title: Identification of Components of the SUMOylation Machinery in Candida glabrata: ROLE OF THE DESUMOYLATION PEPTIDASE CgUlp2 IN VIRULENCE.
abstract: Regulation of protein function by reversible post-translational modification, SUMOylation, is widely conserved in the eukaryotic kingdom. SUMOylation is essential for cell growth, division, and adaptation to stress in most organisms, including fungi. As these are key factors in determination of fungal virulence, in this study, we have investigated the importance of SUMOylation in the human pathogen, Candida glabrata We identified the enzymes involved in small ubiquitin-like modifier conjugation and show that there is strong conservation between Saccharomyces cerevisiae and C. glabrata We demonstrate that SUMOylation is an essential process and that adaptation to stress involves changes in global SUMOylation in C. glabrata Importantly, loss of the deSUMOylating enzyme CgUlp2 leads to highly reduced small ubiquitin-like modifier protein levels, and impaired growth, sensitivity to multiple stress conditions, reduced adherence to epithelial cells, and poor colonization of specific tissues in mice. Our study thus demonstrates a key role for protein SUMOylation in the life cycle and pathobiology of C. glabrata.
authors.affiliation: From the Centre for DNA Fingerprinting and Diagnostics, Building 7, Gruhakalpa, 5-4-399/B, Nampally, Hyderabad 500001.
authors.forename: Rahul
authors.initials: R
authors.lastname: Gujjula
authors.affiliation: the Department of Biochemistry, School of Life Science, University of Hyderabad, Prof. C. R. Rao Road, Gachibowli, Hyderabad 500046.
authors.forename: Sangeetha
authors.initials: S
authors.lastname: Veeraiah
authors.affiliation: From the Centre for DNA Fingerprinting and Diagnostics, Building 7, Gruhakalpa, 5-4-399/B, Nampally, Hyderabad 500001, the Graduate Studies Program, Manipal University, Manipal, Karnataka 576104, and.
authors.forename: Kundan
authors.initials: K
authors.lastname: Kumar
authors.affiliation: the Centre for Cellular and Molecular Biology, Habsiguda, Uppal Road, Hyderabad 500007, India.
authors.forename: Suman S
authors.initials: SS
authors.lastname: Thakur
authors.affiliation: the Department of Biochemistry, School of Life Science, University of Hyderabad, Prof. C. R. Rao Road, Gachibowli, Hyderabad 500046, krishnaveni.mishra@gmail.com.
authors.forename: Krishnaveni
authors.initials: K
authors.lastname: Mishra
authors.affiliation: From the Centre for DNA Fingerprinting and Diagnostics, Building 7, Gruhakalpa, 5-4-399/B, Nampally, Hyderabad 500001, rkaur@cdfd.org.in.
authors.forename: Rupinder
authors.initials: R
authors.lastname: Kaur
mesh_terms: D000818:Animals; D041221:Candida glabrata / Q000201:enzymology* / Q000235:genetics / Q000472:pathogenicity*; D002177:Candidiasis / Q000201:enzymology* / Q000235:genetics / Q000473:pathology; D045744:Cell Line, Tumor; D010450:Endopeptidases / Q000235:genetics / Q000378:metabolism*; D005260:Female; D005656:Fungal Proteins / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D051379:Mice; D008807:Mice, Inbred BALB C; D058207:Sumoylation; D037521:Virulence Factors / Q000235:genetics / Q000378:metabolism*
chemical_list: D005656:Fungal Proteins; D037521:Virulence Factors; D010450:Endopeptidases
keywords: C. glabrata; Epa adhesins; SUMO ligase; SUMO peptidase; adhesion; biofilm; fungal pathogenesis; microbial pathogenesis; small ubiquitin-like modifier (SUMO); sumoylation