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Molecular Cloning, Expression, Purification and Functional Characterization of an Antifungal Cyclophilin Protein from

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Journal Biomed Rep
Specialty Biochemistry
Date 2017 Dec 1
PMID 29188056
Citations 5
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Abstract

Cyclophilins (CyPs), a member of peptidyl-prolyl isomerases (PPIases), are ubiquitously distributed in organisms such as bacteria, yeast, plants and animals. CyPs have diverse biological functions, with some exhibiting antifungal and antiviral activities. In this study, cyclophilin (), a novel gene encoding an antifungal protein from , was cloned, and its protein product was expressed in , and then fractionated by affinity chromatography. The open reading frame of the full-length coding sequence was found to encode a single-domain CyP-like protein of 174 amino residues with a calculated molecular weight of 18.7 kDa. The pGEX system was used to express pgCyP fused to glutathione S-transferase. After affinity purification, the protein showed a strong fungal resistance effect on . In addition, pgCyP showed high PPIase activity. To the best of our knowledge, the present study is the first successful effort to clone and characterize a CyP-like protein gene from .

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