Costa; Fietto, Juliana Lopes Rangel; Silva-Júnior, Abelardo; Almeida, Márcia R.

doi:10.1007/s00705-019-04452-1

Cited by 4 publications

(2 citation statements)

References 52 publications

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“…Here, we used an unbiased mass spectrometry (MS) approach to identify pathways modulated by the PRV US3 protein. Mass spectrometry-based proteomics has previously been used in several studies to gain a better overview of differentially regulated or phosphorylated proteins during alphaherpesvirus infections [21][22][23][24]. By using transfected cells, we focused on proteins differentially phosphorylated by expression of US3 without the complicating background of a viral infection.…”

Section: Introductionmentioning

confidence: 99%

An Unbiased Approach to Mapping the Signaling Network of the Pseudorabies Virus US3 Protein

2020

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The US3 serine/threonine protein kinase is conserved among the alphaherpesvirus family and represents an important virulence factor. US3 plays a role in viral nuclear egress, induces dramatic alterations of the cytoskeleton, represses apoptosis, enhances gene expression and modulates the immune response. Although several substrates of US3 have been identified, an unbiased screen to identify US3 phosphorylation targets has not yet been described. Here, we perform a shotgun and phosphoproteomics analysis of cells expressing the US3 protein of pseudorabies virus (PRV) to identify US3 phosphorylation targets in an unbiased way. We identified several cellular proteins that are differentially phosphorylated upon US3 expression and validated the phosphorylation of lamin A/C at serine 404, both in US3-transfected and PRV-infected cells. These results provide new insights into the signaling network of the US3 protein kinase and may serve as a basis for future research into the role of the US3 protein in the viral replication cycle.

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Section: Introductionmentioning

confidence: 99%

An Unbiased Approach to Mapping the Signaling Network of the Pseudorabies Virus US3 Protein

2020

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“…Published studies have reported that GRP78, a marker protein of ER stress [ 35 ], is up-regulated in Madin–Darby bovine kidney (MDBK) cells at the early stage of BoHV-1 infection using proteomic and phosphoproteomic tools [ 36 ]. However, the induction of the UPR has also not been researched during the BoHV-1 infection.…”

Section: Introductionmentioning

confidence: 99%

Induction of the Unfolded Protein Response during Bovine Alphaherpesvirus 1 Infection

Wang

et al. 2020

Viruses

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Bovine herpesvirus 1 (BoHV-1) is an alphaherpesvirus that causes great economic losses in the cattle industry. Herpesvirus infection generally induces endoplasmic reticulum (ER) stress, and the unfolded protein response (UPR) in infected cells. However, it is not clear whether ER stress and UPR can be induced by BoHV-1 infection. Here, we found that ER stress induced by BoHV-1 infection could activate all three UPR sensors (the activating transcription factor 6 (ATF6), the inositol-requiring enzyme 1 (IRE1), and the protein kinase RNA-like ER kinase (PERK)) in MDBK cells. During BoHV-1 infection, the ATF6 pathway of UPR did not affect viral replication. However, both knockdown and specific chemical inhibition of PERK attenuated the BoHV-1 proliferation, and chemical inhibition of PERK significantly reduced the viral replication at the post-entry step of the BoHV-1 life cycle. Furthermore, knockdown of IRE1 inhibits BoHV-1 replication, indicating that the IRE1 pathway may promote viral replication. Further study revealed that BoHV-1 replication was enhanced by IRE1 RNase activity inhibition at the stage of virus post-entry in MDBK cells. Furthermore, IRE1 kinase activity inhibition and RNase activity enhancement decrease BoHV1 replication via affecting the virus post-entry step. Our study revealed that BoHV-1 infection activated all three UPR signaling pathways in MDBK cells, and BoHV-1-induced PERK and IRE1 pathways may promote viral replication. This study provides a new perspective for the interactions of BoHV-1 and UPR, which is helpful to further elucidate the mechanism of BoHV-1 pathogenesis.

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Proteomics of Animal Viruses

Behera

Suryawanshi

2023

Sustainable Agriculture Reviews

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Proteomic and phosphoproteomic analyses reveal several events involved in the early stages of bovine herpesvirus 1 infection

Cited by 4 publications

References 52 publications

An Unbiased Approach to Mapping the Signaling Network of the Pseudorabies Virus US3 Protein

An Unbiased Approach to Mapping the Signaling Network of the Pseudorabies Virus US3 Protein

Induction of the Unfolded Protein Response during Bovine Alphaherpesvirus 1 Infection

Proteomics of Animal Viruses

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