Fusarium verticillioides SNARE protein FvSyn1 harbours two key functional motifs that play selective roles in fungal development and virulence.

Abstract

Fusarium verticillioides is one of the key fungal pathogens responsible for maize stalk rot. While stalk rot pathogens are prevalent worldwide, our understanding of the stalk rot virulence mechanism in pathogenic fungi is still very limited. We previously identified the F. verticillioides FvSYN1 gene, which was demonstrated to play an important role in maize stalk rot virulence. FvSyn1 belongs to a family of soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteins that play critical roles in a variety of developmental processes. In this study, we further characterized the cellular features of the FvSyn1 protein, namely how different motifs contribute to development and virulence in F. verticillioides by generating motif-specific deletion mutants. Microscopic observation showed that the ∆Fvsyn1 mutant exhibits rough and hyper-branched hyphae when compared to the wild-type progenitor. Moreover, the ∆Fvsyn1 mutant was sensitive to cell wall stress agents, resulting in vegetative growth reduction. We showed that the FvSyn1::GFP protein is associated with the endomembrane, but this did not clarify why the deletion of FvSyn1 led to stress sensitivity and aberrant hyphal development. Characterization of the FvSyn1 domains indicated that both the syntaxin N-terminus (SynN) domain and the SNARE C-terminus domain play distinct roles in fungal development, but also function collectively in the context of virulence. We also determined that two domains in FvSyn1 are not required for fumonisin production. Interestingly, these two domains were involved in carbon nutrient utilization, including pectin, starch and sorbitol. This study further characterized the role of FvSyn1 domains in hyphal growth, cell wall stress response and virulence in F. verticillioides.