Son Ye-Eun, Jung Won-Hee, Oh Sang-Hun, Kwak Jin-Hwan, Cardenas Maria E, Park Hee-Soo
School of Food Science and Biotechnology, Institute of Agricultural Science and Technology, Kyungpook National University, Daegu, Republic of Korea.
School of Life Science, Handong Global University, Pohang, Republic of Korea.
Mycobiology. 2018 May 21;46(2):114-121. doi: 10.1080/12298093.2018.1468053. eCollection 2018.
Mon1 is a guanine nucleotide exchange factor subunit that activates the Ypt7 Rab GTPase and is essential for vacuole trafficking and autophagy in eukaryotic organisms. Here, we identified and characterized the function of Mon1, an ortholog of Mon1, in a human fungal pathogen, . Mutation in resulted in hypersensitivity to thermal stress. The deletion mutant exhibited increased sensitivity to cell wall and endoplasmic reticulum stress. However, the deletion mutant showed more resistance to the antifungal agent fluconazole. studies demonstrated that compared to the wild-type strain, the deletion mutant attenuated virulence in the insect model. Moreover, the deletion mutant was avirulent in the murine inhalation model. These results demonstrate that Mon1 plays a crucial role in stress survival and pathogenicity in .
Mon1是一种鸟嘌呤核苷酸交换因子亚基，可激活Ypt7 Rab GTP酶，对真核生物中的液泡运输和自噬至关重要。在此，我们鉴定并表征了人类真菌病原体中Mon1直系同源物Mon1的功能。Mon1突变导致对热应激超敏。Mon1缺失突变体对细胞壁和内质网应激表现出更高的敏感性。然而，Mon1缺失突变体对抗真菌剂氟康唑表现出更强的抗性。研究表明，与野生型菌株相比，Mon1缺失突变体在昆虫模型中减弱了毒力。此外，Mon1缺失突变体在小鼠吸入模型中无致病性。这些结果表明，Mon1在该病原体的应激存活和致病性中起关键作用。
