Screening and bioinformatics analysis of cellular proteins interacting with chicken bromodomain-containing protein 2 in DF-1 cells

Zhou, Longhu; Han, Yang; Yuan, Chao; Duan, Zhiqiang

doi:10.1080/00071668.2021.1943311

Cited by 4 publications

(3 citation statements)

References 49 publications

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“…BRD2 is reported to interact with many chromatin- and transcriptional activation-related proteins to regulate the transcription of diverse genes [ 32 , 33 , 34 ]. Importantly, several studies have shown that viruses hijacking BRD2 to enhance viral gene transcription is beneficial for viral replication [ 22 , 23 , 35 , 36 ].…”

Section: Discussionmentioning

confidence: 99%

Mutation of Basic Residues R283, R286, and K288 in the Matrix Protein of Newcastle Disease Virus Attenuates Viral Replication and Pathogenicity

Duan

Shi

Xing

et al. 2023

IJMS

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The matrix (M) protein of Newcastle disease virus (NDV) contains large numbers of unevenly distributed basic residues, but the precise function of most basic residues in the M protein remains enigmatic. We previously demonstrated that the C-terminus (aa 264–313) of M protein interacted with the extra-terminal (ET) domain of chicken bromodomain-containing protein 2 (chBRD2), which promoted NDV replication by downregulating chBRD2 expression and facilitating viral RNA synthesis and transcription. However, the key amino acid sites determining M’s interaction with chBRD2/ET and their roles in the replication and pathogenicity of NDV are not known. In this study, three basic residues—R283, R286, and K288—in the NDV M protein were verified to be responsible for its interaction with chBRD2/ET. In addition, mutation of these basic residues (R283A/R286A/K288A) in the M protein changed its electrostatic pattern and abrogated the decreased expression of endogenic chBRD2. Moreover, a recombinant virus harboring these mutations resulted in a pathotype change of NDV and attenuated viral replication and pathogenicity in chickens due to the decreased viral RNA synthesis and transcription. Our findings therefore provide a better understanding of the crucial biological functions of M’s basic residues and also aid in understanding the poorly understood pathogenesis of NDV.

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Section: Discussionmentioning

confidence: 99%

Mutation of Basic Residues R283, R286, and K288 in the Matrix Protein of Newcastle Disease Virus Attenuates Viral Replication and Pathogenicity

Duan

Shi

Xing

et al. 2023

IJMS

Self Cite

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“…Duan et al [ 86 ] demonstrated that the M and chicken bromodomain-containing protein 2 (chBRD2) interaction in the nucleus could promote NDV replication. Generally, the BRD2 protein resides within the nucleus and poses significant effects on modulating the gene transcription and host immune responses [ 87 ]. Subsequent research revealed an interaction between both C-terminus domains of the M and chBRD2 proteins.…”

Section: Main Textmentioning

confidence: 99%

The multifaceted interactions between Newcastle disease virus proteins and host proteins: a systematic review

Lu,

Wang,

Liu

et al. 2024

Virulence

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Newcastle disease virus (NDV) typically induces severe illness in poultry and results in significant economic losses for the worldwide poultry sector. NDV, an RNA virus with a single-stranded negative-sense genome, is susceptible to mutation and immune evasion during viral transmission, thus imposing enormous challenges to avian health and poultry production. NDV is composed of six structural proteins and two nonstructural proteins that exert pivotal roles in viral infection and antiviral responses by interacting with host proteins. Nowadays, there is a particular focus on the mechanisms of virus-host protein interactions in NDV research, yet a comprehensive overview of such research is still lacking. Herein, we briefly summarize the mechanisms regarding the effects of virus-host protein interaction on viral infection, pathogenesis, and host immune responses. This review can not only enhance the present comprehension of the mechanism underlying NDV and host interplay, but also furnish a point of reference for the advancement of antiviral measures.

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“…to promote transcriptional activation of target genes (Rahman, Sowa et al, 2011;Wai, Szyszka et al, 2018). In addition, the ET domain of the BET protein can bind to viral proteins, promoting the integration of the viral genome and host DNA, thereby mediating viral infection and replication (Gallay, Blot et al, 2019;Duan, Han et al, 2020;Aiyer, Swapna et al, 2021;Zhou, Han et al, 2021).…”

Section: Classification and Structure Of Bet Protein Familymentioning

confidence: 99%

Bromodomain and Extraterminal Domain Protein 2 in Multiple Human Diseases

Ji,

Chen,

Wang

2024

J Pharmacol Exp Ther

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Bromodomain and extra-terminal domain protein 2 (BRD2), a member of the Bromodomain and extra-terminal domain (BET) protein family, is a crucial epigenetic regulator with significant function in various diseases and cellular processes. The central function of BRD2 is modulating gene transcription by binding to acetylated lysine residues on histones and transcription factors. This review highlights key findings on BRD2 in recent years, emphasizing its roles in maintaining genomic stability, influencing chromatin spatial organization, and participating in transcriptional regulation. BRD2's diverse functions are underscored by its involvement in diseases such as malignant tumor, neurological disorders, inflammatory conditions, metabolic diseases, and virus infection. Notably, the potential role of BRD2 as a diagnostic marker and therapeutic target is discussed in the context of various diseases. While pan-inhibitors targeting the BET family have shown promise in preclinical studies, a critical need exists for the development of highly selective BRD2 inhibitors. In conclusion, this review offers insights into the multifaceted nature of BRD2 and calls for continued research to unravel its intricate mechanisms and harness its therapeutic potential.

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Screening and bioinformatics analysis of cellular proteins interacting with chicken bromodomain-containing protein 2 in DF-1 cells

Cited by 4 publications

References 49 publications

Mutation of Basic Residues R283, R286, and K288 in the Matrix Protein of Newcastle Disease Virus Attenuates Viral Replication and Pathogenicity

Mutation of Basic Residues R283, R286, and K288 in the Matrix Protein of Newcastle Disease Virus Attenuates Viral Replication and Pathogenicity

The multifaceted interactions between Newcastle disease virus proteins and host proteins: a systematic review

Bromodomain and Extraterminal Domain Protein 2 in Multiple Human Diseases

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