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[1] 何冰芳, 米兰, 陈文华. 大肠杆菌蛋白质分泌机理及其重组蛋白分泌表达新进展. 食品与生物技术学报, 2012, 31(6): 561-569. He B F, Mi L, Chen W H. The secretion mechanism of protein from E. coli and recent advancements of recombinant protein expression. J Food SCI Biotechnol, 2012, 31(6): 561-569.
[2] Ni Y, Chen R. Extracellular recombinant protein production from Escherichia coli. Biotechnol Lett, 2009, 31: 1661-1670.
[3] Yoon S H, Kim S K, Kim J F. Secretory production of recombinant proteins in Escherichia coli. Recent Pat Biotechnol, 2010, 4: 23-29.
[4] 訾祯祯, 杨志伟. 细菌蛋白分泌途径的研究进展. 生物技术通报, 2011, 8: 44-54. Zi Z Z, Yang Z W. Protein secretion pathways in bacterial cells. Biol Bull, 2011, 8: 44-54.
[5] Mergulho F J, Summers D K, Monteiro G A. Recombinant protein secretion in Escherichia coli. Biotechnol Adv, 2005, 23(3): 177-202.
[6] Badyakina A O, Nesmeyanova M A. Biogenesis and secretion of overproduced protein in recombinant strains of Escherichia coli. Process Biochem, 2005, 40: 509-518.
[7] Chen S, Liu Z, Chen J, et al. Study on improvement of extracellular production of recombinant Thermobifida fusca cutinase by Escherichia coli. Appl Biochem Biotechnol, 2011, 165: 666-675.
[8] Yamabhai M, Emrat S, Sukasem S, et al. Secretion of recombinant Bacillus hydrolytic enzymes using Escherichia coli expression systems. J Biotechnol, 2008, 133: 50-57.
[9] Delepelaire P. Type I secretion in gram-negative bacteria. Biochim Biophys Acta, 2004, 1694: 149-161.
[10] Holland I B, Schmitt L, Young J. Type I protein secretion in bacteria, the ABC-transporter dependent pathway. Mol Membr Biol, 2005, 22(1-2): 29-39.
[11] Koronakis V, Sharff A, Koronakis E, et al. Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export. Nature, 2000, 405: 914-919.
[12] Zaitseva J, Jenewein S, Oswald C, et al. A molecular understanding of the catalytic cycle of the nucleotide-binding domain of the ABC transporter HlyB. Biochem Soc Trans, 2005, 33: 990-995.
[13] Sanchez-Magraner L, Viguera A R, Garcia-Pacios M, et al. The calcium-binding C-terminal domain of Echerichia coli alpha-hemolysin is a major determinant in the surface-active properties of the protein. J Biol Chem, 2007, 282(16): 11827-11835.
[14] Ludwig A, Jarchau T, Benz R, et al. The repeat domain of Escherichia coli haemolysin (HlyA) is responsible for its Ca2+-dependent binding to erythrocytes. Mol Gen Genet, 1988, 214: 553-561.
[15] Jones H E, Holland I B, Campbell A K. Direct measurement of free Ca2+shows different regulation of Ca2+ between the periplasm and the cytosol of Escherichia coli. Cell Calcium, 2002, 32:183-192.
[16] Kanonenberg K, Schwarz Christian K W, Schmitt L. Type I secretion systems-a story of appendices. Res Microbiol, 2013, 3: 1-9.
[17] Gentschev I, Dietrich G, Goebel W. The E. coli α-hemolysin secretion system and its use in vaccine development. Trends Microbiol, 2002, 10(1): 39-45.
[18] Mohammadian M, Fathi-Roudsari M, Mollania N, et al. Enhanced expression of a recombinant bacterial laccase at low temperature and microaerobic conditions: purification and biochemical characterization. J Ind Microbiol Biotechnol, 2010, 37: 863-869.
[19] Martins L O, Soares C M, Pereira M M, et al. Molecular and biochemical characterization of a highly stable bacterial laccase that occurs as a structural component of the Bacillus subtilis endospore coat. J Biol Chem, 2002, 277(21): 18849-18859.
[20] Fernandez L A, Sola I, Enjuanes L, et al. Specific secretion of active single-chain Fv antibodies into the supernatants of Escherichia coli cultures by use of the hemolysin system. Appl Environ Microbiol, 2000, 66(11): 5024-5029.
[21] Bisi D C, Lampe D J. Secretion of anti-Plasmodium effector proteins from a natural Pantoea agglomerans isolate by using pelB and hlyA secretion signals. Appl Environ Microbiol, 2011, 77(13): 4669-4675.
[22] Narayanan N, Khan M, Chou C P. Enhancing functional expression of heterologous lipase B in Escherichis coli by extracellular secretion. J Ind Microbiol Biotechnol, 2010, 37: 349-361.
[23] Gomez-duarte O G, Pasetti M, Santiago A, et al. Expression, extracellular secretion, and immunogenicity of the Plasmodium falciparum sporozoite surface protein 2 in Salmonella vaccine strains. Infect Immun, 2001, 69(2): 1192-1198.
[24] Sugamata Y, Shiba T. Improved secretory production of recombinant proteins by random mutagenesis of hlyB, an alpha-hemolysin transporter from Escherichia coli. Appl Environ Microbiol, 2005, 71(2): 656-662.
[25] Li Y, Chen C X, Specht B U, et al. Cloning and hemolysin-mediated secretory expression of a codon-optimized synthetic human interleukin-6 gene in Escherichia coli. Protein Expr Purif, 2002, 25: 437-447.
[26] 宁亚蕾, 周立雄, 张卫军, 等. 利用α-溶血素系统分泌表达重组人白介素. 免疫学杂志, 2008, 24(4): 380-384. Ning Y L, Zhou L X, Zhang W J, et al. Extracellular secretion of recombinant hIL-6 utlizing UPEC α-hemolysin (HlyA) system. J Immunol, 2008, 24(4): 380-384.
[27] Su L, Chen S, Yi L, et al. Extracellular overexpression of recombinant Thermobifida fusca cutinase by alpha-hemolysin secretion system in E. coli BL21(DE3). Microb Cell Fact, 2012, 11: 1-8.
[28] Low K O, Mahadi N M, Rahim R A, et al. Enhanced secretory production of hemolysin-mediated cyclodextrin glucanotransferase in Escherichia coli by random mutagenesis of the ABC transporter system. J Biotechnol, 2010, 150: 453-459.
[29] Low K O, Mahadi N M, Rahim R A, et al. An effective extracellular protein secretion by an ABC transporter system in Escherichia coli: statistical modeling and optimization of cyclodextrin glucanotransferase secretory production. J Ind Microbiol Biotechnol, 2011, 38: 1587-1597.
[30] 张兆山. 大肠杆菌α-溶血素分泌表达系统的构建及应用初探. 北京: 军事科学医学院生物工程研究所, 2004. Zhang Z S. Study of construction and application of the recombinant secretion plasmid based on α-hemolysin secretion system. Beijing: Institute of Biological Engineering of the Military Academy of Medical Sciences, 2004.
[31] Bakkes P J, Jenewein S, Smits S H, et al. The rate of folding dictates substrate secretion by the Escherichia coli hemolysin type I secretion system. J Biol Chem, 2010, 285(52): 40573-40580.
[32] Schwarz C K, Landsberg D, Lenders C, et al. Using an E. coli Type I secretion system to secrete the mammalian, intracellular protein IFABP in its active form. J Biotechnol, 2012, 159: 155-161.
[33] Jumpertz T, Chervaux C, Racher K, et al. Mutations affecting the extreme C terminus of Escherichia coli haemolysin A reduce haemolytic activity by altering the folding of the toxin. Microbiology, 2010, 156: 2495-2505.
[34] Kenny B, Chervaux C, Holland I B. Evidence that residues -15 to -46 of the haemolysin secretion signal are involved in early steps in secretion, leading to recognition of the translocator. Mol Microbiol, 1994, 11: 99-109.
[35] Kenny B, Haigh R, Holland I B. Analysis of the haemolysin transport process through the secretion from Escherichia coli of PCM, CAT or beta-galactosidase fused to the Hly C-terminal signal domain. Mol Microbiol, 1991, 5(10): 2557-2568.
[36] Pimenta A L, Young J, Holland I B, et al. Antibody analysis of the localisation, expression and stability of HlyD, the MF Pcomponent of the E. coli haemolysin translocator. Mol Gen Genet, 1999, 261: 122-132.
[37] Schulein R, Gentschev S, Schlor I, et al. Identification and characterization of two functional domains of the haemolysin translocator protein HlyD. Mol Gen Genet, 1994, 245: 203-211.
[38] Pimenta A L, Racher K, Jamieson L, et al. Mutations in HlyD, part of the type I translocator for hemolysin secretion, affect the folding of the secreted toxin. J Bacteriol, 2005, 187(21): 7471-7480.
[39] Blight M A, Pimenta A L, Lazzaroni J C, et al. Identification and preliminary characterization of temperature-sensitive mutations affecting HlyB, the translocator required for the secretion of haemolysin (HlyA) from Escherichia coli. Mol Gen Genet, 1994, 245: 431-440.
[40] Sheps J A, Cheung I, Ling V. Hemolysin transport in Escherichia coli point mutants in HlyB compensate for a deletion in the predicted amphiphilic helix region of the HlyA signal. J Biol Chem, 1995, 270 (24): 14829-14834.
[41] Lee P S, Lee K H. Engineering HlyA hypersecretion in Escherichia coli based on proteomic and microarray analyses. Biotechnol Bioeng, 2005, 89: 195-205.
[42] Prateek G, Kelvin H L. Silent mutations result in HlyA hypersecretion by reducing intracellular HlyA protein aggregates. Biotechnol Bioeng, 2008, 101(5): 967-974.
[43] Vakharia H, German G J, Misra R. Isolation and characterization of Escherichia coli tolC mutants defective in secreting enzymatically active alpha-hemolysin. J Bacteriol, 2001, 183(23): 6908-6916.
[44] Nakano H, Kawakami Y, Nishimura H. Secretion of genetically-engineered dihydrofolate reductase from Escherichia coli using an E. coli alpha-hemolysin membrane translocation system. Appl Microbiol Biotechnol, 1992, 37(6): 765-771.
[45] Herm-Gotz A, Agop-Nersesian C, Munter S, et al. Rapid control of protein level in the apicomplexan Toxoplasma gondii. Nat Methods, 2007, 4: 1003-1005.
[46] Armstrong C M, Goldberg D E. An FKBP destabilization domain modulates protein levels in Plasmodium falciparum. Nat Meth, 2007, 4: 1007-1009.
[47] Banaszynski L A, Chen L C, Maynard-Smith L A, et al. A rapid reversible, and tunable method to regulate protein function in living cells using synthetic small molecules. Cell, 2006, 126: 995-1004.
[48] Sørensen H P, Mortensen K K. Advanced genetic strategies for recombinant protein expression in Escherichia coli. J Biotechnol, 2005, 115: 113-128.
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