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Bldesin, the first functionally characterized pathogenic fungus defensin with Kv1.3 channel and chymotrypsin inhibitory activities
Author(s) -
Luo Xudong,
Zhu Wen,
Ding Li,
Ye Xiangdong,
Gao Huanhuan,
Tai Xuejiao,
Wu Zheng,
Qian Yi,
Ruan Xuzhi,
Li Jian,
Li Shan,
Chen Zongyun
Publication year - 2019
Publication title -
journal of biochemical and molecular toxicology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.526
H-Index - 58
eISSN - 1099-0461
pISSN - 1095-6670
DOI - 10.1002/jbt.22244
Subject(s) - defensin , serine protease , protease , antimicrobial peptides , antimicrobial , biochemistry , microbiology and biotechnology , proteases , peptide , chymotrypsin , inhibitory postsynaptic potential , chemistry , biology , enzyme , trypsin , neuroscience
Fungus defensin is a kind of important natural peptide resource, such as plectasin from the soil fungus Pseudoplectania nigrella with potential application in the antimicrobial peptide lead drug discovery. Here, a fungus defensin named Bldesin with Kv1.3 channel and serine protease inhibitory activities was first explored. By GST‐Bldesin fusion expression and enterokinase cleaving strategy, recombinant Bldesin was obtained successfully. Antimicrobial assays showed that Bldesin had potent activity against Gram‐positive Staphylococcus aureus , but had no effect on Gram‐negative Escherichia coli . Electrophysiological experiments showed that Bldesin had Kv1.3 channel inhibitory activity. Serine protease inhibitory associated experiments showed that Bldesin had unique chymotrypsin protease inhibitory, elastase protease inhibitory, and serine protease‐associated coagulation inhibitory activities. To the best of our knowledge, Bldesin is the first functionally characterized pathogenic fungus defensin with Kv1.3 channel and chymotrypsin inhibitory activities and highlighted novel pharmacological effects of fungus‐derived defensin peptides.