Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2021 Aug 11;27(9):246.
doi: 10.1007/s00894-021-04853-7.

Unveiling the structure of GPI-anchored protein of Malassezia globosa and its pathogenic role in pityriasis versicolor

Affiliations

Unveiling the structure of GPI-anchored protein of Malassezia globosa and its pathogenic role in pityriasis versicolor

Sanaz Aghaei Gharehbolagh et al. J Mol Model. .

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.

Keywords: GPI-anchored protein; Homology modeling; Malassezia globosa; Molecular dynamic simulation; Phylogenetic; Virulence factor.

PubMed Disclaimer

References

    1. Mirhendi H et al (2005) A simple PCR-RFLP method for identification and differentiation of 11 Malassezia species. J Microbiol Methods 61(2):281–284 - PubMed - DOI - PMC
    1. Gaitanis G et al (2002) Identification of Malassezia species from patient skin scales by PCR-RFLP. Clin Microbiol Infect 8(3):162–173 - PubMed - DOI - PMC
    1. Gupta AK, Kohli Y, Summerbell RC (2000) Molecular differentiation of seven Malassezia species. J Clin Microbiol 38(5):1869–1875 - PubMed - PMC - DOI
    1. Makimura K et al (2000) Species identification and strain typing of Malassezia species stock strains and clinical isolates based on the DNA sequences of nuclear ribosomal internal transcribed spacer 1 regions. J Med Microbiol. 49(1):29–35 - PubMed - DOI - PMC
    1. Morais PMD, Cunha MDGS, Frota MZM (2010) Clinical aspects of patients with pityriasis versicolor seen at a referral center for tropical dermatology in Manaus, Amazonas, Brazil. An Bras Dermatol 85(6):797–803 - PubMed - DOI - PMC

Supplementary concepts

LinkOut - more resources