Abstract
SummarySoluble N‐ethylmaleimide‐sensitive factor attachment protein receptors (SNAREs) are conserved in fungi, plants and animals. The Vam7 gene encodes a v‐SNARE protein that involved in vesicle trafficking in fungi. Here, we identified and characterized the function of FolVam7, a homologue of the yeast SNARE protein Vam7p in Fusarium oxysporum f. sp. lycopersici (Fol), a fungal pathogen of tomato. FolVam7 contains SNARE and PX (Phox homology) domains that are indispensable for normal localization and function of FolVam7. Targeted gene deletion showed that FolVam7‐mediated vesicle trafficking is important for vegetative growth, asexual development, conidial morphology and plant infection. Further cytological examinations revealed that FolVam7 is localized to vesicles and vacuole membranes in the hyphae stage. Moreover, the ΔFolvam7 mutant is insensitive to salt and osmotic stresses and hypersensitive to cell wall stressors. Taken together, our results suggested that FolVam7‐mediated vesicle trafficking promotes vegetative growth, conidiogenesis and pathogenicity of Fol.
Highlights
In eukaryotic cells, directional protein transport between different organelles/compartments of the endomembrane system is mediated by vesicle trafficking and is essential for the survival of organisms (Kienle et al, 2009)
The t-sensitive factor attachment protein receptors (SNAREs) MoSso1 is involved in virulence, as it is required for the formation of a normal biotrophic interfacial complex (BIC) and for the secretion of cytoplasmic effectors during M. oryze infection (Giraldo et al, 2013)
Previous studies have shown that fungal SNARE proteins homologous to Vam7 play an important role in fungal development and vacuole fusion (Wedlich-Soldner et al, 2000; Dou et al, 2011; Zhang et al, 2016)
Summary
Directional protein transport between different organelles/compartments of the endomembrane system is mediated by vesicle trafficking and is essential for the survival of organisms (Kienle et al, 2009). Soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteins are part of the core machineries of these different membrane fusion events and have been characterized extensively in mammals, plants, Saccharomyces cerevisiae and phytopathogens (Burri et al, 2003; Burri and Lithgow, 2004; Kienle et al, 2009; Song et al, 2010; Dou et al, 2011; Qi et al, 2016; Zhang et al, 2016; Li et al, 2017). The t-SNARE MoSso is involved in virulence, as it is required for the formation of a normal biotrophic interfacial complex (BIC) and for the secretion of cytoplasmic effectors during M. oryze infection (Giraldo et al, 2013)
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