Recombinant alpha-fetoprotein receptor-binding domain co-expression with polyglutamate tags facilitates in vivo folding in E. coli.

Mollaev M., Gorokhovets N., Nikolskaya E., Faustova M., Zabolotsky A., Sokol M., Tereshenko O., Zhunina O., Shvets V., Severin E., Yabbarov N.
Тип документаJournal Article
Дата публикации2018-03-25
Название журналаProtein Expression and Purification
ИздательElsevier
Квартиль по SCImagoQ3
Квартиль по Web of ScienceQ4
Импакт-фактор 20212.03
ISSN10465928, 10960279
Biotechnology
Краткое описание
A wide range of methods are known to increase the prokaryotic intracellular recombinant proteins solubility, for instance, growth at low temperature, supplementation of culture media with "chemical chaperones" (proline, glycine-betaine, and trehalose), co-expression with chaperones or highly soluble fusion partners. As an alternative, we have introduced the polyglutamate tag, which, as it has been shown, increased the protein solubility and facilitated folding. In this study we evaluated the minimal quantity of high density negatively charged EEEEVE amino acid repeats (pGlu) necessary to switch the recombinant receptor-binding domain of human alpha-fetoprotein (rbdAFP) expression almost entirely from the inclusion bodies to the soluble cytoplasmic fraction in E. coli. For this purpose, genetic constructs based on pET vectors coding rbdAFP and containing from 1 to 4 additional EEEEVE repeats at the C-terminus have been prepared. It was found that 3 pGlu repeats is the minimal number, that leads to a complete shift of the expression to the soluble cytoplasmic fraction in E. coli SHuffle Express T7 while 4 repeats were required for that in E. coli BL21(DE3). The rbdAFP contained 4 pGlu repeats was purified making use of ion-exchange chromatography and characterized by circular dichroism and ability to bind and accumulate in AFP receptor positive cancer cells in order to check for the structural and specific activity alterations related to the additional polyanionic sequence introduction.
Пристатейные ссылки: 29
Цитируется в публикациях: 4
Magnetic electrochemiluminescent immunoassay with quantum dots label for highly efficient detection of the tumor marker α-fetoprotein
Huang Z., Han W., Wu Y., Hu X., Yuan Y., Chen W., Peng H., Liu A., Lin X.
Q1 Journal of Electroanalytical Chemistry 2017 цитирований: 17
The alpha-fetoprotein third domain receptor binding fragment: in search of scavenger and associated receptor targets
Mizejewski G.J.
Q1 Journal of Drug Targeting 2015 цитирований: 12
Prokaryotic Soluble Overexpression and Purification of Bioactive Human Growth Hormone by Fusion to Thioredoxin, Maltose Binding Protein, and Protein Disulfide Isomerase
Nguyen M.T., Koo B., Thi Vu T.T., Song J., Chong S., Jeong B., Ryu H., Moh S., Choe H.
Q1 PLoS ONE 2014 цитирований: 33
Open Access
Open access
Targeted delivery of doxorubicin: Drug delivery system based on PAMAM dendrimers
Yabbarov N.G., Posypanova G.A., Vorontsov E.A., Popova O.N., Severin E.S.
Q2 Biochemistry (Moscow) 2013 цитирований: 22
A new system for targeted delivery of doxorubicin into tumor cells.
Yabbarov N.G., Posypanova G.A., Vorontsov E.A., Obydenny S.I., Severin E.S.
Q1 Journal of Controlled Release 2013 цитирований: 42
A reference dataset for the analyses of membrane protein secondary structures and transmembrane residues using circular dichroism spectroscopy
Abdul-Gader A., Miles A.J., Wallace B.A.
Q1 Bioinformatics 2011 цитирований: 102
Review of the putative cell-surface receptors for alpha-fetoprotein: identification of a candidate receptor protein family
Mizejewski G.J.
Q2 Tumor Biology 2010 цитирований: 27
Open Access
Open access
High-efficient expression, refolding and purification of functional recombinant C-terminal fragment of human alpha-fetoprotein.
Sharapova O.A., Pozdnykova N.V., Laurinavichyute D.K., Yurkova M.S., Posypanova G.A., Fedorov A.N., Severin S.E., Severin E.S.
Q3 Protein Expression and Purification 2010 цитирований: 8
Separation of blood leucocytes, granulocytes and lymphocytes.
Bøyum A.
Tissue Antigens 2008 цитирований: 482
Protein secondary structure analyses from circular dichroism spectroscopy: methods and reference databases.
Whitmore L., Wallace B.A.
Q2 Biopolymers 2008 цитирований: 1670
Recombinant alpha-fetoprotein C-terminal fragment: The new recombinant vector for targeted delivery
Posypanova G.A., Gorokhovets N.V., Makarov V.A., Savvateeva L.V., Kireeva N.N., Severin S.E., Severin E.S.
Q1 Journal of Drug Targeting 2008 цитирований: 24
Enhancement of soluble protein expression through the use of fusion tags.
Esposito D., Chatterjee D.K.
Q1 Current Opinion in Biotechnology 2006 цитирований: 377
Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli
Sørensen H., Mortensen K.
Q1 Microbial Cell Factories 2005 цитирований: 452
Open Access
Open access
The solubility and stability of recombinant proteins are increased by their fusion to NusA.
De Marco V., Stier G., Blandin S., de Marco A.
Q1 Biochemical and Biophysical Research Communications 2004 цитирований: 104
Biological role of α-fetoprotein in cancer: prospects for anticancer therapy
Mizejewski G.J.
Q2 Expert Review of Anticancer Therapy 2002 цитирований: 75
Метрики
Поделиться
Цитировать
ГОСТ |
Цитировать
1. Mollaev M. и др. Recombinant alpha-fetoprotein receptor-binding domain co-expression with polyglutamate tags facilitates in vivo folding in E. coli // Protein Expression and Purification. 2018. Т. 143. С. 77–82.
RIS |
Цитировать

TY - JOUR

DO - 10.1016/j.pep.2017.11.001

UR - http://dx.doi.org/10.1016/j.pep.2017.11.001

TI - Recombinant alpha-fetoprotein receptor-binding domain co-expression with polyglutamate tags facilitates in vivo folding in E. coli

T2 - Protein Expression and Purification

AU - Mollaev, Murad

AU - Gorokhovets, Neonila

AU - Nikolskaya, Elena

AU - Faustova, Maria

AU - Zabolotsky, Arthur

AU - Sokol, Maria

AU - Tereshenko, Oksana

AU - Zhunina, Olga

AU - Shvets, Vitaliy

AU - Severin, Evgeniy

AU - Yabbarov, Nikita

PY - 2018

DA - 2018/03

PB - Elsevier BV

SP - 77-82

VL - 143

SN - 1046-5928

ER -

BibTex |
Цитировать

@article{Mollaev_2018,

doi = {10.1016/j.pep.2017.11.001},

url = {https://doi.org/10.1016%2Fj.pep.2017.11.001},

year = 2018,

month = {mar},

publisher = {Elsevier {BV}},

volume = {143},

pages = {77--82},

author = {Murad Mollaev and Neonila Gorokhovets and Elena Nikolskaya and Maria Faustova and Arthur Zabolotsky and Maria Sokol and Oksana Tereshenko and Olga Zhunina and Vitaliy Shvets and Evgeniy Severin and Nikita Yabbarov},

title = {Recombinant alpha-fetoprotein receptor-binding domain co-expression with polyglutamate tags facilitates in vivo folding in E. coli},

journal = {Protein Expression and Purification}

}

MLA
Цитировать
Mollaev, Murad, et al. “Recombinant Alpha-Fetoprotein Receptor-Binding Domain Co-Expression with Polyglutamate Tags Facilitates in Vivo Folding in E. Coli.” Protein Expression and Purification, vol. 143, Mar. 2018, pp. 77–82. Crossref, https://doi.org/10.1016/j.pep.2017.11.001.