TMT-based quantitative proteomics analysis reveals the attenuated replication mechanism of Newcastle disease virus caused by nuclear localization signal mutation in viral matrix protein

Duan, Zhiqiang; Yuan, Chao; Han, Yang; Zhou, Longhu; Zhao, Jianjian; Ruan, Yuhua; Chen, Jiaqi; Ni, Mingkang; Ji, Xinqin

doi:10.1080/21505594.2020.1770482

Cited by 18 publications

(11 citation statements)

References 101 publications

(155 reference statements)

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“…Other studies reported that the VSV M protein directly inhibits host cell transcription by inactivating host RNA polymerases I and II [ 44 ] and interacts with nuclear pore complexes to impair nuclear export of cellular mRNAs, which indirectly leads to a decrease and an increase in host cell and virus gene transcription, respectively [ 45 – 47 ]. Recently, we revealed that nuclear localization of the NDV M protein possibly affected host cell transcription because transcription repressor activity-related differentially expressed (DE) genes were upregulated and transcriptional activator activity-related DE genes were downregulated [ 10 ], and the expression of most DE proteins related to “transcription” and “RNA processing and modification” was significantly decreased in NDV-infected cells early in infection when compared to that in cells infected with the mutant NDV harbouring M/NLS mutation [ 48 ]. More importantly, these upregulated or downregulated DE genes participated in regulating viral RNA synthesis and NDV replication [ 10 ].…”

Section: Discussionmentioning

confidence: 99%

“…Currently, accumulating studies have also revealed that the BRD2, BRD3 and BRD4 proteins participate in the host immune response against virus infection [ 51 – 53 ]. In our recent studies using quantitative proteomics analysis, we found that the parental virus rSS1GFP but not the mutant virus rSS1GFP-M/NLSm harbouring an NLS mutation in the M protein reduced the expression of the BRD2, BRD3 and BRD4 proteins to different degrees in virus-infected cells, suggesting that the decreased expression of BRD2, BRD3 and BRD4 was caused by early nuclear localization of the M protein [ 48 ]. Here, we also found that chBRD2 knockdown or overexpression continued to increase or reduce the viral titres in DF-1 cells, respectively, indicating that chBRD2 might be involved in the immune response against NDV infection.…”

Section: Discussionmentioning

confidence: 99%

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Chicken bromodomain-containing protein 2 interacts with the Newcastle disease virus matrix protein and promotes viral replication

Duan

Han

Zhou

et al. 2020

Vet Res

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Bromodomain-containing protein 2 (BRD2) is a nucleus-localized serine-threonine kinase that plays pivotal roles in the transcriptional control of diverse genes. In our previous study, the chicken BRD2 (chBRD2) protein was found to interact with the Newcastle disease virus (NDV) matrix (M) protein using a yeast two-hybrid screening system, but the role of the chBRD2 protein in the replication of NDV remains unclear. In this study, we first confirmed the interaction between the M protein and chBRD2 protein using fluorescence co-localization, co-immunoprecipitation and pull-down assays. Intracellular binding studies indicated that the C-terminus (aa 264–313) of the M protein and the extra-terminal (ET) domain (aa 619–683) of the chBRD2 protein were responsible for interactions with each other. Interestingly, although two amino acids (T621 and S649) found in the chBRD2/ET domain were different from those in the human BRD2/ET domain and in that of other mammals, they did not disrupt the BRD2-M interaction or the chBRD2-M interaction. In addition, we found that the transcription of the chBRD2 gene was obviously decreased in both NDV-infected cells and pEGFP-M-transfected cells in a dose-dependent manner. Moreover, small interfering RNA-mediated knockdown of chBRD2 or overexpression of chBRD2 remarkably enhanced or reduced NDV replication by upregulating or downregulating viral RNA synthesis and transcription, respectively. Overall, we demonstrate for the first time that the interaction of the M protein with the chBRD2 protein in the nucleus promotes NDV replication by downregulating chBRD2 expression and facilitating viral RNA synthesis and transcription. These results will provide further insight into the biological functions of the M protein in the replication of NDV.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Chicken bromodomain-containing protein 2 interacts with the Newcastle disease virus matrix protein and promotes viral replication

Duan

Han

Zhou

et al. 2020

Vet Res

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“…Screening the different proteins between the normal and cancer MSCs could find key players which are responsible for cancer initiation and development ( 9 , 10 ). Spatial proteomics and TMT are the most powerful proteomics methods to identify and quantify the hallmarks of many diseases including cancer ( 57 , 58 ). Reviewing our proteomics and IPA results, we notice there are some proteins translocated abnormally into the nucleus in NSC lung cancer-MSCs compared to the normal control MSCs.…”

Section: Discussionmentioning

confidence: 99%

SFPQ Promotes Lung Cancer Malignancy via Regulation of CD44 v6 Expression

Yang

Jacobson

et al. 2022

Front. Oncol.

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Mesenchymal stem cells (MSCs) contribute to tumor pathogenesis and elicit antitumor immune responses in tumor microenvironments. Nuclear proteins might be the main players in these processes. In the current study, combining spatial proteomics with ingenuity pathway analysis (IPA) in lung non-small cell (NSC) cancer MSCs, we identify a key nuclear protein regulator, SFPQ (Splicing Factor Proline and Glutamine Rich), which is overexpressed in lung cancer MSCs and functions to promote MSCs proliferation, chemical resistance, and invasion. Mechanistically, the knockdown of SFPQ reduces CD44v6 expression to inhibit lung cancer MSCs stemness, proliferation in vitro, and metastasis in vivo. The data indicates that SFPQ may be a potential therapeutic target for limiting growth, chemotherapy resistance, and metastasis of lung cancer.

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“…After hypoxia−reoxygenation, TLR4/ MyD88 signaling induces TIFA interaction with TRAF6 and IRAK1, leading to rapid release of extracellular factors, such as tumor necrosis factor (TNF)-a. TIFA-mediated release of TNF-a is a predictor of survival during hemorrhage [37]. Moreover, a significant role of TIFA/TRAF6/NF-kB signaling complexes in immune surveillance was recently reported by Duan et al [38], who found that the matrix protein of a paramyxovirus, Newcastle disease virus (NDV), promotes NDV replication by reducing TIFA expression, and thus, downregulating TIFA/TRAF6/NF-kB−mediated production of cytokines [38].…”

Section: Biology Of Tifamentioning

confidence: 99%

TIFA and TIFAB: FHA-domain proteins involved in inflammation, hematopoiesis, and disease

Niederkorn

Agarwal

Starczynowski

2020

Experimental Hematology

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Forkhead-associated (FHA) domain−containing proteins are widely expressed across eubacteria and in eukaryotes. FHA domains contain phosphopeptide recognition motifs, which operate in a variety of phosphorylation-dependent and-independent biological processes, including the DNA damage response, signal transduction, and regulation of the cell cycle. More recently, two FHA domain−containing proteins were discovered in mammalian cells as tumor necrosis factor receptor-associated factor (TRAF)−interacting proteins: TIFA and TIFAB. TIFA and TIFAB are important modifiers of the innate immune signaling through their regulation of TRAF proteins. Recent studies have also revealed distinct roles for TIFA and TIFAB in the context of immune cell function, chronic inflammation, hematopoiesis, and hematologic disorders. Collectively, these studies indicate the important role of TIFA-and TIFAB-dependent signaling in hematopoietic cells and their dysregulation in several human diseases. In this review, we summarize the molecular mechanisms and biological role of these FHA-domain homologues, placing them into the context of human disease.

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TMT-based quantitative proteomics analysis reveals the attenuated replication mechanism of Newcastle disease virus caused by nuclear localization signal mutation in viral matrix protein

Abstract: Ji (2020) TMT-based quantitative proteomics analysis reveals the attenuated replication mechanism of Newcastle disease virus caused by nuclear localization signal mutation in viral matrix protein

Cited by 18 publications

References 101 publications

Chicken bromodomain-containing protein 2 interacts with the Newcastle disease virus matrix protein and promotes viral replication

Chicken bromodomain-containing protein 2 interacts with the Newcastle disease virus matrix protein and promotes viral replication

SFPQ Promotes Lung Cancer Malignancy via Regulation of CD44 v6 Expression

TIFA and TIFAB: FHA-domain proteins involved in inflammation, hematopoiesis, and disease

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