Glu1, a conserved GH30_3 β-(1,6)-glucanase requires its catalytic residues for full virulence in Ustilago maydis

Glu1, a conserved GH30_3 β-(1,6)-glucanase from Ustilago maydis, requires its catalytic residues to achieve full virulence during maize infection.

• Why it matters: Plant-pathogenic fungi must remodel their cell wall during infection, yet the specific GH30 enzymes that support successful colonization and tumor formation remain unclear.
• What they did: The authors characterized Glu1 by structural comparison to GH30_3 β-(1,6)-glucanases, measured infection-induced expression and secretion, localized it to the plasma membrane, and tested glu1 deletion and catalytic-site rescue variants.
• The result: Deleting glu1 reduced virulence, plant colonization, and tumour formation and altered septation and morphology; catalytic-site variants largely restored saprophytic phenotypes but not virulence, while Umag_04357 deletion did not affect virulence.

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