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The herpesvirus UL11 protein is encoded by the gene and is a membrane-anchored protein with multiple functions. In the last stage of viral replication, UL11 participates in the secondary envelopment process. It also plays a key role in primary envelopment, the transportation of newly assembled viral particles through cytoplasmic vesicles, and virion egress from the cell. UL11 is an important accessory protein and sometimes cooperates with other proteins that participate in virus-induced cell fusion. Cell fusion is necessary for cell-to-cell transmissions. This review summarizes the latest literature and discusses the roles of UL11 in viral assembly, primary and secondary envelopment, and cell-to-cell transmission to obtain a better understanding of the UL11 protein in the life cycle of herpesviruses and to serve as a reference for studying other viruses. Additionally, some recently discovered characteristics of UL11 are summarized.
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http://dx.doi.org/10.3389/fmicb.2022.829754 | DOI Listing |
Int J Biol Macromol
May 2025
Institute of Veterinary Medicine and Immunology Drugs, Veterinary Department in College of Animal Science, State Key Laboratory of Green Pesticide, GuiZhou University, GuiYang 550025, China. Electronic address:
Unique long (UL) 11, 16, and 21 proteins are duck plague virus (DPV) tegument proteins that are important in virus replication and cell-to-cell spread. gE is an envelope glycoprotein that is critical for DPV virulence. However, information regarding the interactions among DPV viral proteins is limited.
View Article and Find Full Text PDFbioRxiv
November 2024
Department of Oncology, Johns Hopkins University School of Medicine, Baltimore.
J Cell Biochem
December 2024
Molecular and Structural Biophysics Laboratory, Department of Biochemistry, North-Eastern Hill University, Shillong, India.
In recent years, it has been shown that the liquid-liquid phase separation (LLPS) of virus proteins plays a crucial role in their life cycle. It promotes the formation of viral replication organelles, concentrating viral components for efficient replication and facilitates the assembly of viral particles. LLPS has emerged as a crucial process in the replication and assembly of herpes simplex virus-1 (HSV-1).
View Article and Find Full Text PDFJ Gen Virol
January 2023
Department of Applied Veterinary Sciences, United Graduated School of Veterinary Sciences, Gifu University, 1-1 Yanagido, Gifu 501-1193, Japan.
Equine herpesvirus type 1 (EHV-1) UL11 is a 74-amino-acid (aa) protein encoded by ORF51. UL11 is modified by acylation including myristoylation and palmitoylation. Myristoylation of EHV-1 UL11 is assumed to occur on the N-terminal glycine, while palmitoylation is assumed to occur on the seventh and ninth cysteines.
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