doi:10.1016/j.peptides.2003.11.014
Copyright © 2004 Elsevier Inc. All rights reserved.
Eryngin, a novel antifungal peptide from fruiting bodies of the edible mushroom Pleurotus eryngii
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Hexiang Wang a, b and T. B. Ng 
, 
, c
a Department of Microbiology, College of Biological Science, China Agricultural University, Beijing, China
b State Key Laboratory of Agrobiotechnology, Beijing, China
c Department of Biochemistry, Faculty of Medicine, The Chinese University of Hong Kong, Shatin, New Territories, Hong Kong, China
Received 21 July 2003;
accepted 25 November 2003.
Available online 31 January 2004.
Abstract
An antifungal peptide with a molecular mass of 10 kDa was isolated from fruiting bodies of the mushroom Pleurotus eryngii. The peptide, designated as eryngin, inhibited mycelial growth in Fusarium oxysporum and Mycosphaerella arachidicola. It was unadsorbed on DEAE-cellulose and adsorbed on Affi-gel blue gel and S-Sepharose. Its N-terminal sequence demonstrated some similarity to the antifungal protein from the mushroom Lyophyllum shimeiji and little resemblance to thaumatin and thaumatin-like proteins.
Author Keywords: Author Keywords: Mushroom; Antifungal peptide; Fruiting bodies
Fig. 1. Ion exchange chromatography on an S-Sepharose column (1.5 cm×15 cm). Sample: fraction of fruiting body extract unadsorbed on DEAE-cellulose and subsequently adsorbed on Affi-gel blue gel. Buffer: 10 mM NH4OAc (pH 4.6). Slanting dotted line across the chromatogram indicates linear NaCl concentration gradient (0–1 M) employed to elute the adsorbed fractions S2 and S3.
Fig. 2. Gel filtration on a Superdex HR 10/30 column by fast protein liquid chromatograpy. Sample: fraction S3 from S-Sepharose column chromatography. Buffer: 0.2 M NH4HCO3 (pH 8.5). Flow rate: 0.4 ml/min. Fraction size: 0.8 ml.
Fig. 3. Sodium dodecyl sulfate–polyacrylamide gel electrophoresis of fraction SU2 from Superdex 75 column chromatography. Right lane: SU2 (12 μg). Left lane: molecular mass markers from Amersham Biosciences. From top downward: phosphorylase b (94 kDa), bovine serum albumin (67 kDa), ovalbumin (43 kDa), carbonic anhydrase (30 kDa), soybean trypsin inhibitor (20 kDa) and α-lactalbmin (14.4 kDa).
Fig. 4. Antifungal activity of eryngin toward Fusarium oxysporum: (A) control (12 μl 0.1-M MES buffer pH 6.5), (B) 72 μg eryngin in 12 μl MES buffer, (C) 14.4 μg eryngin in 12 μl MES buffer.
Fig. 5. Antifungal activity of eryngin toward Mycosphaerella arachidicola: (A) control (12 μl 0.1-M MES buffer, pH 6.5), (B) 72 μg eryngin in 12 μl MES buffer, (C) 14.4 μg eryngin in 12 μl MES buffer.
Table 1. Comparison of N-terminal sequences of eryngin, Lyophyllum antifungal protein, thaumatin-like proteins and thaumatin
(··): space created to maximize sequence similarity.
Identical corresponding amino acid residues are underlined.
Corresponding author. Tel.: +852-2609-6872; fax: +852-2603-5123.
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