Global phosphoproteome analysis identifies PeVYV P4-induced host protein phosphorylation changes that facilitate viral proliferation.

ABSTRACT:

Background

Protein phosphorylation is a pivotal post-translational modification that regulates diverse biological processes, including signal transduction, growth and development, stress response, and metabolic regulation. Although it is known that the PeVYV P4 protein can co-attract vector and non-vector insects by fine-tuning the volatilization (VOL) of host metabolites, thereby facilitating viral infection and transmission [1], the functional consequences of P4-induced phosphorylation of these host proteins and their potential role in modulating host-PeVYV interaction remain unexplored. In this study, we present the first comprehensive phosphoproteomic analysis of Nicotiana tabacum induced by PeVYV P4 protein, revealing key phosphorylation events that may underlie P4-mediated vi

SUBMITTER: Li S 

PROVIDER: S-EPMC12628578 | biostudies-literature | 2025 Nov

REPOSITORIES: biostudies-literature