SUMOylation in Human Pathogenic Fungi: Role in Physiology and Virulence

• Published in: Journal of fungi (Basel) Vol. 6; no. 1; p. 32
• Main Authors: Sahu, Mahima Sagar, Patra, Sandip, Kumar, Kundan, Kaur, Rupinder
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 01-03-2020; MDPI
• Subjects: candida albicans; candida glabrata; Development and progression; Mycoses; Pathogenic fungi; Physiological aspects; Post-translational modifications; Review; small ubiquitin-like modifier (sumo), human pathogenic fungi; stress survival; sumo-specific proteases and ligases; virulence; Virulence (Microbiology); India; Candida albicans; Stress survival; Small ubiquitin-like modifier (SUMO), Human pathogenic fungi; Candida glabrata; SUMO-specific proteases and ligases; Virulence
• ISSN: 2309-608X; 2309-608X
• 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.