A Novel Aspartic Protease with HIV-1 Reverse Transcriptase Inhibitory Activity from Fresh Fruiting Bodies of the Wild Mushroom Xylaria hypoxylonReport as inadecuate




A Novel Aspartic Protease with HIV-1 Reverse Transcriptase Inhibitory Activity from Fresh Fruiting Bodies of the Wild Mushroom Xylaria hypoxylon - Download this document for free, or read online. Document in PDF available to download.

Journal of Biomedicine and BiotechnologyVolume 2012 2012, Article ID 728975, 8 pages

Research Article

State Key Laboratory for Agrobiotechnology and Department of Microbiology, China Agricultural University, Beijing 100193, China

Institute of Agricultural Resources and Regional Planning, Chinese Academy of Agricultural Sciences, Beijing 100081, China

Key Laboratory of Urban Agriculture North of Ministry of Agriculture, Beijing University of Agriculture, Beijing 102206, China

Beijing Academy of Science and Technology, Beijing 100089, China

School of Biomedical Sciences, Faculty of Medicine, The Chinese University of Hong Kong, Shatin, New Territories, Hong Kong

Received 18 January 2012; Revised 17 March 2012; Accepted 17 March 2012

Academic Editor: Guihua H. Bai

Copyright © 2012 Qing-Xiu Hu et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

A novel aspartic protease with HIV-1 RT inhibitory activity was isolated and characterized from fruiting bodies of the wild mushroom Xylaria hypoxylon. The purification protocol comprised distilled water homogenization and extraction step, three ion exchange chromatographic steps on DEAE-cellulose, Q-Sepharose, and CM-cellulose in succession, and final purification was by FPLC on Superdex 75. The protease was adsorbed on all the three ion exchangers. It was a monomeric protein with a molecular mass of 43 kDa as estimated by SDS-PAGE and FPLC. Its N-terminal amino acid sequence was HYTELLSQVV, which exhibited no sequence homology to other proteases reported. The activity of the protease was adversely affected by Pepstatin A, indicating that it is an aspartic protease. The protease activity was maximal or nearly so in the pH range 6–8 and in the temperature range 35– 6 0 ∘ C . The purified enzyme exhibited HIV-1 RT inhibitory activity with an IC50 value of 8.3 μM, but was devoid of antifungal, ribonuclease, and hemagglutinating activities.





Author: Qing-Xiu Hu, Guo-Qing Zhang, Rui-Ying Zhang, Dan-Dan Hu, He-Xiang Wang, and Tzi Bun Ng

Source: https://www.hindawi.com/



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