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Интеллектуальная Система Тематического Исследования НАукометрических данных |
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Amyloids are highly widespread at the surface of microorganisms, including cell wall (CW) of Candida albicans /Otoo et al., 2008/. The investigation of these proteins is of special importance for understanding of their potential to cause pathogenic process, particularly by originating the “seeds” of amyloid deposits in macroorganisms. The properties of amyloid proteins of Saccharomyces cerevisiae CW are studied insufficiently. The goal of our work was to investigate the ability of SEP (SDS\β-mercaptoethanol extractable proteins) of S. cerevisiae CW to form amyloid-like fibrils. Methods: Bioinformatic analysis, western blotting, сircular dichroism, fluorescence spectroscopy, electron and fluorescent microscopy were used. Proteinase-treatment and Thioflavin T (ThT)-test were used for revealing the presence of amyloids. Results: ThT-binding SEPs, Bgl2 and Exg1 among them, were discovered in S.cerevisiae CW. Bgl2 is the only ThT-binding SEP that could not be released from CW by sequential SDS and proteinase treatment. Its attachment to the CW did not involve disulfide bonds. We have revealed seven amyloidogenic determinants in Bgl2 molecule. We indicated the presence of beta-sheet structures in Bgl2 isolates. Bgl2 formed fibrils with different morphology, the process being enforced by other CW components. In the absence of Bgl2 in Δbgl, the increasing of other CW ThT-binding SEPs was detected /Kalebina et al., 2008; Gorkovsky et al., 2009; Bezsonov et al., 2010; Bezsonov et al., 2013/. Conclusions: The data obtained give the strong evidence for existence of proteins with amyloid-like properties among S.crevisiae CW SEPs. The most pronounced amyloids properties were described for conserved protein Bgl2.