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      An inhibition model of BPTI to unlinked dengue virus NS2B-NS3 protease.

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          Abstract

          One approach to treating the dengue virus infection is to inhibit its NS2B-NS3 protease that plays a vital role in virus maturation. However, the lack of structural information on the active conformation of the protease hindered related drug design. With a co-expression system, we obtained the active two-component protease in its unlinked form. BPTI shows strong competitive inhibitory activity (Ki = 6.5 nM) against this unlinked protease, which adopts a closed conformation. Based on the biochemical and NMR perturbation information, an inhibition model of BPTI to NS2B-NS3 protease is proposed.

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          Author and article information

          Journal
          Journal ID (iso-abbrev): FEBS Lett.
          Title: FEBS letters
          Publisher: Elsevier BV
          ISSN (Electronic): 1873-3468
          ISSN (Print): 0014-5793
          Publication date (Electronic): Aug 25 2014
          Volume: 588
          Issue: 17
          Affiliations
          [1 ] Guangzhou Institutes of Biomedicine and Health, Chinese Academy of Sciences, Guangzhou 510530, China; Graduate University of Chinese Academy of Sciences, Beijing 100049, China.
          [2 ] High Magnetic Field Laboratory, Chinese Academy of Sciences, Hefei 230031, China; Graduate University of Chinese Academy of Sciences, Beijing 100049, China.
          [3 ] Guangzhou Institutes of Biomedicine and Health, Chinese Academy of Sciences, Guangzhou 510530, China.
          [4 ] High Magnetic Field Laboratory, Chinese Academy of Sciences, Hefei 230031, China.
          [5 ] High Magnetic Field Laboratory, Chinese Academy of Sciences, Hefei 230031, China. Electronic address: junfeng@hmfl.ac.cn.
          [6 ] Guangzhou Institutes of Biomedicine and Health, Chinese Academy of Sciences, Guangzhou 510530, China. Electronic address: liu_jinsong@gibh.ac.cn.
          Article
          Publisher Item ID: S0014-5793(14)00481-5
          DOI: 10.1016/j.febslet.2014.05.063
          PubMed ID: 24931377
          SO-VID: 36a34779-fda9-487c-a224-1b889b1a0242
          History

          Keywords: NMR spectroscopy,Bovine pancreatic trypsin inhibitor,Closed/active conformation,Dengue virus,NS2B-NS3 protease
          Data availability:
          Keywords: NMR spectroscopy, Bovine pancreatic trypsin inhibitor, Closed/active conformation, Dengue virus, NS2B-NS3 protease

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