A Leucine Zipper Dimerization Strategy to Generate Soluble T Cell Receptors Using the <i<Escherichia coli</i< Expression System

T cell-mediated adaptive immunity plays a key role in immunological surveillance and host control of infectious diseases. A better understanding of T cell receptor (TCR) recognition of pathogen-derived epitopes or cancer-associated neoantigens is the basis for developing T cell-based vaccines and im...
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Autor*in:	Angela Zhang [verfasserIn] Alicja Piechocka-Trocha [verfasserIn] Xiaolong Li [verfasserIn] Bruce D. Walker [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2022

Schlagwörter:	T cell receptor protein engineering leucine zipper refolding purification

Übergeordnetes Werk:	In: Cells - MDPI AG, 2012, 11(2022), 3, p 312
Übergeordnetes Werk:	volume:11 ; year:2022 ; number:3, p 312

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.3390/cells11030312

Katalog-ID:	DOAJ047355972

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allfieldsSound	10.3390/cells11030312 doi (DE-627)DOAJ047355972 (DE-599)DOAJ3f20c35f90174dfa807d3afb68b5f2cf DE-627 ger DE-627 rakwb eng QH573-671 Angela Zhang verfasserin aut A Leucine Zipper Dimerization Strategy to Generate Soluble T Cell Receptors Using the <i<Escherichia coli</i< Expression System 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier T cell-mediated adaptive immunity plays a key role in immunological surveillance and host control of infectious diseases. A better understanding of T cell receptor (TCR) recognition of pathogen-derived epitopes or cancer-associated neoantigens is the basis for developing T cell-based vaccines and immunotherapies. Studies on the interaction between soluble TCR α:β heterodimers and peptide-bound major histocompatibility complexes (pMHCs) inform underlying mechanisms driving TCR recognition, but not every isolated TCR can be prepared in soluble form for structural and functional studies using conventional methods. Here, taking a challenging HIV-specific TCR as a model, we designed a general leucine zipper (LZ) dimerization strategy for soluble TCR preparation using the <i<Escherichia coli</i< expression system. We report details of TCR construction, inclusion body expression and purification, and protein refolding and purification. Measurements of binding affinity between the TCR and its specific pMHC using surface plasmon resonance (SPR) verify its activity. We conclude that this is a feasible approach to produce challenging TCRs in soluble form, needed for studies related to T cell recognition. T cell receptor protein engineering leucine zipper <i<E. coli</i< expression refolding purification Cytology Alicja Piechocka-Trocha verfasserin aut Xiaolong Li verfasserin aut Bruce D. Walker verfasserin aut In Cells MDPI AG, 2012 11(2022), 3, p 312 (DE-627)718622081 (DE-600)2661518-6 20734409 nnns volume:11 year:2022 number:3, p 312 https://doi.org/10.3390/cells11030312 kostenfrei https://doaj.org/article/3f20c35f90174dfa807d3afb68b5f2cf kostenfrei https://www.mdpi.com/2073-4409/11/3/312 kostenfrei https://doaj.org/toc/2073-4409 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 11 2022 3, p 312
language	English
source	In Cells 11(2022), 3, p 312 volume:11 year:2022 number:3, p 312
sourceStr	In Cells 11(2022), 3, p 312 volume:11 year:2022 number:3, p 312
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	T cell receptor protein engineering leucine zipper <i<E. coli</i< expression refolding purification Cytology
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container_title	Cells
authorswithroles_txt_mv	Angela Zhang @@aut@@ Alicja Piechocka-Trocha @@aut@@ Xiaolong Li @@aut@@ Bruce D. Walker @@aut@@
publishDateDaySort_date	2022-01-01T00:00:00Z
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callnumber-first	Q - Science
author	Angela Zhang
spellingShingle	Angela Zhang misc QH573-671 misc T cell receptor misc protein engineering misc leucine zipper misc <i<E. coli</i< expression misc refolding misc purification misc Cytology A Leucine Zipper Dimerization Strategy to Generate Soluble T Cell Receptors Using the <i<Escherichia coli</i< Expression System
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topic_title	QH573-671 A Leucine Zipper Dimerization Strategy to Generate Soluble T Cell Receptors Using the <i<Escherichia coli</i< Expression System T cell receptor protein engineering leucine zipper <i<E. coli</i< expression refolding purification
topic	misc QH573-671 misc T cell receptor misc protein engineering misc leucine zipper misc <i<E. coli</i< expression misc refolding misc purification misc Cytology
topic_unstemmed	misc QH573-671 misc T cell receptor misc protein engineering misc leucine zipper misc <i<E. coli</i< expression misc refolding misc purification misc Cytology
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title	A Leucine Zipper Dimerization Strategy to Generate Soluble T Cell Receptors Using the <i<Escherichia coli</i< Expression System
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title_full	A Leucine Zipper Dimerization Strategy to Generate Soluble T Cell Receptors Using the <i<Escherichia coli</i< Expression System
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title_sort	leucine zipper dimerization strategy to generate soluble t cell receptors using the <i<escherichia coli</i< expression system
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title_auth	A Leucine Zipper Dimerization Strategy to Generate Soluble T Cell Receptors Using the <i<Escherichia coli</i< Expression System
abstract	T cell-mediated adaptive immunity plays a key role in immunological surveillance and host control of infectious diseases. A better understanding of T cell receptor (TCR) recognition of pathogen-derived epitopes or cancer-associated neoantigens is the basis for developing T cell-based vaccines and immunotherapies. Studies on the interaction between soluble TCR α:β heterodimers and peptide-bound major histocompatibility complexes (pMHCs) inform underlying mechanisms driving TCR recognition, but not every isolated TCR can be prepared in soluble form for structural and functional studies using conventional methods. Here, taking a challenging HIV-specific TCR as a model, we designed a general leucine zipper (LZ) dimerization strategy for soluble TCR preparation using the <i<Escherichia coli</i< expression system. We report details of TCR construction, inclusion body expression and purification, and protein refolding and purification. Measurements of binding affinity between the TCR and its specific pMHC using surface plasmon resonance (SPR) verify its activity. We conclude that this is a feasible approach to produce challenging TCRs in soluble form, needed for studies related to T cell recognition.
abstractGer	T cell-mediated adaptive immunity plays a key role in immunological surveillance and host control of infectious diseases. A better understanding of T cell receptor (TCR) recognition of pathogen-derived epitopes or cancer-associated neoantigens is the basis for developing T cell-based vaccines and immunotherapies. Studies on the interaction between soluble TCR α:β heterodimers and peptide-bound major histocompatibility complexes (pMHCs) inform underlying mechanisms driving TCR recognition, but not every isolated TCR can be prepared in soluble form for structural and functional studies using conventional methods. Here, taking a challenging HIV-specific TCR as a model, we designed a general leucine zipper (LZ) dimerization strategy for soluble TCR preparation using the <i<Escherichia coli</i< expression system. We report details of TCR construction, inclusion body expression and purification, and protein refolding and purification. Measurements of binding affinity between the TCR and its specific pMHC using surface plasmon resonance (SPR) verify its activity. We conclude that this is a feasible approach to produce challenging TCRs in soluble form, needed for studies related to T cell recognition.
abstract_unstemmed	T cell-mediated adaptive immunity plays a key role in immunological surveillance and host control of infectious diseases. A better understanding of T cell receptor (TCR) recognition of pathogen-derived epitopes or cancer-associated neoantigens is the basis for developing T cell-based vaccines and immunotherapies. Studies on the interaction between soluble TCR α:β heterodimers and peptide-bound major histocompatibility complexes (pMHCs) inform underlying mechanisms driving TCR recognition, but not every isolated TCR can be prepared in soluble form for structural and functional studies using conventional methods. Here, taking a challenging HIV-specific TCR as a model, we designed a general leucine zipper (LZ) dimerization strategy for soluble TCR preparation using the <i<Escherichia coli</i< expression system. We report details of TCR construction, inclusion body expression and purification, and protein refolding and purification. Measurements of binding affinity between the TCR and its specific pMHC using surface plasmon resonance (SPR) verify its activity. We conclude that this is a feasible approach to produce challenging TCRs in soluble form, needed for studies related to T cell recognition.
collection_details	GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700
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title_short	A Leucine Zipper Dimerization Strategy to Generate Soluble T Cell Receptors Using the <i<Escherichia coli</i< Expression System
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A Leucine Zipper Dimerization Strategy to Generate Soluble T Cell Receptors Using the <i<Escherichia coli</i< Expression System

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