| Autor: |
Sulatsky MI; Institute of Cytology, Russian Academy of Sciences, 194064 St. Petersburg, Russia., Belousov MV; All-Russia Research Institute for Agricultural Microbiology, 196608 St. Petersburg, Russia.; Faculty of Biology, St. Petersburg State University, 199034 St. Petersburg, Russia., Kosolapova AO; All-Russia Research Institute for Agricultural Microbiology, 196608 St. Petersburg, Russia.; Faculty of Biology, St. Petersburg State University, 199034 St. Petersburg, Russia., Mikhailova EV; Institute of Cytology, Russian Academy of Sciences, 194064 St. Petersburg, Russia., Romanenko MN; All-Russia Research Institute for Agricultural Microbiology, 196608 St. Petersburg, Russia.; Faculty of Biology, St. Petersburg State University, 199034 St. Petersburg, Russia., Antonets KS; All-Russia Research Institute for Agricultural Microbiology, 196608 St. Petersburg, Russia.; Faculty of Biology, St. Petersburg State University, 199034 St. Petersburg, Russia., Kuznetsova IM; Institute of Cytology, Russian Academy of Sciences, 194064 St. Petersburg, Russia., Turoverov KK; Institute of Cytology, Russian Academy of Sciences, 194064 St. Petersburg, Russia., Nizhnikov AA; All-Russia Research Institute for Agricultural Microbiology, 196608 St. Petersburg, Russia.; Faculty of Biology, St. Petersburg State University, 199034 St. Petersburg, Russia., Sulatskaya AI; Institute of Cytology, Russian Academy of Sciences, 194064 St. Petersburg, Russia. |
| Abstrakt: |
Although incurable pathologies associated with the formation of highly ordered fibrillar protein aggregates called amyloids have been known for about two centuries, functional roles of amyloids have been studied for only two decades. Recently, we identified functional amyloids in plants. These amyloids formed using garden pea Pisum sativum L. storage globulin and vicilin, accumulated during the seed maturation and resisted treatment with gastric enzymes and canning. Thus, vicilin amyloids ingested with food could interact with mammalian proteins. In this work, we analyzed the effects of vicilin amyloids on the fibril formation of proteins that form pathological amyloids. We found that vicilin amyloids inhibit the fibrillogenesis of these proteins. In particular, vicilin amyloids decrease the number and length of lysozyme amyloid fibrils; the length and width of β-2-microglobulin fibrils; the number, length and the degree of clustering of β-amyloid fibrils; and, finally, they change the structure and decrease the length of insulin fibrils. Such drastic influences of vicilin amyloids on the pathological amyloids' formation cause the alteration of their toxicity for mammalian cells, which decreases for all tested amyloids with the exception of insulin. Taken together, our study, for the first time, demonstrates the anti-amyloid effect of vicilin fibrils and suggests the mechanisms underlying this phenomenon. |
