Applied Microbiology and Biotechnology

, Volume 72, Issue 6, pp 1185–1191 | Cite as

A hemolysin from the mushroom Pleurotus eryngii

  • Patrick H. K. NgaiEmail author
  • T. B. Ng
Biotechnologically Relevant Enzymes and Proteins


A monomeric 17-kDa hemolysin designated as eryngeolysin was isolated from fresh fruiting bodies of the mushroom Pleurotus eryngii, using a protocol that involved gel filtration on Superdex 75, ion exchange chromatography on Mono Q and gel filtration on Superdex 75. Its N-terminal sequence demonstrated striking homology to that of its counterparts ostreolysin from the oyster mushroom Pleurotus ostreatus and aegerolysin from the mushroom Agrocybe cylindracea. Its hemolytic activity was unaffected over the pH range 4.0–12.0, but no activity was observed at pH 13 and at and below pH 2. The hemolysin was stable between 0 and 30 °C. At 40 °C, only residual activity was detectable. At and above 50 °C, activity was indiscernible. Eryngeolysin exhibited cytotoxicity toward leukemia (L1210) cells but not toward fungi. The hemolysin was inactivated by treatment with trypsin. It exhibited antibacterial activity against Bacillus sp. but not against other species. It inhibited basal as well as ConA-stimulated mitogenic response of murine splenocytes. N-Glycolyneuraminic acid was the only sugar capable of inhibiting the hemolytic activity. Eryngeolysin-induced hemolysis was osmotically protected by polyethylene glycol (PEG) 10000 with a mean hydrated diameter dose to 9.3 nm. However, no protection was offered by PEG 10000 to the anti-mitogenic and antiproliferative activities of eryngeolysin. The susceptibility of erythrocytes from different classes of vertebrates to eryngeolysin was mammalian > avian > reptilian > piscine.


Fruiting Body Fast Protein Liquid Chromatography Rabbit Erythrocyte Mouse Splenocytes Pleurotus Eryngii 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.



The skilled secretarial assistance of Miss Fion Yung is appreciated.


  1. Berne S, Krizaj I, Pohleven F, Tuck T, Macek P, Sepcic K (2002) Pleurotus and Agrocybe hemolysins, new proteins hypothetically improved in fungal fruiting. Biochim Biophys Acta 1570:153–159Google Scholar
  2. Fuji Y, Nomura T, Yokoyama R, Shinoda S, Okamoto K (2003) Studies of the mechanism of action of the aerolysin-like hemolysis of Aeromonas sobria in stimulating T84 cells to produce cyclic AMP. Infect Immun 71:1557–1560CrossRefGoogle Scholar
  3. Giardina P, Palmieri G, Scaloni A, Fontanella B, Faraco V, Cennamo G, Sannia G (1999) Protein and gene structure of a blue laccase from Pleurotus ostreatus. Biochem J 341:655–663CrossRefGoogle Scholar
  4. Han JH, Lee JH, Choi YH, Park JH, Choi TJ, Kong IS (2002) Purification, characterization and molecular cloning of Vibrio fluvialis hemolysin. Biochim Biophys Acta 1599:106–114Google Scholar
  5. Kudo Y, Fukuchi Y, Kumagai T, Ebina K, Yokota K (2001) Oxidized low-density lipoprotein-binding specificity of Asp-hemolysin from Aspergillus fumigatus. Biochim Biophys Acta 1568:183–188Google Scholar
  6. Laemmli UK, Favre M (1973) Gel electrophoresis of proteins. J Mol Biol 80:575–599CrossRefGoogle Scholar
  7. Lam SK, Ng TB (2001) First stimultaneous isolation of a ribosome inactivating protein and an antifungal protein from a mushroom (Lyophyllum shimeiji) together with evidence for synergism of their antifungal effects. Arch Biochem Biophys 393:271–280CrossRefGoogle Scholar
  8. Raimondi F, Kao JP, Fiorentini C, Fabbori A, Donelli G, Gaspanni N, Rubino A, Fasano A (2000) Enterotoxicity and cytotoxicity of Vibrio parahemolyticus thermostable direct hemolysin in in vitro systems. Infect Immun 68:3180–3185CrossRefGoogle Scholar
  9. Sakaguchi O, Shimade H, Yokota K (1975) Purification and some characteristics of hemolytic toxin from Aspergillus fumigatus. Jpn J Med Sci Biol 28:328–331Google Scholar
  10. Wang HX, Ng TB, Liu WK, Ooi VEC, Chang ST (1996) Isolation and characterization of two distinct lectins with antiproliferative activity from the cultured mycelia of the mushroom Tricholoma mongolicum. Int J Pept Protein Res 46:508–513CrossRefGoogle Scholar

Copyright information

© Springer-Verlag 2006

Authors and Affiliations

  1. 1.Department of Biochemistry, Faculty of MedicineChinese University of Hong KongNew TerritoriesChina

Personalised recommendations