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2017 | 64 | 1 | 21-24
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Trypsin-specific Inhibitors from the Macrolepiota procera, Armillaria mellea and Amanita phalloides wild mushrooms

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Wild growing mushrooms are a rich source of novel proteins with unique features. We have isolated and characterized trypsin inhibitors from two edible mushrooms, the honey fungus (Armillaria mellea) and the parasol mushroom (Macrolepiota procera), and from the poisonous death cap (Amanita phalloides). The trypsin inhibitors isolated: armespin, macrospin and amphaspin, have similar molecular masses, acidic isoelectric points and are not N-glycosylated. They are very strong trypsin inhibitors and weak chymotrypsin inhibitors. They are resistant to exposure to high temperatures and withstand extreme pH values. These exceptional characteristics are advantageous for their potential use in biotechnology, agriculture and medicine.
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  • Department of Biotechnology, Jožef Stefan Institute, SI1000 Ljubljana, Slovenia
  • Department of Biotechnology, Jožef Stefan Institute, SI1000 Ljubljana, Slovenia
  • Department of Biotechnology, Jožef Stefan Institute, SI1000 Ljubljana, Slovenia
  • Department of Pharmaceutical Biology, Faculty of Pharmacy, University of Ljubljana, SI1000 Lubljana, Slovenia
  • Department of Biotechnology, Jožef Stefan Institute, SI1000 Ljubljana, Slovenia
  • Ali PP, Sapna K, Mol KR, Bhat SG, Chandrasekaran M, Elyas KK (2014) Trypsin inhibitor from edible mushroom Pleurotus floridanus active against proteases of microbial origin. Appl Biochem Biotechnol 173: 167-178. doi: 10.1007/s12010-014-0826-1.
  • Avanzo Caglič P, Renko M, Turk D, Kos J, Sabotič J (2014) Fungal β-trefoil trypsin inhibitors cnispin and cospin demonstrate the plasticity of the β-trefoil fold. Biochim Biophys Acta 1844: 1749-1756. doi: 10.1016/j.bbapap.2014.07.004.
  • Avanzo P, Sabotič J, Anžlovar S, Popovič T, Leonardi A, Pain RH, Kos J, Brzin J (2009) Trypsin-specific inhibitors from the basidiomycete Clitocybe nebularis with regulatory and defensive functions. Microbiology 155: 3971-3981. doi: 10.1099/mic.0.032805-0.
  • Barros L, Cruz T, Baptista P, Estevinho LM, Ferreira IC (2008) Wild and commercial mushrooms as source of nutrients and nutraceuticals. Food Chem Toxicol 46: 2742-2747. doi: 10.1016/j.fct.2008.04.030.
  • Brzin J, Rogelj B, Popovič T, Štrukelj B, Ritonja A (2000) Clitocypin, a new type of cysteine proteinase inhibitor from fruit bodies of mushroom Clitocybe nebularis. J Biol Chem 275: 20104-20109. doi: 10.1074/jbc.M001392200.
  • Dubovenko AG, Dunaevsky YE, Belozersky MA, Oppert B, Lord JC, Elpidina EN (2010) Trypsin-like proteins of the fungi as possible markers of pathogenicity. Fungal Biol 114: 151-159. doi: 10.1016/j.funbio.2009.11.004.
  • Dunaevsky YE, Popova VV, Semenova TA, Beliakova GA, Belozersky MA (2014) Fungal inhibitors of proteolytic enzymes: Classification, properties, possible biological roles, and perspectives for practical use. Biochimie 101: 10-20. doi: 10.1016/j.biochi.2013.12.007.
  • Erjavec J, Kos J, Ravnikar M, Dreo T, Sabotič J (2012) Proteins of higher fungi--from forest to application. Trends Biotechnol 30: 259-273. doi: 10.1016/j.tibtech.2012.01.004.
  • Gosavi S, Whitford PC, Jennings PA, Onuchic JN (2008) Extracting function from a beta-trefoil folding motif. Proc Natl Acad Sci U S A 105: 10384-10389. doi: 10.1073/pnas.0801343105.
  • Gzogian LA, Proskuriakov MT, Ievleva EV, Valueva TA (2005) Trypsin-like proteinases and trypsin inhibitors in fruiting bodies of higher fungi. Prikl Biokhim Mikrobiol 41: 612-615.
  • Henderson PJ (1972) A linear equation that describes steady-state kinetics of enzymes and subcellular particles interacting with tightly bound inhibitors. Biochem J 127: 321-333. doi: 10.1042/bj1270321.
  • Kalač P (2009) Chemical composition and nutritional value of European species of wild growing mushrooms: A review. Food Chem 113: 9-16. doi: 10.1016/j.foodchem.2008.07.077
  • Kidrič M, Fabian H, Brzin J, Popovič T, Pain RH (2002) Folding, stability, and secondary structure of a new dimeric cysteine proteinase inhibitor. Biochem Biophys Res Commun 297: 962-967. doi: 10.1016/S0006-291x(02)02328-8.
  • Odani S, Tominaga K, Kondou S, Hori H, Koide T, Hara S, Isemura M, Tsunasawa S (1999) The inhibitory properties and primary structure of a novel serine proteinase inhibitor from the fruiting body of the basidiomycete, Lentinus edodes. Eur J Biochem 262: 915-923. doi: 10.1046/j.1432-1327.1999.00463.x.
  • Renko M, Sabotič J, Mihelič M, Brzin J, Kos J, Turk D (2010) Versatile loops in mycocypins inhibit three protease families. J Biol Chem 285: 308-316. doi: 10.1074/jbc.M109.043331.
  • Renko M, Sabotič J, Turk D (2012) β-trefoil inhibitors - from the work of Kunitz onward. Biol Chem 393: 1043–1054. doi: 10.1515/hsz-2012-0159.
  • Sabotič J, Bleuler-Martinez S, Renko M, Avanzo Caglič P, Kallert S, Štrukelj B, Turk D, Aebi M, Kos J, Künzler M (2012) Structural basis of trypsin inhibition and entomotoxicity of cospin, serine protease inhibitor involved in defense of Coprinopsis cinerea fruiting bodies. J Biol Chem 287: 3898-3907. doi: 10.1074/jbc.M111.285304.
  • Sabotič J, Galeša K, Popovič T, Leonardi A, Brzin J (2007) Comparison of natural and recombinant clitocypins, the fungal cysteine protease inhibitors. Protein Expr Purif 53: 104-111. doi: 10.1016/j.pep.2006.11.015.
  • Sabotič J, Kos J (2012) Microbial and fungal protease inhibitors - current and potential applications. Appl Microbiol Biotechnol 93: 1351–1375. doi: 10.1007/s00253-011-3834-x.
  • Sabotič J, Popovič T, Puizdar V, Brzin J (2009) Macrocypins, a family of cysteine protease inhibitors from the basidiomycete Macrolepiota procera. FEBS J 276: 4334-4345. doi: 10.1111/j.1742-4658.2009.07138.x.
  • St Leger RJ, Joshi L, Roberts DW (1997) Adaptation of proteases and carbohydrates of saprophytic, phytopathogenic and entomopathogenic fungi to the requirements of their ecological niches. Microbiology 143: 1983-1992. doi: 10.1099/00221287-143-6-1983.
  • Vetter J (2000) Trypsin inhibitory activity of basidiomycetous mushrooms. Eur Food Res Technol 211: 346-348. doi: 10.1007/s002170000180
  • Žurga S, Pohleven J, Renko M, Bleuler-Martinez S, Sosnowski P, Turk D, Künzler M, Kos J, Sabotič J (2014) A novel β-trefoil lectin from the parasol mushroom (Macrolepiota procera) is nematotoxic. FEBS J 281: 3489-3506. doi: 10.1111/febs.12875.
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