Abstract
In Aspergillus fumigatus, an opportunistic fungal pathogen causing fatal invasive aspergillosis, N-glycosylation is vital for polarized growth. To investigate its mechanism, two putative L-type lectin genes emp47 (AFUB_032470) and vip36 (AFUB_027870) were identified in A. fumigatus. Deletion of the emp47 or vip36 gene resulted in delayed germination and abnormal polarity. Also, the Δemp47 displayed an increased resistance to azoles whereas the Δvip36 showed an increased susceptibility to amphotericin B. Secretome analysis revealed that 205 proteins were differentially secreted in the Δemp47 and 145 of them were reduced, while 153 proteins displayed a differential secretion and 134 of them were increased in the Δvip36 as compared with that of the wild-type strain. Also, potential cargo glycoproteins of Emp47 and Vip36 were identified by comparative secretome analysis. Our results suggest that Emp47 is responsible for the transport of proteins from endoplasmic reticulum (ER) to Golgi, while Vip36 acts in protein retrieval from Golgi to ER.
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