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Abstract

Phosphorylation and dephosphorylation of viral movement proteins plays a crucial role in regulating virus movement. Our study focused on investigating the movement protein TGBp1 of (BaMV), which is a single-stranded positive-sense RNA virus. Specifically, we examined four potential phosphorylation sites (S15, S18, T58, and S247) within the TGBp1 protein. To study the impact of phosphorylation, we introduced amino acid substitutions at the selected sites. Alanine substitutions were used to prevent phosphorylation, while aspartate substitutions were employed to mimic phosphorylation. Our findings suggest that mimicking phosphorylation at S15, S18 and T58 of TGBp1 might be linked to silencing suppressor activities. The phosphorylated form at these sites exhibits a loss of silencing suppressor activity, leading to reduced viral accumulation in the inoculated leaves. Furthermore, mimicking phosphorylation at residues S15 and S18 could diminish viral accumulation at the single-cell level, while doing so at residue T58 could influence virus movement. However, mimicking phosphorylation at residue S247 does not appear to be relevant to both functions of TGBp1. Overall, our study provides insights into the functional significance of specific phosphorylation sites in BaMV TGBp1, illuminating the regulatory mechanisms involved in virus movement and silencing suppression.

Funding
This study was supported by the:
  • Tzu Chi University (Award TCMRC-P-111006)
    • Principal Award Recipient: Chi-PingCheng
  • Ministry of Education,Taiwan
    • Principal Award Recipient: Ching-HsiuTsai
  • Tzu Chi University (Award TCMRC-P-111005)
    • Principal Award Recipient: Chi-PingCheng
  • This is an open-access article distributed under the terms of the Creative Commons Attribution License.
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/content/journal/jgv/10.1099/jgv.0.001945
2024-01-08
2025-12-07

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