Newcastle disease virus (NDV) is a significant member of the Paramyxoviridae family, known for causing epidemics and substantial economic losses in the poultry industry worldwide. The NDV RNA genome primarily encodes six structural proteins (N, P, M, F, HN, and L) and two non-structural proteins (V and W). Among these, the polymerase-associated proteins (N, P, and L) and the viral RNA (vRNA) genome form the ribonucleoprotein complex, which plays a crucial role in the synthesis and transcription of NDV vRNA. In the last two decades, numerous studies have demonstrated that the polymerase-associated proteins are linked to the virulence, pathotype, and thermostability of NDV. Additionally, the interactions between these polymerase-associated proteins and host proteins are closely related to the NDV's replication and pathogenicity. Despite significant progress in understanding the unique and shared functions of NDV polymerase-associated proteins, research on these viral proteins' structure and function is less comprehensive than other NDV proteins, and the available information is often scattered. Therefore, this article systematically summarises and reviews the research progress made in understanding the structural features, virulence, pathotype, and thermostability correlation of NDV polymerase-associated proteins, as well as the critical roles of interactions between polymerase-associated proteins and host proteins in NDV replication and pathogenicity. This review aims to enhance our understanding of the complex functions of polymerase-associated proteins in NDV replication and pathogenesis and to contribute to the development of more effective vaccines and antiviral drugs against NDV challenges.
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http://dx.doi.org/10.1186/s13567-024-01429-0 | DOI Listing |
Vet Res
January 2025
Key Laboratory of Animal Genetics, Breeding and Reproduction in The Plateau Mountainous Region, Ministry of Education, Guizhou University, Guiyang, 550025, China.
Newcastle disease virus (NDV) is a significant member of the Paramyxoviridae family, known for causing epidemics and substantial economic losses in the poultry industry worldwide. The NDV RNA genome primarily encodes six structural proteins (N, P, M, F, HN, and L) and two non-structural proteins (V and W). Among these, the polymerase-associated proteins (N, P, and L) and the viral RNA (vRNA) genome form the ribonucleoprotein complex, which plays a crucial role in the synthesis and transcription of NDV vRNA.
View Article and Find Full Text PDFInt J Biol Macromol
January 2025
Department of Cardiology, the First hospital of Shanxi Medical University, and Key Laboratory of Cellular Physiology at Shanxi Medical University, Ministry of Education, Taiyuan, China; Guangxi Key Laboratory of Precision Medicine for Genetic Diseases, Maternal and Child Health Hospital of Guangxi Zhuang Autonomous Region, Nanning, China. Electronic address:
Plant Physiol
December 2024
State Key Laboratory of Wheat Improvement, College of Life Sciences, Shandong Agricultural University, Tai' an 271018, China.
CELL DIVISION CYCLE 5 (CDC5) is a R2R3-type MYB transcription factor, serving as a key component of modifier of snc1, 4-associated complex/NineTeen complex, which is associated with plant immunity, RNA splicing, and miRNA biogenesis. In this study, we demonstrate that mutation of CDC5 accelerates flowering in Arabidopsis (Arabidopsis thaliana). CDC5 activates the expression of FLOWERING LOCUS C (FLC) by binding to and affecting the enrichment of RNA polymerase II on FLC chromatin.
View Article and Find Full Text PDFMol Cell
December 2024
Department of Microbiology, The University of Texas Southwestern Medical Center, Dallas, TX, USA. Electronic address:
The polymerase associated factor 1 (PAF1) complex (PAF1c) promotes RNA polymerase II (RNA Pol II) transcription at the elongation step; however, how PAF1c transcription activity is selectively regulated during cell fate transitions remains poorly understood. Here, we reveal that the alternative reading frame (ARF) tumor suppressor operates at two levels to restrain PAF1c-dependent oncogenic transcriptional programs upon p53 loss in mouse cells. First, ARF assembles into homo-oligomers to bind the PAF1 subunit to promote PAF1c disassembly, consequently dampening PAF1c interaction with RNA Pol II and PAF1c-dependent transcription.
View Article and Find Full Text PDFCell Death Differ
November 2024
Department of Biochemistry and Molecular Biology, International Cancer Center, Guangdong Key Laboratory of Genome Instability and Human Disease Prevention, Marshall Laboratory of Biomedical Engineering, Shenzhen University Medical School, Shenzhen, China.
Repair of double strand breaks (DSBs) by RNA-binding proteins (RBPs) is vital for ensuring genome integrity. DSB repair is accompanied by local transcriptional repression in the vicinity of transcriptionally active genes, but the mechanism by which RBPs regulate transcriptional regulation is unclear. Here, we demonstrated that RBP hnRNPA2B1 functions as a RNA polymerase-associated factor that stabilizes the transcription complex under physiological conditions.
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