Previous studies of the lipid droplet-coating protein Cap20 in Colletotrichum show that it plays a key role in appressorium development and virulence. In this study, the hydrophobin CsHydr1, which contains a signal peptide of 19 amino acids and a hydrophobic domain (HYDRO), was shown to interact with CsCap20 in Colletotrichum siamense. The CsHydr1 deletion mutant showed slightly enhanced mycelial growth, small conidia, slow spore germination and appressoria formation, cell wall integrity and virulence. Like CsCAP20, CsHydr1 is also localized on the lipid droplet surface of C. siamense. However, when CsCap20 was absent, some CsHydr1 was observed in other parts. Quantitative lipid determination showed that the absence of either CsHydr1 or CsCap20 reduced the content of lipids in mycelia and conidia, while the effect of CsCap20 was more obvious; these results suggest that an interaction protein CsHydr1 of CsCap20 is localized on the lipid droplet surface and involved in lipid metabolism, which affects appressorium formation and virulence in C. siamense.
Keywords: Colletotrichum siamense; appressoriual turgor pressure; hydrophobin CsHydr1; lipid droplet-coating protein CsCap20; virulence.