Application of genetically modified microorganisms for potential human amyloids search
- Авторы: Ryabinina M.V.1, Zelinsky A.A.1, Rubel A.A.1
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Учреждения:
- Saint Petersburg State University
- Выпуск: Том 20 (2022): Спецвыпуск
- Страницы: 52-52
- Раздел: «ГМО: ИСТОРИЯ, ДОСТИЖЕНИЯ, СОЦИАЛЬНЫЕ И ЭКОЛОГИЧЕСКИЕ РИСКИ»
- URL: https://journals.eco-vector.com/ecolgenet/article/view/112346
- DOI: https://doi.org/10.17816/ecogen112346
- ID: 112346
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Аннотация
Amyloids are fibrous protein structures often found in patients with severe diseases, such as Alzheimer’s, Parkinson’s diseases etc. A number of studies have shown that the production of heterologous amyloidogenic proteins in Saccharomyces cerevisiae strains results in formation of amyloid aggregates with properties similar to those found in mammals.
Amyloid aggregates formed in yeasts usually do not have their own phenotypic manifestation. To assess amyloidogenic potential of individual proteins a yeast test-system was developed under supervision of Prof. Y.O. Chernoff. The system is based on usage of genetically modified S. cerevisiae cells auxotrophic for certain growth factors, allowing effective phenotypic selection to search for amyloidogenic proteins within proteomes of various organisms [1]. Using this test-system, our laboratory evaluated amyloid potential of a spectrum of human proteins, the amyloidogenicity of which was previously predicted by bioinformatics algorithms. The proteins that have shown amyloidogenic potential in yeast-based model are being currently tested in vitro and in vivo. Some mutant Escherichia coli strains can be applied for studying propensity of heterologous proteins to form amyloids in vitro. Thus, application of genetically modified microorganisms makes it possible to identify new human amyloidogenic proteins and to improve predictive ability of bioinformatics algorithms.
The research is supported by RSF grant №20-14-00148 and by St. Petersburg State University (project No. 93025998). Authors acknowledge SPbSU Resource Centers “Chromas”, “Molecular and Cell Technologies” and “Biobank”.
Полный текст
Amyloids are fibrous protein structures often found in patients with severe diseases, such as Alzheimer’s, Parkinson’s diseases etc. A number of studies have shown that the production of heterologous amyloidogenic proteins in Saccharomyces cerevisiae strains results in formation of amyloid aggregates with properties similar to those found in mammals.
Amyloid aggregates formed in yeasts usually do not have their own phenotypic manifestation. To assess amyloidogenic potential of individual proteins a yeast test-system was developed under supervision of Prof. Y.O. Chernoff. The system is based on usage of genetically modified S. cerevisiae cells auxotrophic for certain growth factors, allowing effective phenotypic selection to search for amyloidogenic proteins within proteomes of various organisms [1]. Using this test-system, our laboratory evaluated amyloid potential of a spectrum of human proteins, the amyloidogenicity of which was previously predicted by bioinformatics algorithms. The proteins that have shown amyloidogenic potential in yeast-based model are being currently tested in vitro and in vivo. Some mutant Escherichia coli strains can be applied for studying propensity of heterologous proteins to form amyloids in vitro. Thus, application of genetically modified microorganisms makes it possible to identify new human amyloidogenic proteins and to improve predictive ability of bioinformatics algorithms.
The research is supported by RSF grant №20-14-00148 and by St. Petersburg State University (project No. 93025998). Authors acknowledge SPbSU Resource Centers “Chromas”, “Molecular and Cell Technologies” and “Biobank”.
Об авторах
Marina Ryabinina
Saint Petersburg State University
Автор, ответственный за переписку.
Email: marina.v1205@gmail.com
B.Sci. (Biology), Laboratory Assistant, Laboratory of Amyloid Biology
Россия, Saint PetersburgAndrew Zelinsky
Saint Petersburg State University
Email: andrew_zelinsky@mail.ru
M.Sci. (Biology), Researcher, Laboratory of Amyloid Biology
Россия, Saint PetersburgAleksandr Rubel
Saint Petersburg State University
Email: arubel@mail.ru
SPIN-код: 3961-4690
PhD, The Head of the Laboratory, Laboratory of Amyloid Biology
Россия, Saint PetersburgСписок литературы
- Chandramowlishwaran P, Sun, Casey K, et al. Mammalian amyloidogenic proteins promote prion nucleation in yeast. J Biol Chem. 2018;293(9):3436–3450. doi: 10.1074/jbc.M117.809004