Related Experiment Video

Updated: Jan 13, 2026

A High Resolution Method to Monitor Phosphorylation-dependent Activation of IRF3
11:44

A High Resolution Method to Monitor Phosphorylation-dependent Activation of IRF3

Published on: January 24, 2016

12.4K

Phosphorylation of T425 and methylation of R426 synergistically regulate IBDV VP1 function and viral replication

Huiping Liang1, Xiangxiang Gao2, Yan Xiao1

  • 1Department of Veterinary Preventive Medicine, College of Animal Science and Technology, Jiangxi Agricultural University, Nanchang 330045, PR China; Jiangxi Provincial Key Laboratory for Animal Health, College of Animal Science and Technology, Jiangxi Agricultural University, Nanchang 330045, PR China.

Veterinary Microbiology
|January 8, 2026
PubMed

Insights

This study reveals how Infectious Bursal Disease Virus (IBDV) VP1 protein phosphorylation at T425 and methylation at R426 work together to boost viral replication. Understanding this crosstalk offers new antiviral targets.

Area of Science:

  • Virology
  • Molecular Biology
  • Biochemistry

Background:

  • Post-translational modifications (PTMs) regulate viral protein function and replication.
  • The interplay of multiple PTMs on Infectious Bursal Disease Virus (IBDV) polymerase VP1 is not well understood.

Purpose of the Study:

  • To identify and characterize novel PTMs on IBDV VP1.
  • To investigate the functional interplay between VP1 phosphorylation and methylation.
  • To explore potential antiviral targets for IBDV.

Main Methods:

  • Mass spectrometry and phospho-specific antibodies were used to identify and confirm VP1 phosphorylation at threonine 425 (T425).
  • Functional assays assessed the impact of T425 phosphorylation and arginine 426 (R426) methylation on VP1 polymerase activity and viral replication.
  • Recombinant IBDV with mutations in T425 and R426 sites were generated to study their combined effects.

Main Results:

  • A novel phosphorylation site at T425, adjacent to the R426 methylation site, was identified on IBDV VP1.
  • Phosphorylation at T425 enhances VP1 polymerase activity and viral replication; its mutation impairs viral growth.
  • A synergistic relationship exists between T425 phosphorylation and PRMT5-mediated R426 methylation; loss of one affects the other.
  • IBDV with double T425A/R426A mutations showed significantly reduced replication compared to single mutants.

Conclusions:

  • Adjacent phosphorylation and methylation sites on IBDV VP1 exhibit crosstalk, fine-tuning viral replication.
  • This crosstalk represents a novel regulatory mechanism for IBDV.
  • The identified PTMs offer potential targets for antiviral strategies and vaccine development.
Keywords:
IBDVMethylation of R426Phosphorylation of T425Post-translational modifications

More Related Videos

Dissecting Host-virus Interaction in Lytic Replication of a Model Herpesvirus11:28

Dissecting Host-virus Interaction in Lytic Replication of a Model Herpesvirus

Published on: October 7, 2011

11.4K
Dissecting Innate Immune Signaling in Viral Evasion of Cytokine Production08:32

Dissecting Innate Immune Signaling in Viral Evasion of Cytokine Production

Published on: March 2, 2014

10.9K

Related Concept Videos

Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
8.6K
Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
10.1K
Phosphorylation01:02

Phosphorylation

The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
53.6K
Leaky Scanning02:28

Leaky Scanning

During most eukaryotic translation processes, the small 40S ribosome subunit scans an mRNA from its 5' end until it encounters the first start AUG codon. The large 60S ribosomal subunit then joins the smaller one to initiate protein synthesis. The location of the translation initiation is largely determined by the nucleotides near the start codon as there may be multiple translation initiation sites present on the mRNA.  Marilyn Kozak discovered that the sequence RCCAUGG (where R...
5.6K
DNA Bacteriophages01:26

DNA Bacteriophages

Bacteriophages, or phages, are viruses that specifically infect bacteria, utilizing their genetic material to hijack host cellular machinery for replication. DNA bacteriophages employ single-stranded DNA (ssDNA) or double-stranded DNA (dsDNA) genomes. These phages exhibit diverse replication strategies and host interactions, influencing their ecological roles and applications in biotechnology and medicine.ssDNA BacteriophagesssDNA phages, with their small genomes, utilize unique strategies to...
790
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
14.9K