{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,9]],"date-time":"2026-09-09T19:42:34Z","timestamp":1788982954725,"version":"build-2803163510"},"reference-count":34,"publisher":"MDPI AG","issue":"4","license":[{"start":{"date-parts":[[2024,12,23]],"date-time":"2024-12-23T00:00:00Z","timestamp":1734912000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Ministry of Science and Higher Education of the Russian Federation","award":["075-15-2021-1355"],"award-info":[{"award-number":["075-15-2021-1355"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["BioTech"],"abstract":"<jats:p>Heterologous protein expression often faces significant challenges, particularly when the target protein has posttranslational modifications, is toxic, or is prone to misfolding. These issues can result in low expression levels, aggregation, or even cell death. Such problems are exemplified by the expression of phospholipase p37, a critical target for chemotherapeutic drugs against pathogenic human orthopoxviruses, including monkeypox and smallpox viruses. The complex structure and broad enzymatic activity of phospholipase p37 render it toxic to host cells, necessitating specialized strategies for heterologous expression. In our study, we addressed these challenges using the vaccinia virus F13 protein as a model. We demonstrated that p37 can be effectively synthesized in E. coli as a GST fusion protein by co-expressing it with the GroEL\/ES chaperone system and Trigger Factor chaperone.<\/jats:p>","DOI":"10.3390\/biotech13040057","type":"journal-article","created":{"date-parts":[[2024,12,23]],"date-time":"2024-12-23T10:06:52Z","timestamp":1734948412000},"page":"57","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":4,"title":["The Effects of the Combined Co-Expression of GroEL\/ES and Trigger Factor Chaperones on Orthopoxvirus Phospholipase F13 Production in E. coli"],"prefix":"10.3390","volume":"13","author":[{"given":"Iuliia A.","family":"Merkuleva","sequence":"first","affiliation":[{"name":"State Research Center of Virology and Biotechnology VECTOR, Rospotrebnadzor, 630559 Koltsovo, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vladimir N.","family":"Nikitin","sequence":"additional","affiliation":[{"name":"State Research Center of Virology and Biotechnology VECTOR, Rospotrebnadzor, 630559 Koltsovo, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tatyana D.","family":"Belaya","sequence":"additional","affiliation":[{"name":"State Research Center of Virology and Biotechnology VECTOR, Rospotrebnadzor, 630559 Koltsovo, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Egor. A.","family":"Mustaev","sequence":"additional","affiliation":[{"name":"Department of Natural Sciences, Novosibirsk State University, 630090 Novosibirsk, Russia"},{"name":"Synchrotron Radiation Facility\u2014Siberian Circular Photon Source \u201cSKIF\u201d Boreskov Institute of Catalysis of Siberian Branch of the Russian Academy of Sciences, 630559 Koltsovo, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8023-4453","authenticated-orcid":false,"given":"Dmitriy N.","family":"Shcherbakov","sequence":"additional","affiliation":[{"name":"State Research Center of Virology and Biotechnology VECTOR, Rospotrebnadzor, 630559 Koltsovo, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2024,12,23]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"679","DOI":"10.1056\/NEJMoa2207323","article-title":"Monkeypox Virus Infection in Humans across 16 Countries\u2014April\u2013June 2022","volume":"387","author":"Thornhill","year":"2022","journal-title":"N. 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