Inhibition of Key Fungal (02) Protein(s) (Aspergillus fumigatus) In-Response to Treatment with Poly-Acid Ligand

Author(s): Sonam Ruhil, Vikash Kumar, Meenakshi Balhara, Monika Malik, Sandeep Dhankhar, Anil Kumar Chhillar

Journal Name: Current Proteomics

Volume 13 , Issue 3 , 2016

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Graphical Abstract:


Background: The fungal genus Aspergillus contains a number of species that are capable of causing a spectrum of diseases in immunocompromised humans. A. fumigatus accounts for approximately 90% of life-threatening infections. Poly –acid ligand i.e. EDTA having potent antifungal activity against A. fumigatus was investigated for its effect on fungal proteins.

Objective: The foremost objective of this research to reveal A.fumigatus proteins inhibited in response to polyacid ligand i.e. EDTA.

Methods: The proteins profile has been analysed by silver stained gel electrophoresis. The inhibited proteins then subjected to mass spectrophotometer. Further to quantify the results, morphological effect of EDTA (MIC50-19.0 µg/ml) on fungus is studied by Scanning Electron Microscopy (SEM). The toxicity of EDTA was determined by MTT assay.

Results: The research identified expression of two protein(s) i.e. 74/86kDa is inhibited. The peptide mass fingerprinting identified these protein(s) bands as Phenyl alanyl t-RNA synhetase alpha subunit PodG and di-peptidyl peptidase. The Scanning electron microscopy showed EDTA inhibited the hyphal growth and also induced striking changes in hyphal morphology (like wrinkled, flattened hyphae with disrupted tips). These cytological effects on hyphal growth and two targeted proteins of A. fumigatus might be responsible for anti- Aspergillus activity of EDTA. Moreover EDTA was found to be non toxic up to 250 µg/ml by MTT assay.

Conclusion: Phenyl alanyl t-RNA synhetase alpha subunit PodG and di-peptidyl peptidase might be further studied to use them as target molecules in future or in translational medicine. It can be proceeded for establishing an animal model to test its efficacy (in progress).

Keywords: A. fumigatus, Di-peptidyl peptidase, EDTA, Electron microscopy, Hyphal morphology, Phenyl alanyl t-RNA synhetase alpha subunit PodG.

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Article Details

Year: 2016
Page: [179 - 186]
Pages: 8
DOI: 10.2174/1570164613666160609083557
Price: $25

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