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OMICS. 2018 Aug;22(8):544-552. doi: 10.1089/omi.2018.0093.

Dissecting Candida Pathobiology: Post-Translational Modifications on the Candida tropicalis Proteome.

Author information

1
1 Center for Systems Biology and Molecular Medicine, Yenepoya Research Centre, Yenepoya (Deemed to be University) , Mangalore, India .
2
2 Institute of Bioinformatics , International Technology Park, Bangalore, India .
3
3 School of Biotechnology, KIIT (Deemed to be University) , Bhubaneswar, India .
4
4 Department of Biochemistry and Molecular Biology, School of Life Sciences, Pondicherry University , Pondicherry, India .
5
5 Department of Biological Chemistry, Johns Hopkins University School of Medicine , Baltimore, Maryland.
6
6 Department of Oncology, Johns Hopkins University School of Medicine , Baltimore, Maryland.
7
7 Department of Pathology, Johns Hopkins University School of Medicine , Baltimore, Maryland.
8
8 Manipal Academy of Higher Education (MAHE), Manipal 576104, Karnatka, India .

Abstract

Candida tropicalis belongs to the non-albicans group of Candida, and causes epidermal, mucosal, or systemic candidiasis in immunocompromised individuals. Although the prevalence of candidiasis has increased worldwide and non-albicans Candida (NAC) are becoming more significant, there are very few studies that focus on the NAC biology. Proteins and their post-translational modifications (PTMs) are an integral aspect in the pathobiology of such medically important fungi. Previously, we had reported the largest proteomic catalog of C. tropicalis. Notably, PTMs can be identified from proteomics data without a priori enrichment for a particular PTM, thus allowing broad-scale omics analyses. In this study, we developed the "PTM-Pro," a graphical user interface-based tool for identification and summary of high-confidence PTM sites based on statistical threshold of users' choice. We mined available proteomic data of C. tropicalis, and using PTM-Pro identified nearly 600 high-confidence PTM sites. The PTMs identified include phosphorylation of serine, threonine, and tyrosine; acetylation, crotonylation, methylation, and succinylation of lysine. These PTMs reside on biologically significant molecules, including histones, enzymes, and transcription factors. To our knowledge, this is the first report of PTMs in C. tropicalis and lays a foundation for future investigations of C. tropicalis PTMs. In addition, the PTM-Pro offers a graphical user interface tool for research on PTM sites in the field of proteomics.

KEYWORDS:

bioinformatics; candidiasis; infectious diseases; mass spectrometry; proteomics

PMID:
30106353
DOI:
10.1089/omi.2018.0093
[Indexed for MEDLINE]

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