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What is the role of VP4 in the pathogenesis of IBDV infection? 


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VP4, a viral protease encoded by Infectious Bursal Disease Virus (IBDV), plays crucial roles in the pathogenesis of IBDV infection. VP4 forms intracellular tubule-like structures during infection, potentially impacting host cell integrity and viral replication . Additionally, VP4 utilizes a Ser/Lys catalytic dyad mechanism for polyprotein processing, with phosphorylation at specific sites affecting its protease activity . Furthermore, differences in VP4 proteins from various IBDV strains influence the expression of anti-viral type I interferon and proinflammatory genes, impacting disease outcomes . Moreover, VP4 has been identified as an interferon suppressor by interacting with host cell proteins, leading to the suppression of type I interferon and facilitating viral growth . Overall, VP4's multifaceted functions in viral replication, host cell interactions, and immune response modulation highlight its significance in the pathogenesis of IBDV infection.

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VP4 of IBDV interacts with GILZ to suppress type I interferon, aiding in immunosuppression and enhancing IBDV growth in host cells, highlighting its crucial role in pathogenesis.
VP4 in IBDV infection acts as a phosphoprotein with phosphorylated residues Ser538, Tyr611, and Thr674, contributing to cleavage of precursor VP4-VP3 polyprotein, affecting serine-protease activity.
VP4 protein of IBDV strains influences pathogenesis by downregulating innate antiviral responses, particularly type I IFN, contributing to enhanced virulence of very virulent strains like UK661.
The VP4 region in IBDV's polymerase plays a crucial role in viral replication and pathogenicity. Substitutions in this region can reduce pathogenicity but may not completely attenuate the virus.
VP4 in IBDV infection forms insoluble fibrils, reducing cytotoxicity, potentially preventing premature cell death, and facilitating viral replication by deforming host cell structures.

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