The Effects of the Combined Co-Expression of GroEL/ES and Trigger Factor Chaperones on Orthopoxvirus Phospholipase F13 Production in E. coli

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The Effects of the Combined Co-Expression of GroEL/ES and Trigger Factor Chaperones on Orthopoxvirus Phospholipase F13 Production in E. coli. / Merkuleva, Iuliia A.; Nikitin, Vladimir N.; Belaya, Tatyana D. et al.

In: BioTech, Vol. 13, No. 4, 57, 20.12.2024.

Research output: Contribution to journal › Article › peer-review

BibTeX

@article{2591d7a34fa6433ba5852f36f662e87b,

title = "The Effects of the Combined Co-Expression of GroEL/ES and Trigger Factor Chaperones on Orthopoxvirus Phospholipase F13 Production in E. coli",

abstract = "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.",

keywords = "GroEL/ES, NIOCH-14, ST-246, chaperone, monkeypox virus, orthopoxviruses, p37, phospholipase F13, trigger factor, chaperone, GroEL/ES, monkeypox virus, NIOCH-14, orthopoxviruses, p37, phospholipase F13, ST-246, trigger factor",

author = "Merkuleva, {Iuliia A.} and Nikitin, {Vladimir N.} and Belaya, {Tatyana D.} and Mustaev, {Egor A.} and Shcherbakov, {Dmitriy N.}",

note = "Финансирование: Ministry of Education and Science of the Russian Federation 075-15-2021-1355",

year = "2024",

month = dec,

day = "20",

doi = "10.3390/biotech13040057",

language = "English",

volume = "13",

journal = "BioTech",

issn = "2673-6284",

number = "4",

}

RIS

TY - JOUR

T1 - The Effects of the Combined Co-Expression of GroEL/ES and Trigger Factor Chaperones on Orthopoxvirus Phospholipase F13 Production in E. coli

AU - Merkuleva, Iuliia A.

AU - Nikitin, Vladimir N.

AU - Belaya, Tatyana D.

AU - Mustaev, Egor A.

AU - Shcherbakov, Dmitriy N.

N1 - Финансирование: Ministry of Education and Science of the Russian Federation 075-15-2021-1355

PY - 2024/12/20

Y1 - 2024/12/20

N2 - 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.

AB - 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.

KW - GroEL/ES

KW - NIOCH-14

KW - ST-246

KW - chaperone

KW - monkeypox virus

KW - orthopoxviruses

KW - p37

KW - phospholipase F13

KW - trigger factor

KW - chaperone

KW - GroEL/ES

KW - monkeypox virus

KW - NIOCH-14

KW - orthopoxviruses

KW - p37

KW - phospholipase F13

KW - ST-246

KW - trigger factor

UR - https://www.mendeley.com/catalogue/e6cbbee0-d1f8-3e74-a39a-f3a9ea8bbdd3/

UR - https://www.scopus.com/record/display.uri?eid=2-s2.0-85213024144&origin=inward&txGid=f0f246fcf6725ace46bc1f1345e80bef

U2 - 10.3390/biotech13040057

DO - 10.3390/biotech13040057

M3 - Article

C2 - 39727494

VL - 13

JO - BioTech

JF - BioTech

SN - 2673-6284

IS - 4

M1 - 57

ER -

ID: 61415709