一种G蛋白偶联受体-趋化因子受体的表达方法
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摘要
趋化因子受体为7次跨膜蛋白G蛋白偶联受体,在人体疾病及肿瘤的发生和发展中扮演重要角色,其结构破解对未来分子靶向药物开发具有巨大的潜在价值。趋化因子受体的成功表达是破解其结构的前提条件。然而,由于跨膜结构的特殊性,其表达方法相较于一般蛋白更具有挑战。通过对趋化因子受体在大肠杆菌、哺乳动物细胞、以及昆虫细胞表达系统内的表达方法进行综述,为相关趋化因子受体的表达方法提供参考。
Chemokine receptors are seven transmembrane protein G-protein coupled receptors, which play important role in human diseases and tumor development. Their structural information has significant and potential value in the development of molecular targeted drugs. Successful expression of chemokine receptors is a key prerequisite for its structure characterization. However, due to membrane structure, the expression method is much more challenging compared with general proteins. This paper reviewed the expression methods of chemokine receptors in E-coli and mammalian cell and insect cell systems providing a method reference for future expression of chemokine receptors.
Chemokine receptors are seven transmembrane protein G-protein coupled receptors, which play important role in human diseases and tumor development. Their structural information has significant and potential value in the development of molecular targeted drugs. Successful expression of chemokine receptors is a key prerequisite for its structure characterization. However, due to membrane structure, the expression method is much more challenging compared with general proteins. This paper reviewed the expression methods of chemokine receptors in E-coli and mammalian cell and insect cell systems providing a method reference for future expression of chemokine receptors.
引文
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[5]CAMPBELL L, MAXWELL P, WAUGH D. Rationale and Means to Target Pro-Inflammatory Interleukin-8(CXCL8)Signalingin Cancer[J]. Pharmaceuticals, 2013, 6(8):929-959.
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[10]WU B, CHIEN E Y, MOL C D, et al. Structures of the CXCR4 chemokine GPCR with small-molecule and cyclic peptideantagonists[J]. Science, 2010, 330(6007):1066-1071.
[11]JOSHUA B, RUBIN A L, KUNG R S, et al. A small-molecule antagonist of CXCR4 inhibits intracranial growth of primarybrain tumors[J]. Proceedings of the National Academy of Sciences of the United States of America, 2003, 100(23):13513.
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[13]SKRETAS G, MAKINO T, VARADARAJAN N, et al. Multi-copy genes that enhance the yield of mammalian Gprotein-coupled receptors in Escherichia coli[J]. Metab Eng, 2012, 14(5):591-602.
[14]REN H, YU D, GE B, et al. High-level production, solubilization and purification of synthetic human GPCR chemokinereceptors CCR5, CCR3, CXCR4 and CX3CR1[J]. PLo S One, 2009, 4(2):e4509.
[15]LU Z, DI Blasio-Smith E A, GRANT K L, et al. Histidine patchthioredoxins. Mutant forms ofthioredoxin with metal chelatingaffinity that provide for convenient purifications of thioredoxin fusion proteins[J]. J Biol Chem, 1996, 271(9):5059-5065.
[16]吴芳明,刘永学. GPCR-Gα融合蛋白及其在o GPCRs配基筛选中的应用[J].中国药理学通报, 2005, 21(5):518-521.
[17]白立川. M_3-G_(11α)融合蛋白在Sf9细胞中的表达及特异性配体的筛选[D].沈阳:中国医科大学, 2009.
[18]GE B, LI W, YIN Y. Enrichment separation of recombinant human CCR3 using detergent/polymer two-phase system[J].Biotechnol Lett, 2010, 32(3):393-397.
[19]WHITE J F, TRINH L B, SHILOACH J, et al. Automated large-scale purification of a G protein-coupled receptor forneurotensin[J]. FEBS Lett, 2004, 564(3):289-293.
[20]WHITE J F, TRINH L B, SHILOACH J, et al. Automated large-scale purification of a G-protein-coupled receptor forneurotensin[J]. Febs Letters, 2004, 564(3):289-293.
[21]GRISSHAMMER R, WHITE J F, TRINH L B, et al. Large-scale expression and purification of a G-protein-coupledreceptor for structure determination-an overview[J]. J StructFunct Genomics, 2005, 6(2-3):159-163.
[22]王明清.人趋化因子受体CCR3的制备及生物活性研究[D].青岛:中国石油大学(华东), 2013.
[23]REN H, YU D, GE B, et al. High-level production, solubilization and purification of synthetic human GPCR chemokinereceptors CCR5, CCR3, CXCR4 and CX3CR1[J]. PLo S One, 2009, 4(2):e4509.
[24]ZHAO Q, WU B L. Ice breaking in GPCR structural biology[J].ActaPharmacol Sin, 2012, 33(3):324-334.
[25]郁硕,陈锋,刘英富,等.可溶性GST-CRH蛋白原核表达条件的优化及纯化[J].天津医药, 2017, 45(2):146-150.
[26]MAKRIDES S C. Strategies for achieving high-level expression of genes in Escherichia coli[J]. Microbiol Rev, 1996, 60(3):512-538.
[27]REN H, YU D, GE B, et al. High-level production, solubilization and purification of synthetic human GPCR chemokinereceptors CCR5, CCR3, CXCR4 and CX3CR1[J]. PLo S One, 2009, 4(2):e4509.
[28]ZHAO Q, WU B L. Ice breaking in GPCR structural biology[J]. ActaPharmacol Sin, 2012, 33(3):324-334.
[29]SEDDON A M, CURNOW P, BOOTH P J. Membrane proteins, lipids and detergents:not just a soap opera[J]. BiochimBiophys Acta, 2004, 1666(1-2):105-117,
[30]LEMARIRE M, CHAMPEIL P, MOLLER J V. Interaction of membrane proteins and lipids with solubilizing detergents[J].Biochim Biophys Acta, 2000, 1508(1-2):86-111.
[31]BANE S E, VELASQIEZ J E, ROBINSON A S. Expression and purification of milligram levels of inactive G-proteincoupled receptors in E. coli[J]. Protein ExprPurif, 2007, 52(2):348-355.
[32]O'MALLEY M A, MANCINI J D, YOUNG C L, et al. Progress toward heterologous expression of active G-protein-coupled receptors in Saccharomyces cerevisiae:Linking cellular stress response with translocation and trafficking[J].Protein Sci, 2009, 18(11):2356-2370.
[33]XIANG J, CHUN E, LIU C, et al. 2016 Successful Strategies to Determine High-resolution Structures of GPCRs(1)[J].Trends in Pharmacological Sciences, 2016, 37(12):1055-1069.
[34]MIRZABEKOV T, BANNERT N, FARZAN M, et al. Enhanced expression, native purification, and characterization ofCCR5, a principal HIV-1 coreceptor[J]. J Biol Chem, 1999, 274(40):28745-28750.
[35]BABCOCK G J, MIRZABEKOV T, WOJTOWICZ W, et al. Ligand binding characteristics of CXCR4 incorporated intoparamagnetic proteoliposomes[J]. J Biol Chem, 2001, 276(42):38433-38440.
[36]STONE M J, CHUANG S, HOU X, et al. Tyrosine sulfation:an increasingly recognised post-translational modification ofsecreted proteins[J]. N Biotechnol, 2009, 25(5):299-317.
[37]GUTIERREZ J, KREMER L, ZABALLOS A, et al. Analysis of post-translational CCR8 modifications and their influenceon receptor activity[J]. J Biol Chem, 2004, 279(15):14726-14733.
[38]ZHU J Z, MILLARD C J, LUDEMAN J P, et al. Tyrosine sulfation influences the chemokine binding selectivity ofpeptides derived from chemokine receptor CCR3[J]. Biochemistry, 2011, 50(9):1524-1534.
[39]MASSOTTE D. G protein-coupled receptor overexpression with the baculovirus-insect cell system:a tool for structuraland functional studies[J]. Biochimica et biophysica acta, 2003, 1610(1):77.
[40]ALOIA A L, GLATZ R V, MCMURCHIE E J, et al. GPCR expression using baculovirus-infected Sf9 cells[J]. Methods inMolecular Biology, 2009, 552:115.
[41]KUFAREVAL I, STEPHENS B S, HOLDEN L G, et al. Stoichiometry and geometry of the CXC chemokine receptor 4complex with CXC ligand 12:Molecular modeling and experimental validation[J]. Proceedings of the National Academyof Sciences of the United States of America, 2014, 111(50):5363-5372.
[42]WU B, CHIEN E Y, MOL C D, et al. Structures of the CXCR4 chemokine GPCR with small-molecule and cyclic peptideantagonists[J]. Science, 2010, 330(6007):1066-1071.
[43]THORSEN T S, MATT R, WERIS W I, et al. Modified T4 Lysozyme Fusion Proteins Facilitate G Protein-CoupledReceptor Crystallogenesis[J]. Structure, 2014, 22(11):1657-1664.
[44]KLEEMANN P, PAPA D, VIGILCRUZ S, et al. Functional reconstitution of the human chemokine receptor CXCR4 withG(i)/G(o)-proteins in Sf9 insect cells[J]. Naunyn-Schmiedeberg's archives of pharmacology, 2008, 378(3):261.
[45]LUCKOW V A, SUMMERS M D. High level expression of nonfused foreign genes with Autographa californica, nuclearpolyhedrosis virus expression vectors[J]. Virology, 1989, 170(1):31-39.
[46]SCHNEIDER E H, SEIFERT R. Sf9 cells:a versatile model system to investigate the pharmacological properties of Gprotein-coupled receptors[J]. Pharmacology&Therapeutics, 2010, 128(3):387-418.
[47]HSIEH P, ROBBINS P W. Regulation of asparagine-linked oligosaccharide processing. Oligosaccharide processing inAedes albopictus mosquito cells[J]. Journal of Biological Chemistry, 1984, 259(4):2375-2382.
[2]GRIFFITH J W, SOKOL C L, LUSTER A D. Chemokines and Chemokine Receptors:Positioning Cells for Host Defense andImmunity[J]. Annual Review of Immunology, 2014, 32(1):659.
[3]SINGH A K, ARYA R K, TRIVEDI A K, et al. Chemokine receptor trio:CXCR3, CXCR4 and CXCR7 crosstalk via CXCL11and CXCL12[J]. Cytokine&Growth Factor Reviews, 2013, 24(1):41-49.
[4]VIOLA A, LUSTER A D. Chemokines and their receptors:drug targets in immunity andinflammation[J]. Annu RevPharmacolToxicol, 2008, 48(1):171-197.
[5]CAMPBELL L, MAXWELL P, WAUGH D. Rationale and Means to Target Pro-Inflammatory Interleukin-8(CXCL8)Signalingin Cancer[J]. Pharmaceuticals, 2013, 6(8):929-959.
[6]ZHANG Q, SUN L, YIN L, et al. CCL19/CCR7 upregulatesheparanase via specificity protein-1(Sp1)to promote invasion ofcell in lung cancer[J]. TumourBiol, 2013, 34(5):2703-2708.
[7]ERRENI M, LAGHI L, CELESTI G, et al. W1767 Expression and Function of the Chemokine CX3CL1 and Its Receptor Cx3cr1in Human Colorectal Cancer[J]. Gastroenterology, 2010, 138(5):736.
[8]ZHAO L, LIM S Y, GORDON-WEEKS A N, et al. Recruitment of a myeloid cell subset(CD11b/Gr1 mid)via CCL2/CCR2promotes the development of colorectal cancer liver metastasis[J]. Hepatology(Baltimore,Md.), 2013, 57(2):829-839.
[9]LU E, SU J, ZHOU Y, et al. CCL20/CCR6 promotes cell proliferation and metastasis in laryngeal cancer by activating p38pathway[J]. Biomed Pharmacother, 2017, 85:486-492.
[10]WU B, CHIEN E Y, MOL C D, et al. Structures of the CXCR4 chemokine GPCR with small-molecule and cyclic peptideantagonists[J]. Science, 2010, 330(6007):1066-1071.
[11]JOSHUA B, RUBIN A L, KUNG R S, et al. A small-molecule antagonist of CXCR4 inhibits intracranial growth of primarybrain tumors[J]. Proceedings of the National Academy of Sciences of the United States of America, 2003, 100(23):13513.
[12]TATE C G. Overexpression of mammalian integral membrane proteins for structural studies[J]. FEBS Lett, 2001, 504(3):94-98.
[13]SKRETAS G, MAKINO T, VARADARAJAN N, et al. Multi-copy genes that enhance the yield of mammalian Gprotein-coupled receptors in Escherichia coli[J]. Metab Eng, 2012, 14(5):591-602.
[14]REN H, YU D, GE B, et al. High-level production, solubilization and purification of synthetic human GPCR chemokinereceptors CCR5, CCR3, CXCR4 and CX3CR1[J]. PLo S One, 2009, 4(2):e4509.
[15]LU Z, DI Blasio-Smith E A, GRANT K L, et al. Histidine patchthioredoxins. Mutant forms ofthioredoxin with metal chelatingaffinity that provide for convenient purifications of thioredoxin fusion proteins[J]. J Biol Chem, 1996, 271(9):5059-5065.
[16]吴芳明,刘永学. GPCR-Gα融合蛋白及其在o GPCRs配基筛选中的应用[J].中国药理学通报, 2005, 21(5):518-521.
[17]白立川. M_3-G_(11α)融合蛋白在Sf9细胞中的表达及特异性配体的筛选[D].沈阳:中国医科大学, 2009.
[18]GE B, LI W, YIN Y. Enrichment separation of recombinant human CCR3 using detergent/polymer two-phase system[J].Biotechnol Lett, 2010, 32(3):393-397.
[19]WHITE J F, TRINH L B, SHILOACH J, et al. Automated large-scale purification of a G protein-coupled receptor forneurotensin[J]. FEBS Lett, 2004, 564(3):289-293.
[20]WHITE J F, TRINH L B, SHILOACH J, et al. Automated large-scale purification of a G-protein-coupled receptor forneurotensin[J]. Febs Letters, 2004, 564(3):289-293.
[21]GRISSHAMMER R, WHITE J F, TRINH L B, et al. Large-scale expression and purification of a G-protein-coupledreceptor for structure determination-an overview[J]. J StructFunct Genomics, 2005, 6(2-3):159-163.
[22]王明清.人趋化因子受体CCR3的制备及生物活性研究[D].青岛:中国石油大学(华东), 2013.
[23]REN H, YU D, GE B, et al. High-level production, solubilization and purification of synthetic human GPCR chemokinereceptors CCR5, CCR3, CXCR4 and CX3CR1[J]. PLo S One, 2009, 4(2):e4509.
[24]ZHAO Q, WU B L. Ice breaking in GPCR structural biology[J].ActaPharmacol Sin, 2012, 33(3):324-334.
[25]郁硕,陈锋,刘英富,等.可溶性GST-CRH蛋白原核表达条件的优化及纯化[J].天津医药, 2017, 45(2):146-150.
[26]MAKRIDES S C. Strategies for achieving high-level expression of genes in Escherichia coli[J]. Microbiol Rev, 1996, 60(3):512-538.
[27]REN H, YU D, GE B, et al. High-level production, solubilization and purification of synthetic human GPCR chemokinereceptors CCR5, CCR3, CXCR4 and CX3CR1[J]. PLo S One, 2009, 4(2):e4509.
[28]ZHAO Q, WU B L. Ice breaking in GPCR structural biology[J]. ActaPharmacol Sin, 2012, 33(3):324-334.
[29]SEDDON A M, CURNOW P, BOOTH P J. Membrane proteins, lipids and detergents:not just a soap opera[J]. BiochimBiophys Acta, 2004, 1666(1-2):105-117,
[30]LEMARIRE M, CHAMPEIL P, MOLLER J V. Interaction of membrane proteins and lipids with solubilizing detergents[J].Biochim Biophys Acta, 2000, 1508(1-2):86-111.
[31]BANE S E, VELASQIEZ J E, ROBINSON A S. Expression and purification of milligram levels of inactive G-proteincoupled receptors in E. coli[J]. Protein ExprPurif, 2007, 52(2):348-355.
[32]O'MALLEY M A, MANCINI J D, YOUNG C L, et al. Progress toward heterologous expression of active G-protein-coupled receptors in Saccharomyces cerevisiae:Linking cellular stress response with translocation and trafficking[J].Protein Sci, 2009, 18(11):2356-2370.
[33]XIANG J, CHUN E, LIU C, et al. 2016 Successful Strategies to Determine High-resolution Structures of GPCRs(1)[J].Trends in Pharmacological Sciences, 2016, 37(12):1055-1069.
[34]MIRZABEKOV T, BANNERT N, FARZAN M, et al. Enhanced expression, native purification, and characterization ofCCR5, a principal HIV-1 coreceptor[J]. J Biol Chem, 1999, 274(40):28745-28750.
[35]BABCOCK G J, MIRZABEKOV T, WOJTOWICZ W, et al. Ligand binding characteristics of CXCR4 incorporated intoparamagnetic proteoliposomes[J]. J Biol Chem, 2001, 276(42):38433-38440.
[36]STONE M J, CHUANG S, HOU X, et al. Tyrosine sulfation:an increasingly recognised post-translational modification ofsecreted proteins[J]. N Biotechnol, 2009, 25(5):299-317.
[37]GUTIERREZ J, KREMER L, ZABALLOS A, et al. Analysis of post-translational CCR8 modifications and their influenceon receptor activity[J]. J Biol Chem, 2004, 279(15):14726-14733.
[38]ZHU J Z, MILLARD C J, LUDEMAN J P, et al. Tyrosine sulfation influences the chemokine binding selectivity ofpeptides derived from chemokine receptor CCR3[J]. Biochemistry, 2011, 50(9):1524-1534.
[39]MASSOTTE D. G protein-coupled receptor overexpression with the baculovirus-insect cell system:a tool for structuraland functional studies[J]. Biochimica et biophysica acta, 2003, 1610(1):77.
[40]ALOIA A L, GLATZ R V, MCMURCHIE E J, et al. GPCR expression using baculovirus-infected Sf9 cells[J]. Methods inMolecular Biology, 2009, 552:115.
[41]KUFAREVAL I, STEPHENS B S, HOLDEN L G, et al. Stoichiometry and geometry of the CXC chemokine receptor 4complex with CXC ligand 12:Molecular modeling and experimental validation[J]. Proceedings of the National Academyof Sciences of the United States of America, 2014, 111(50):5363-5372.
[42]WU B, CHIEN E Y, MOL C D, et al. Structures of the CXCR4 chemokine GPCR with small-molecule and cyclic peptideantagonists[J]. Science, 2010, 330(6007):1066-1071.
[43]THORSEN T S, MATT R, WERIS W I, et al. Modified T4 Lysozyme Fusion Proteins Facilitate G Protein-CoupledReceptor Crystallogenesis[J]. Structure, 2014, 22(11):1657-1664.
[44]KLEEMANN P, PAPA D, VIGILCRUZ S, et al. Functional reconstitution of the human chemokine receptor CXCR4 withG(i)/G(o)-proteins in Sf9 insect cells[J]. Naunyn-Schmiedeberg's archives of pharmacology, 2008, 378(3):261.
[45]LUCKOW V A, SUMMERS M D. High level expression of nonfused foreign genes with Autographa californica, nuclearpolyhedrosis virus expression vectors[J]. Virology, 1989, 170(1):31-39.
[46]SCHNEIDER E H, SEIFERT R. Sf9 cells:a versatile model system to investigate the pharmacological properties of Gprotein-coupled receptors[J]. Pharmacology&Therapeutics, 2010, 128(3):387-418.
[47]HSIEH P, ROBBINS P W. Regulation of asparagine-linked oligosaccharide processing. Oligosaccharide processing inAedes albopictus mosquito cells[J]. Journal of Biological Chemistry, 1984, 259(4):2375-2382.