Secretome-Wide Lysine Acetylation Profiling of Fusarium oxysporum Reveals Potential Virulence Factors in Sugarcane Pokkah Boeng Disease

TL;DR

This study identifies acetylated proteins in Fusarium oxysporum that may help cause sugarcane disease.

Contribution

The first secretome-wide lysine acetylation profiling in Fusarium oxysporum during sugarcane Pokkah Boeng disease.

Findings

291 acetylation sites identified in 85 secreted proteins of Fusarium oxysporum.

Eight upregulated Kac proteins are potential virulence factors in early sugarcane infection stages.

Abstract

Fusarium oxysporum is the causal agent of Pokkah Boeng disease (PBD) in sugarcane. Lysine acetylation (Kac) is a dynamic and reversible post-translational modification that plays a critical role in regulating diverse cellular processes. Although Kac is known to significantly influence protein function, its specific role within the F. oxysporum secretome during PBD pathogenesis remains poorly understood. In this study, we conducted a comprehensive analysis of the lysine acetylome across the F. oxysporum secretome. Utilizing highly sensitive immunoaffinity purification coupled with high-resolution liquid chromatography-tandem mass spectrometry (LC-MS/MS), we identified 291 acetylation sites within 85 potentially secreted proteins. Bioinformatics analysis revealed that these acetylated proteins are involved in a wide array of biological functions and exhibit diverse subcellular localizations. Notably, these secreted proteins represent a valuable resource for identifying novel effectors; specifically, eight upregulated genes encoding Kac proteins were identified as potential players during the initial asymptomatic stages of infection. Collectively, these findings provide a global overview of the F. oxysporum secretome acetylome and offer a foundational resource for elucidating the functional significance of lysine acetylation in sugarcane PBD pathogenesis.

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