The N-terminal glycine of EHV-1 UL11 is essential for the localization of UL11 and EHV-1 replication in cultured cells.
Abstract: 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. ORF51, which encodes the first 24 aa, overlaps ORF50 encoding UL12. We previously demonstrated that UL11 was essential for EHV-1 replication in cultured cells and that UL11 was localized at the Golgi apparatus where herpesviruses obtain their final envelope. It is unclear whether the acylation is related to the localization of EHV-1 UL11 and viral replication. In this study, we investigated the role of UL11 acylation in the intracellular localization and viral growth and replication of EHV-1. We constructed seven UL11 acylation mutant plasmids and seven UL11 acylation mutant BAC DNAs; then, we analysed the localizations of the mutant UL11s and attempted virus rescue. We found that both the N-terminal glycine and the seventh or ninth cysteine, especially N-terminal glycine, were involved in the localization of UL11 and viral replication. Taken together, these results suggest that EHV-1 viral growth requires that UL11 is modified by myristoylation of an N-terminal glycine and by palmitoylation of at least one of the cysteines, and that UL11 is localized at the Golgi apparatus. This study shows that a single amino acid in EHV-1 can determine the fate of viral replication.
Publication Date: 2023-02-08 PubMed ID: 36748631DOI: 10.1099/jgv.0.001798Google Scholar: Lookup
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- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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The research article is about an investigation on how the acylation of UL11, a protein of the Equine herpesvirus type 1 (EHV-1), contributes to its intracellular localization and the virus’s replication process.
Introduction
- The study focuses on EHV-1 UL11, a protein made up of 74 amino acids, which is encoded by the ORF51 gene.
- This protein undergoes modification by acylation processes, which include myristoylation and palmitoylation.
- Myristoylation involves the N-terminal glycine, while palmitoylation occurs on the seventh and ninth cysteines.
- Previous research showed that UL11 is crucial to viral replication, and it is found at the Golgi apparatus where herpesviruses obtain their final envelope.
Purpose of the Study
- The goal was to ascertain the role of UL11 acylation in its positioning within the cell and its contribution to EHV-1 growth and replication.
- This aims to address an existing gap in knowledge, as it wasn’t clear if acylation was linked to the location of EHV-1 UL11 and to viral replication.
Procedure
- The researchers built seven UL11 acylation mutant plasmids and seven UL11 acylation mutant BAC DNAs.
- The positions of the mutant UL11s were analyzed and virus rescue efforts were conducted.
Results
- It was discovered that both the N-terminal glycine and the seventh or ninth cysteine, especially N-terminal glycine, participated in the localization of UL11 and viral replication.
- Overall, the findings suggest that for the virus to grow, UL11 has to be modified by myristoylation of an N-terminal glycine and by palmitoylation of at least one of the cysteines.
- The modification ensures that UL11 is localized at the Golgi apparatus, where it plays a critical role.
Conclusion
- This study elucidates that a single amino acid in EHV-1 can determine the success or failure of viral replication.
- It provides a deeper insight into how herpesviruses like EHV-1 operate and how their replication process can potentially be curtailed.
Cite This Article
APA
Fukushi N, Badr Y, Fukushi H.
(2023).
The N-terminal glycine of EHV-1 UL11 is essential for the localization of UL11 and EHV-1 replication in cultured cells.
J Gen Virol, 104(1).
https://doi.org/10.1099/jgv.0.001798 Publication
Researcher Affiliations
- Department of Applied Veterinary Sciences, United Graduated School of Veterinary Sciences, Gifu University, 1-1 Yanagido, Gifu 501-1193, Japan.
- Department of Applied Veterinary Sciences, United Graduated School of Veterinary Sciences, Gifu University, 1-1 Yanagido, Gifu 501-1193, Japan.
- Department of Animal Medicine (Branch of Infectious Disease), Faculty of Veterinary Medicine, Damanhour University, El-Beheira 2251, Egypt.
- Department of Applied Veterinary Sciences, United Graduated School of Veterinary Sciences, Gifu University, 1-1 Yanagido, Gifu 501-1193, Japan.
- Laboratory of Veterinary Microbiology, Faculty of Applied Biological Sciences, Gifu University, 1-1 Yanagido, Gifu 501-1193, Japan.
- Joint Graduate School of Veterinary Sciences, Gifu University, 1-1 Yanagido, Gifu 501-1193, Japan.
MeSH Terms
- Animals
- Horses
- Herpesvirus 1, Equid / genetics
- Glycine / metabolism
- Viral Structural Proteins / metabolism
- Virus Replication
- Cell Line
- Amino Acids / metabolism
- Cysteine
Citations
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