Sahu Mahima Sagar, Patra Sandip, Kumar Kundan, Kaur Rupinder
Laboratory of Fungal Pathogenesis, Centre for DNA Fingerprinting and Diagnostics, Hyderabad 500039, Telangana, India.
Graduate studies, Regional Centre for Biotechnology, Faridabad 121001, Haryana, India.
J Fungi (Basel). 2020 Mar 4;6(1):32. doi: 10.3390/jof6010032.
The small ubiquitin-related modifier (SUMO) protein is an important component of the post-translational protein modification systems in eukaryotic cells. It is known to modify hundreds of proteins involved in diverse cellular processes, ranging from nuclear pore dynamics to signal transduction pathways. Owing to its reversible nature, the SUMO-conjugation of proteins (SUMOylation) holds a prominent place among mechanisms that regulate the functions of a wide array of cellular proteins. The dysfunctional SUMOylation system has been associated with many human diseases, including neurodegenerative and autoimmune disorders. Furthermore, the non-pathogenic yeast has served as an excellent model to advance our understanding of enzymes involved in SUMOylation and proteins modified by SUMOylation. Taking advantage of the tools and knowledge obtained from the SUMOylation system, research on fungal SUMOylation is beginning to gather pace, and new insights into the role of SUMOylation in the pathobiology of medically important fungi are emerging. Here, we summarize the known information on components of the SUMOylation machinery, and consequences of overexpression or deletion of these components in the human pathogenic fungi, with major focus on two prevalent bloodstream pathogens, and . Additionally, we have identified SUMOylation components, through in silico analysis, in four medically relevant fungi, and compared their sequence similarity with counterparts. SUMOylation modulates the virulence of and , while it is required for conidia production in and . In addition to highlighting these recent developments, we discuss how SUMOylation fine tunes the expression of virulence factors, and influences survival of fungal cells under diverse stresses in vitro and in the mammalian host.
小泛素相关修饰物（SUMO）蛋白是真核细胞中翻译后蛋白质修饰系统的重要组成部分。已知它能修饰数百种参与多种细胞过程的蛋白质，从核孔动态变化到信号转导途径。由于其可逆性，蛋白质的SUMO化修饰（SUMOylation）在调节多种细胞蛋白质功能的机制中占据显著地位。功能失调的SUMO化系统与许多人类疾病相关，包括神经退行性疾病和自身免疫性疾病。此外，非致病性酵母已成为一个优秀的模型，有助于我们深入了解参与SUMO化修饰的酶以及被SUMO化修饰的蛋白质。利用从SUMO化系统获得的工具和知识，对真菌SUMO化修饰的研究开始加速，关于SUMO化修饰在医学上重要真菌的病理生物学中的作用也有了新的见解。在这里，我们总结了关于SUMO化修饰机制组成部分的已知信息，以及在人类致病真菌中这些组成部分过表达或缺失的后果，主要聚焦于两种常见的血液传播病原体，即[病原体名称1]和[病原体名称2]。此外，我们通过计算机分析在四种医学相关真菌中鉴定了SUMO化修饰成分，并将它们与[对比对象]的序列相似性进行了比较。SUMO化修饰调节[病原体名称1]和[病原体名称2]的毒力，而在[真菌名称1]和[真菌名称2]中分生孢子的产生需要SUMO化修饰。除了强调这些最新进展外，我们还讨论了SUMO化修饰如何微调毒力因子的表达，以及如何影响真菌细胞在体外和哺乳动物宿主的各种应激条件下的存活。
