Abstract
Soluble N-ethylmaleimide-sensitive factor attachment receptors (SNAREs) play a crucial role in the development and virulence through mediation of membrane fusion and vesicle trafficking in pathogens. Our previous studies reported that the SNARE protein FgVam7 and its binding proteins FgVps39/41 are involved in vesicle trafficking and are important for vegetative growth, asexual/sexual development, deoxynivalenol production and virulence in the Fusarium head blight fungus Fusarium graminearum. Here, we identified and characterized another FgVam7 binding protein in F. graminearum, FgPep12, an ortholog of yeast t-SNARE Pep12 with both the SNARE and TM domains being essential for its localization and function. Deletion of FgPep12 caused defects in vegetative growth, conidiogenesis, deoxynivalenol production and virulence. Cytological observation revealed that FgPep12 localizes to the Golgi apparatus, late endosomes and vacuoles, and is necessary for transport from the vacuole to prevacuolar compartment. Further investigation revealed that both FgPep12 and FgVam7 are essential for ascospore discharge through interaction with and trafficking of the Ca2+ ATPase FgNeo1 between the Golgi and endosomal/vacuolar system. FgNeo1 has similar biological roles to FgPep12 and is required for ascospore discharge in F. graminearum. Together, these results provide solid evidence to help unravel the mechanisms underlying the manipulation of ascospore discharge and plant infection by SNARE proteins in F. graminearum.
Highlights
In eukaryotic cells, directional transport among the organelles of the endomembrane system is mediated by vesicles that bud from a donor organelle and fuse with an acceptor organelle [1]
Together with the cognate effectors, sensitive factor attachment receptors (SNAREs) coordinate the dynamics of trafficking pathway and determines
We further provide multiple lines of evidence showing that SNARE proteins modulate development and ascospore discharge in pathogenic fungi
Summary
Directional transport among the organelles of the endomembrane system is mediated by vesicles that bud from a donor organelle and fuse with an acceptor organelle [1]. One family of integral membrane proteins, called soluble N-ethylmaleimide-sensitive factor attachment receptor (SNARE) proteins, constitute the key machinery of these membrane fusion events [1] and have been studied extensively in budding yeast, mammals, plants, and phytopathogens [4,5,6,7,8,9,10]. Despite their differences in sizes and structures among organisms, SNAREs share a conserved SNARE motif of 60–70 amino acids (AAs) arranged in heptad repeats [4, 6, 11,12]. T-SNARE MoSso is involved in virulence and is necessary for normal biotrophic interfacial complex development, as well as for secretion of cytoplasmic effectors during M. oryzae infection [20]
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