Authors: Verma, Pravesh
Doharey, Pawan Kumar
Yadav, Sunita
Omer, Ankur
Singh, Poonam
Saxena, Jitendra Kumar
Title: Molecular cloning and characterization of protein disulfide isomerase of Brugia malayi, a human lymphatic filarial parasite
Language (ISO): en
Abstract: Lymphatic filariasis results in an altered lymphatic system and the abnormal enlargement of body parts, causing pain, serious disability and social stigma. Effective vaccines are still not available nowadays, drugs against the disease is required. Protein disulfide isomerase (PDI) is an essential catalyst of the endoplasmic reticulum which is involved in folding and chaperone activities in different biological systems. Here, we report the enzymatic characterization of a Brugia malayi Protein disulfide isomerase (BmPDI), which was expressed and purified from Escherichia coli BL21 (DE3). Western blotting analysis showed the recombinant BmPDI could be recognized by anti-BmPDI Rabbit serum. The rBmPDI exhibited an optimum activity at pH 8 and 40 °C. The enzyme was inhibited by aurin and PDI inhibitor. Recombinant BmPDI showed interaction with recombinant Brugia malayi calreticulin (rBmCRT). The three-dimensional model for BmPDI and BmCRT was generated by homology modelling. A total of 25 hydrogen bonds were found to be formed between two interfaces. There are 259 non-bonded contacts present in the BmPDI-BmCRT complex and 12 salt bridges were formed in the interaction.
Subject Headings: protein disulfide isomerase
Brugia malayi
antifilarials
homology modelling and docking
URI: http://hdl.handle.net/2003/36202
http://dx.doi.org/10.17877/DE290R-18216
Issue Date: 2017-06-01
Appears in Collections:Original Articles

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