L. N. Borschevskaya, T. L. Gordeeva, E. B. Pichkur, V. R. Samygina, S. P. Sineoky
{"title":"噬甲酵母 Komagataella phaffii（Pichia pastoris）组装噬菌体 MS2 病毒样颗粒的生物技术潜力","authors":"L. N. Borschevskaya, T. L. Gordeeva, E. B. Pichkur, V. R. Samygina, S. P. Sineoky","doi":"10.1134/S0003683823090028","DOIUrl":null,"url":null,"abstract":"<div><p>Successful assembly of bacteriophage MS2 virus-like particles (VLPs) from a secreted recombinant capsid protein in the culture medium of the <i>Komagataella phaffii</i> methylotrophic yeast has been shown. The yield of VLPs was 5 g/L and reached 30% of the total protein of the culture liquid supernatant. The VLPs were well-ordered icosahedral structures with a diameter of 26‒28 nm, which was confirmed by transmission electron microscopy. A simple method for the isolation and purification of the VLPs was proposed, which ensures the purity of the target protein structures of more than 90%. The results we obtained can be used for development of a technology for the large-scale production of recombinant vaccines based on bacteriophage MS2 VLPs.</p></div>","PeriodicalId":466,"journal":{"name":"Applied Biochemistry and Microbiology","volume":null,"pages":null},"PeriodicalIF":1.0000,"publicationDate":"2024-01-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"The Biotechnological Potential of Methylotrophic Yeast Komagataella phaffii (Pichia pastoris) for Assembly of Bacteriophage MS2 Virus-Like Particles\",\"authors\":\"L. N. Borschevskaya, T. L. Gordeeva, E. B. Pichkur, V. R. Samygina, S. P. Sineoky\",\"doi\":\"10.1134/S0003683823090028\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>Successful assembly of bacteriophage MS2 virus-like particles (VLPs) from a secreted recombinant capsid protein in the culture medium of the <i>Komagataella phaffii</i> methylotrophic yeast has been shown. The yield of VLPs was 5 g/L and reached 30% of the total protein of the culture liquid supernatant. The VLPs were well-ordered icosahedral structures with a diameter of 26‒28 nm, which was confirmed by transmission electron microscopy. A simple method for the isolation and purification of the VLPs was proposed, which ensures the purity of the target protein structures of more than 90%. The results we obtained can be used for development of a technology for the large-scale production of recombinant vaccines based on bacteriophage MS2 VLPs.</p></div>\",\"PeriodicalId\":466,\"journal\":{\"name\":\"Applied Biochemistry and Microbiology\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":1.0000,\"publicationDate\":\"2024-01-12\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Applied Biochemistry and Microbiology\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://link.springer.com/article/10.1134/S0003683823090028\",\"RegionNum\":4,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q4\",\"JCRName\":\"BIOTECHNOLOGY & APPLIED MICROBIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Applied Biochemistry and Microbiology","FirstCategoryId":"99","ListUrlMain":"https://link.springer.com/article/10.1134/S0003683823090028","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"BIOTECHNOLOGY & APPLIED MICROBIOLOGY","Score":null,"Total":0}
The Biotechnological Potential of Methylotrophic Yeast Komagataella phaffii (Pichia pastoris) for Assembly of Bacteriophage MS2 Virus-Like Particles
Successful assembly of bacteriophage MS2 virus-like particles (VLPs) from a secreted recombinant capsid protein in the culture medium of the Komagataella phaffii methylotrophic yeast has been shown. The yield of VLPs was 5 g/L and reached 30% of the total protein of the culture liquid supernatant. The VLPs were well-ordered icosahedral structures with a diameter of 26‒28 nm, which was confirmed by transmission electron microscopy. A simple method for the isolation and purification of the VLPs was proposed, which ensures the purity of the target protein structures of more than 90%. The results we obtained can be used for development of a technology for the large-scale production of recombinant vaccines based on bacteriophage MS2 VLPs.
期刊介绍：
Applied Biochemistry and Microbiology is an international peer reviewed journal that publishes original articles on biochemistry and microbiology that have or may have practical applications. The studies include: enzymes and mechanisms of enzymatic reactions, biosynthesis of low and high molecular physiologically active compounds; the studies of their structure and properties; biogenesis and pathways of their regulation; metabolism of producers of biologically active compounds, biocatalysis in organic synthesis, applied genetics of microorganisms, applied enzymology; protein and metabolic engineering, biochemical bases of phytoimmunity, applied aspects of biochemical and immunochemical analysis; biodegradation of xenobiotics; biosensors; biomedical research (without clinical studies). Along with experimental works, the journal publishes descriptions of novel research techniques and reviews on selected topics.
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