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Unveiling the Structure of Gpi-Anchored Protein of Malassezia Globosa and Its Pathogenic Role in Pityriasis Versicolor Publisher Pubmed



Aghaei Gharehbolagh S1 ; Mafakher L2 ; Salehi Z3 ; Asgari Y4 ; Hashemi SJ1, 5 ; Mahmoudi S6 ; Nasimi M7 ; Rezaie S1
Authors
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Authors Affiliations
  1. 1. Department of Medical Parasitology and Mycology, School of Public Health, Tehran University of Medical Sciences, Tehran, Iran
  2. 2. Thalassemia & Hemoglobinopathy Research center, Health research institute, Ahvaz Jundishapur University of Medical Science, Ahvaz, Iran
  3. 3. Department of Mycology, Faculty of Medical Sciences, Tarbiat Modares University, Tehran, 14115-331, Iran
  4. 4. Department of Medical Biotechnology, School of Advanced Technologies in Medicine, Tehran University of Medical Sciences, Tehran, Iran
  5. 5. Food Microbiology Research Center, Tehran University of Medical Sciences, Tehran, Iran
  6. 6. Department of Medical Parasitology and Mycology, School of Medicine, Iran University of Medical Sciences, Tehran, Iran
  7. 7. Department of Dermatology, Razi Hospital, Tehran University of Medical Sciences, Tehran, Iran

Source: Journal of Molecular Modeling Published:2021


Abstract

Glycosylphosphatidylinositols (GPI)-anchored proteins (GpiPs) are related to the cell wall biogenesis, adhesion, interactions, protease activity, mating, etc. These proteins have been identified in many organisms, including fungi such as Neurospora crassa, Candida albicans, Saccharomyces cerevisiae, and Fusarium graminearum. MGL-3153 gene of Malassezia globosa (M. globosa) encodes a protein which is homologous of the M. restricta, M. sympodialis, M. Pachydermatis, and U. maydis GpiPs. Real-time PCR assay showed that the expression of MGL_3153 gene was significantly up-regulated among M. globosa isolated from patients with pityriasis versicolor (PV) compared to a healthy individual, suggesting the contribution of this gene in the virulence of M. globosa. Accordingly, the sequence of this protein was analyzed by bioinformatics tools to evaluate the structure of that. The conservation analysis of MGL-3153 protein showed that the C-terminal region of this protein, which is responsible for GPI-anchor ligation, was highly conserved during evolution while the N-terminal region just conserved in Malassezia species. Moreover, the predicted tertiary structure of this protein by homology modeling showed that this protein almost has alpha helix structure and represented a stable structure during 150 ns of molecular dynamic simulation. Our results revealed that this protein potentially belongs to GPI-anchored proteins and may contribute to the virulence of M. globosa which warrants further investigations in this area. © 2021, The Author(s), under exclusive licence to Springer-Verlag GmbH Germany, part of Springer Nature.
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