Establishment of cell surface engineering and its development

References

• Anonymous. Arming yeast with cell-surface catalysts. Chem. Eng. News. 1997;75:32.
   Web of Science ®Google Scholar
• Ueda M, Tanaka A. Genetic immobilization of proteins on the yeast cell surface. Biotechnol. Adv. 2000;18:121–140.10.1016/S0734-9750(00)00031-8
   PubMed Web of Science ®Google Scholar
• Ueda M, Tanaka A. Cell surface engineering of yeast: construction of arming yeast with biocatalyst. J. Biosci. Bioeng. 2000;90:125–136.10.1016/S1389-1723(00)80099-7
   PubMed Web of Science ®Google Scholar
• Su GD, Zhang X, Lin Y. Surface display of active lipase in Pichia pastoris using Sed1 as an anchor protein. Biotechnol. Lett. 2010;32:1131–1136.10.1007/s10529-010-0270-4
   PubMed Web of Science ®Google Scholar
• Chen YP, Hwang IE, Lin CJ, et al. Enhancing the stability of xylanase from Cellulomonas fimi by cell-surface display on Escherichia coli. J. Appl. Microbiol. 2012;112:455–463.10.1111/jam.2012.112.issue-3
   PubMed Web of Science ®Google Scholar
• Aoki W, Yoshino Y, Morisaka H, et al. High-throughput screening of improved protease inhibitors using a yeast cell surface display system and a yeast cell chip. J. Biosci. Bioeng. 2011;111:16–18.10.1016/j.jbiosc.2010.08.006
   PubMed Web of Science ®Google Scholar
• Boder ET, Wittrup KD. Yeast surface display for screening combinatorial polypeptide libraries. Nat. Biotechnol. 1997;15:553–557.10.1038/nbt0697-553
   PubMed Web of Science ®Google Scholar
• Chen W, Georgiou G. Cell-surface display of heterologous proteins: from high-throughput screening to environmental applications. Biotechnol. Bioeng. 2002;79:496–503.10.1002/(ISSN)1097-0290
   PubMed Web of Science ®Google Scholar
• Fukuda T, Kato M, Kadonosono T, et al. Enhancement of substrate recognition ability by combinatorial mutation of β-glucosidase displayed on the yeast cell surface. Appl. Microbiol. Biotechnol. 2007;76:1027–1033.10.1007/s00253-007-1070-1
   PubMed Web of Science ®Google Scholar
• Yeung YA, Wittrup KD. Quantitative screening of yeast surface-displayed polypeptide libraries by magnetic bead capture. Biotechnol. Prog. 2002;18:212–220.10.1021/bp010186l
   PubMed Web of Science ®Google Scholar
• Georgiou G, Poetschke HL, Stathopoulos C, et al. Practical applications of engineering gram-negative bacterial cell surfaces. Trends Biotechnol. 1993;11:6–10.10.1016/0167-7799(93)90068-K
   PubMed Web of Science ®Google Scholar
• Kuroda K, Ueda M. Engineering of microorganisms towards recovery of rare metal ions. Appl. Microbiol. Biotechnol. 2010;87:53–60.10.1007/s00253-010-2581-8
   PubMed Web of Science ®Google Scholar
• Kuroda K, Ueda M. Molecular design of the microbial cell surface toward the recovery of metal ions. Curr. Opin. Biotechnol. 2011;22:427–433.10.1016/j.copbio.2010.12.006
   PubMed Web of Science ®Google Scholar
• Kuroda K, Ueda M. Cell surface engineering of yeast for applications in white biotechnology. Biotechnol. Lett. 2011;33:1–9.10.1007/s10529-010-0403-9
   PubMed Web of Science ®Google Scholar
• Samuelson P, Gunneriusson E, Nygren PA, et al. Display of proteins on bacteria. J. Biotechnol. 2002;96:129–154.10.1016/S0168-1656(02)00043-3
   PubMed Web of Science ®Google Scholar
• Ståhl S, Uhlén M. Bacterial surface display: trends and progress. Trends Biotechnol. 1997;15:185–192.10.1016/S0167-7799(97)01034-2
   PubMed Web of Science ®Google Scholar
• Smith GP. Filamentous fusion phage: novel expression vectors that display cloned antigens on the virion surface. Science. 1985;228:1315–1317.10.1126/science.4001944
   PubMed Web of Science ®Google Scholar
• Smith GP. Surface presentation of protein epitopes using bacteriophage expression systems. Curr. Opin. Biotechnol. 1991;2:668–673.10.1016/0958-1669(91)90032-Z
   PubMedGoogle Scholar
• Tabuchi S, Ito J, Adachi T, et al. Display of both N- and C-terminal target fusion proteins on the Aspergillus oryzae cell surface using a chitin-binding module. Appl. Microbiol. Biotechnol. 2010;87:1783–1789.10.1007/s00253-010-2664-6
   PubMed Web of Science ®Google Scholar
• Adachi T, Ito J, Kawata K, et al. Construction of an Aspergillus oryzae cell-surface display system using a putative GPI-anchored protein. Appl. Microbiol. Biotechnol. 2008;81:711–719.10.1007/s00253-008-1687-8
   PubMed Web of Science ®Google Scholar
• Tanino T, Fukuda H, Kondo A. Construction of a Pichia pastoris cell-surface display system using Flo1p anchor system. Biotechnol. Prog. 2006;22:989–993.10.1021/bp060133+
   PubMed Web of Science ®Google Scholar
• Wang Q, Li L, Chen M, et al. Construction of a novel system for cell surface display of heterologous proteins on Pichia pastoris. Biotechnol. Lett. 2007;29:1561–1566.10.1007/s10529-007-9430-6
   PubMed Web of Science ®Google Scholar
• Wang Q, Li L, Chen M, et al. Construction of a novel Pichia pastoris cell-surface display system based on the cell wall protein Pir1. Curr. Microbiol. 2008;56:352–357.10.1007/s00284-007-9089-1
   PubMed Web of Science ®Google Scholar
• Yuzbasheva EY, Yuzbashev TV, Laptev IA, et al. Efficient cell surface display of Lip2 lipase using C-domains of glycosylphosphatidylinositol-anchored cell wall proteins of Yarrowia lipolytica. Appl. Microbiol. Biotechnol. 2011;91:645–654.10.1007/s00253-011-3265-8
   PubMed Web of Science ®Google Scholar
• Washida M, Takahashi S, Ueda M, et al. Spacer-mediated display of active lipase on the yeast cell surface. Appl. Microbiol. Biotechnol. 2001;56:681–686.10.1007/s002530100718
   PubMed Web of Science ®Google Scholar
• Breinig F, Schmitt MJ. Spacer-elongated cell wall fusion proteins improve cell surface expression in the yeast Saccharomyces cerevisiae. Appl. Microbiol. Biotechnol. 2002;58:637–644.
   PubMed Web of Science ®Google Scholar
• Lipke PN, Kurja J. Sexual agglutination in budding yeasts: Structure, function, and regulation of adhesion glycoproteins. Microbiol. Rev. 1992;56:180–194.
   PubMedGoogle Scholar
• Kuroda K, Ueda M. Generation of arming yeasts with active proeins and peptides via cell surface display system—Cell surface engineering, bio-arming technology. Methods Mol. Biol. 2014;1152:137–155.10.1007/978-1-4939-0563-8
   PubMedGoogle Scholar
• Kuroda K, Matsui K, Higuchi S, et al. Enhancement of display efficiency in yeast display system by vector engineering and gene disruption. Appl. Microbiol. Biotechnol. 2009;82:713–719.10.1007/s00253-008-1808-4
   PubMed Web of Science ®Google Scholar
• Sato N, Matsumoto T, Ueda M, et al. Long anchor using Flo1 protein enhances reactivity of cell surface-displayed glucoamylase to polymer substrates. Appl. Microbiol. Biotechnol. 2002;60:469–474.
   PubMed Web of Science ®Google Scholar
• Van der Vaart JM, te Biesebeke R, Chapman JW, et al. Comparison of cell wall proteins of Saccharomyces cerevisiae as anchors for cell surface expression of heterologous proteins. Appl. Environ. Microbiol. 1997;63:615–620.
   PubMed Web of Science ®Google Scholar
• Wang Z, Mathias A, Stavrou S, et al. A new yeast display vector permitting free scFv amino termini can augment ligand binding affinities. Protein Eng. Des. Sel. 2005;18:337–343.10.1093/protein/gzi036
   PubMed Web of Science ®Google Scholar
• Wentz AE, Shusta EV. A novel high-throughput screen reveals yeast genes that increase secretion of heterologous proteins. Appl. Environ. Microbiol. 2007;73:1189–1198.10.1128/AEM.02427-06
   PubMed Web of Science ®Google Scholar
• Matsumoto T, Fukuda H, Ueda M, et al. Construction of yeast strains with high cell surface lipase activity by using novel display systems based on the flo1p flocculation functional domain. Appl. Environ. Microbiol. 2002;68:4517–4522.10.1128/AEM.68.9.4517-4522.2002
   PubMed Web of Science ®Google Scholar
• Abe H, Ohba M, Shimma Y, et al. Yeast cells harboring human α-1,3-fucosyltransferase at the cell surface engineered using Pir, a cell wall-anchored protein. FEMS Yeast Res. 2004;4:417–425.10.1016/S1567-1356(03)00193-4
   PubMed Web of Science ®Google Scholar
• Hara K, Ono T, Kuroda K, et al. Membrane-displayed peptide ligand activates the pheromone response pathway in Saccharomyces cerevisiae. J. Biochem. 2012;151:551–557.10.1093/jb/mvs027
   PubMed Web of Science ®Google Scholar
• Hara K, Shigemori T, Kuroda K, et al. Membrane-displayed somatostatin activates somatostatin receptor subtype-2 heterologously produced in Saccharomyces cerevisiae. AMB Express. 2012;2:e63.10.1186/2191-0855-2-63
   Google Scholar
• Lynd LR, van Zyl WH, Mcbride JE, et al. Consolidated bioprocessing of cellulosic biomass: an update. Curr. Opin. Biotechnol. 2005;16:577–583.10.1016/j.copbio.2005.08.009
   PubMed Web of Science ®Google Scholar
• Murai T, Ueda M, Yamamura M, et al. Construction of a starch-utilizing yeast by cell surface engineering. Appl. Environ. Microbiol. 1997;63:1362–1366.
   PubMed Web of Science ®Google Scholar
• Murai T, Ueda M, Shibasaki Y, et al. Development of an arming yeast strain for efficient utilization of starch by co-display of sequential amylolytic enzymes on the cell surface. Appl. Microbiol. Biotechnol. 1999;51:65–70.10.1007/s002530051364
   PubMed Web of Science ®Google Scholar
• Shigechi H, Koh J, Fujita Y, et al. Direct production of ethanol from raw corn starch via fermentation by use of a novel surface-engineered yeast strain codisplaying glucoamylase and α-amylase. Appl. Environ. Microbiol. 2004;70:5037–5040.10.1128/AEM.70.8.5037-5040.2004
   PubMed Web of Science ®Google Scholar
• Murai T, Ueda M, Kawaguchi T, et al. Assimilation of cellooligosaccharides by a cell surface-engineered yeast expressing β-glucosidase and carboxymethylcellulase from Aspergillus aculeatus. Appl. Environ. Microbiol. 1998;64:4857–4861.
   PubMed Web of Science ®Google Scholar
• Fujita Y, Ito J, Ueda M, et al. Synergistic saccharification, and direct fermentation to ethanol, of amorphous cellulose by use of an engineered yeast strain codisplaying three types of cellulolytic enzyme. Appl. Environ. Microbiol. 2004;70:1207–1212.10.1128/AEM.70.2.1207-1212.2004
   PubMed Web of Science ®Google Scholar
• Kotaka A, Bando H, Kaya M, et al. Direct ethanol production from barley β-glucan by sake yeast displaying Aspergillus oryzae β-glucosidase and endoglucanase. J. Biosci. Bioeng. 2008;105:622–627.10.1263/jbb.105.622
   PubMed Web of Science ®Google Scholar
• Ito J, Kosugi A, Tanaka T, et al. Regulation of the display ratio of enzymes on the Saccharomyces cerevisiae cell surface by the immunoglobulin g and cellulosomal enzyme binding domains. Appl. Environ. Microbiol. 2009;75:4149–4154.10.1128/AEM.00318-09
   PubMed Web of Science ®Google Scholar
• Yamada R, Taniguchi N, Tanaka T, et al. Cocktail δ-integration: a novel method to construct cellulolytic enzyme expression ratio-optimized yeast strains. Microb. Cell Fact. 2010;9:e32.10.1186/1475-2859-9-32
   PubMed Web of Science ®Google Scholar
• Nakanishi A, Bae J, Kuroda K, et al. Construction of a novel selection system for endoglucanases exhibiting carbohydrate-binding modules optimized for biomass using yeast cell-surface engineering. AMB Express. 2012;2:e56.10.1186/2191-0855-2-56
   Google Scholar
• Bae J, Morisaka H, Kuroda K, et al. Cellulosome complexes – natural biocatalysts as arming micro-compartments of enzymes. J. Molecul. Microbiol. Biotechnol. 2013;23:370–378.
   PubMed Web of Science ®Google Scholar
• Tsai SL, Oh J, Singh S, et al. Functional assembly of minicellulosomes on the Saccharomyces cerevisiae cell surface for cellulose hydrolysis and ethanol production. Appl. Environ. Microbiol. 2009;75:6087–6093.10.1128/AEM.01538-09
   PubMed Web of Science ®Google Scholar
• Goyal G, Tsai SL, Madan B, et al. Simultaneous cell growth and ethanol production from cellulose by an engineered yeast consortium displaying a functional mini-cellulosome. Microb. Cell Fact. 2011;10:e89.10.1186/1475-2859-10-89
   PubMedGoogle Scholar
• Bae J, Kuroda K, Ueda M. Proximity effect between cellulose-degrading enzymes displayed on the Saccharomyces cerevisiae cell surface. Appl. Environ. Microbiol. 2015;81:59–66.10.1128/AEM.02864-14
   PubMed Web of Science ®Google Scholar
• Matsui K, Bae J, Esaka K, et al. Exoproteome profiles of Clostridium cellulovorans on various carbon sources. Appl. Environ. Microbiol. 2013;79:6576–6584.10.1128/AEM.02137-13
   PubMed Web of Science ®Google Scholar
• Esaka K, Aburaya S, Morisaka H, et al. Exoproteome analysis of Clostridium cellulovorans in natural soft-biomass degradation. AMB Express. 2015;5:2.10.1186/s13568-014-0089-9
   PubMed Web of Science ®Google Scholar
• Aburaya S, Esaka K, Morisaka H, et al. Elucidation of the recognition mechanisms for hemicellulose and pectin in Clostridium cellulovorans using intracellular quantitative proteome analysis. AMB Express. 2015;5:29.10.1186/s13568-015-0115-6
   PubMed Web of Science ®Google Scholar
• Katahira S, Fujita Y, Mizuike A, et al. Construction of a xylan-fermenting yeast strain through codisplay of xylanolytic enzymes on the surface of xylose-utilizing Saccharomyces cerevisiae cells. Appl. Environ. Microbiol. 2004;70:5407–5414.10.1128/AEM.70.9.5407-5414.2004
   PubMed Web of Science ®Google Scholar
• Katahira S, Mizuike A, Fukuda H, et al. Ethanol fermentation from lignocellulosic hydrolysate by a recombinant xylose- and cellooligosaccharide-assimilating yeast strain. Appl. Microbiol. Biotechnol. 2006;72:1136–1143.10.1007/s00253-006-0402-x
   PubMed Web of Science ®Google Scholar
• Ota M, Sakuragi H, Morisaka H, et al. Display of Clostridium cellulovorans xylose isomerase on the cell surface of Saccharomyces cerevisiae and its direct application to xylose fermentation. Biotechnol. Prog. 2013;29:346–351.10.1002/btpr.1700
   PubMed Web of Science ®Google Scholar
• Nakanishi A, Bae JG, Fukai K, et al. Effect of pretreatment of hydrothermally processed rice straw with laccase-displaying yeast on ethanol fermentation. Appl. Microbiol. Biotechnol. 2012;94:939–948.10.1007/s00253-012-3876-8
   PubMed Web of Science ®Google Scholar
• Takagi T, Morisaka H, Aburaya S, et al. Putative alginate assimilation process of the marine bacterium Saccharophagus degradans 2-40 based on quantitative proteome analysis. Mar. Biotechnol. 2016;18:15–23.
   PubMedGoogle Scholar
• Takagi T, Yokoi T, Shibata T, et al. Engineered yeast whole-cell biocatalyst for direct degradation of alginate from macroalgae and production of non-commercialized useful monosaccharide from alginate. Appl. Microbiol. Biotechnol. 2016;100;1723–1732.
   PubMed Web of Science ®Google Scholar
• Shiraga S, Kawakami M, Ishiguro M, et al. Enhanced reactivity of Rhizopus oryzae lipase displayed on yeast cell surfaces in organic solvents: potential as a whole-cell biocatalyst in organic solvents. Appl. Environ. Microbiol. 2005;71:4335–4338.10.1128/AEM.71.8.4335-4338.2005
   PubMed Web of Science ®Google Scholar
• Nakamura Y, Matsumoto T, Nomoto F, et al. Enhancement of activity of lipase-displaying yeast cells and their application to optical resolution of (R,S)-1-benzyloxy-3-chloro-2-propyl monosuccinate. Biotechnol. Prog. 2006;22:998–1002.10.1021/bp060136m
   PubMed Web of Science ®Google Scholar
• Kato M, Fuchimoto J, Tanino T, et al. Preparation of a whole-cell biocatalyst of mutated Candida antarctica lipase B (mCALB) by a yeast molecular display system and its practical properties. Appl. Microbiol. Biotechnol. 2007;75:549–555.10.1007/s00253-006-0835-2
   PubMed Web of Science ®Google Scholar
• Inaba C, Maekawa K, Morisaka H, et al. Efficient synthesis of enantiomeric ethyl lactate by Candida antarctica lipase B (CALB)-displaying yeasts. Appl. Microbiol. Biotechnol. 2009;83:859–864.10.1007/s00253-009-1931-x
   PubMed Web of Science ®Google Scholar
• Tanino T, Aoki T, Chung WY, et al. Improvement of a Candida antarctica lipase B-displaying yeast whole-cell biocatalyst and its application to the polyester synthesis reaction. Appl. Microbiol. Biotechnol. 2009;82:59–66.10.1007/s00253-008-1764-z
   PubMed Web of Science ®Google Scholar
• Tanino T, Ohno T, Aoki T, et al. Development of yeast cells displaying Candida antarctica lipase B and their application to ester synthesis reaction. Appl. Microbiol. Biotechnol. 2007;75:1319–1325.10.1007/s00253-007-0959-z
   PubMed Web of Science ®Google Scholar
• Han SY, Pan ZY, Huang DF, et al. Highly efficient synthesis of ethyl hexanoate catalyzed by CALB-displaying Saccharomyces cerevisiae whole-cells in non-aqueous phase. J. Mol. Catal. B. 2009;59:168–172.10.1016/j.molcatb.2009.02.007
   Web of Science ®Google Scholar
• Su GD, Huang DF, Han SY, et al. Display of Candida antarctica lipase B on Pichia pastoris and its application to flavor ester synthesis. Appl. Microbiol. Biotechnol. 2010;86:1493–1501.10.1007/s00253-009-2382-0
   PubMed Web of Science ®Google Scholar
• Jiang Z, Gao B, Ren R, et al. Efficient display of active lipase LipB52 with a Pichia pastoris cell surface display system and comparison with the LipB52 displayed on Saccharomyces cerevisiae cell surface. BMC Biotechnol. 2008;8:e4.10.1186/1472-6750-8-4
   Google Scholar
• Jiang ZB, Song HT, Gupta N, et al. Cell surface display of functionally active lipases from Yarrowia lipolytica in Pichia pastoris. Protein Expr. Purif. 2007;56:35–39.10.1016/j.pep.2007.07.003
   PubMed Web of Science ®Google Scholar
• Kaya M, Ito J, Kotaka A, et al. Isoflavone aglycones production from isoflavone glycosides by display of β-glucosidase from Aspergillus oryzae on yeast cell surface. Appl. Microbiol. Biotechnol. 2008;79:51–60.10.1007/s00253-008-1393-6
   PubMed Web of Science ®Google Scholar
• Inaba C, Higuchi S, Morisaka H, et al. Synthesis of functional dipeptide carnosine from nonprotected amino acids using carnosinase-displaying yeast cells. Appl. Microbiol. Biotechnol. 2010;86:1895–1902.10.1007/s00253-009-2396-7
   PubMed Web of Science ®Google Scholar
• Fukuda T, Isogawa D, Takagi M, et al. Yeast cell-surface expression of chitosanase from Paenibacillus fukuinensis. Biosci. Biotechnol. Biochem. 2007;71:2845–2847.10.1271/bbb.70315
   PubMed Web of Science ®Google Scholar
• Isogawa D, Morisaka H, Kuroda K, et al. Evaluation of chitosan-binding amino acid residues of chitosanase from Paenibacillus fukuinensis. Biosci. Biotechnol. Biochem. 2014;78:1177–1182.10.1080/09168451.2014.917263
   PubMed Web of Science ®Google Scholar
• Kotrba P, Ruml T. Surface display of metal fixation motifs of bacterial P1-type ATPases specifically promotes biosorption of Pb2+ by Saccharomyces cerevisiae. Appl. Environ. Microbiol. 2010;76:2615–2622.10.1128/AEM.01463-09
   PubMed Web of Science ®Google Scholar
• Kuroda K, Shibasaki S, Ueda M, et al. Cell surface-engineered yeast displaying a histidine oligopeptide (hexa-His) has enhanced adsorption of and tolerance to heavy metal ions. Appl. Microbiol. Biotechnol. 2001;57:697–701.10.1007/s002530100813
   PubMed Web of Science ®Google Scholar
• Kuroda K, Ueda M. Bioadsorption of cadmium ion by cell surface-engineered yeasts displaying metallothionein and hexa-His. Appl. Microbiol. Biotechnol. 2003;63:182–186.10.1007/s00253-003-1399-z
   PubMed Web of Science ®Google Scholar
• Kuroda K, Ueda M. Effective display of metallothionein tandem repeats on the bioadsorption of cadmium ion. Appl. Microbiol. Biotechnol. 2006;70:458–463.10.1007/s00253-005-0093-8
   PubMed Web of Science ®Google Scholar
• Satomura A, Kuroda K, Ueda M. Environmental stress tolerance engineering by modification of cell surface and transcription factor in Saccharomyces cerevisiae. Cur. Environ. Eng. 2014;1:149–156.
   Google Scholar
• Grunden AM, Ray RM, Rosentel JK, et al. Repression of the Escherichia coli modABCD (molybdate transport) operon by ModE. J. Bacteriol. 1996;178:735–744.
   PubMed Web of Science ®Google Scholar
• Nishitani T, Shimada M, Kuroda K, et al. Molecular design of yeast cell surface for adsorption and recovery of molybdenum, one of rare metals. Appl. Microbiol. Biotechnol. 2010;86:641–648.10.1007/s00253-009-2304-1
   PubMed Web of Science ®Google Scholar
• Kuroda K, Nishitani T, Ueda M. Specific adsorption of tungstate by cell surface display of the newly designed ModE mutant. Appl. Microbiol. Biotechnol. 2012;96:153–159.10.1007/s00253-012-4069-1
   PubMed Web of Science ®Google Scholar
• Kuroda K, Ebisutani K, Iida K, et al. Enhanced adsorption and recovery of uranyl ions by NikR mutant-displaying yeast. Biomolecules. 2014;4:390–401.10.3390/biom4020390
   PubMedGoogle Scholar
• Yasui M, Shibasaki S, Kuroda K, et al. An arming yeast with the ability to entrap fluorescent 17β-estradiol on the cell surface. Appl. Microbiol. Biotechnol. 2002;59:329–331.
   PubMed Web of Science ®Google Scholar
• Fukuda T, Tsuchiyama K, Makishima H, et al. Improvement in organophosphorus hydrolase activity of cell surface-engineered yeast strain using Flo1p anchor system. Biotechnol. Lett. 2010;32:655–659.10.1007/s10529-010-0204-1
   PubMed Web of Science ®Google Scholar
• Takayama K, Suye S, Kuroda K, et al. Surface display of organophosphorus hydrolase on Saccharomyces cerevisiae. Biotechnol. Prog. 2006;22:939–943.10.1021/bp060107b
   PubMed Web of Science ®Google Scholar
• Fukuda T, Tsuchiya K, Makishima H, et al. Organophosphorus compound detection on a cell chip with yeast coexpressing hydrolase and eGFP. Biotechnol. J. 2010;5:515–519.10.1002/biot.200900292
   PubMed Web of Science ®Google Scholar
• Takayama K, Suye S, Tanaka Y, et al. Estimation of enzyme kinetic parameters of cell surface-displayed organophosphorus hydrolase and construction of a biosensing system for organophosphorus compounds. Anal. Sci. 2011;27:823–826.10.2116/analsci.27.823
   PubMed Web of Science ®Google Scholar
• Shibasaki S, Ueda M, Ye K, et al. Creation of cell surface-engineered yeast that display different fluorescent proteins in response to the glucose concentration. Appl. Microbiol. Biotechnol. 2001;57:528–533.
   PubMed Web of Science ®Google Scholar
• Shibasaki S, Ninomiya Y, Ueda M, et al. Intelligent yeast strains with the ability to self-monitor the concentrations of intra- and extracellular phosphate or ammonium ion by emission of fluorescence from the cell surface. Appl. Microbiol. Biotechnol. 2001;57:702–707.
   PubMed Web of Science ®Google Scholar
• Shibasaki S, Tanaka A, Ueda M. Development of combinatorial bioengineering using yeast cell surface display—order-made design of cell and protein for bio-monitoring. Biosens. Bioelectron. 2003;19:123–130.10.1016/S0956-5663(03)00169-6
   PubMed Web of Science ®Google Scholar
• Tamaru Y, Ohtsuka M, Kato K, et al. Application of the arming system for the expression of the 380R antigen from red sea bream iridovirus (RSIV) on the surface of yeast cells: a first step for the development of an oral vaccine. Biotechnol. Prog. 2006;22:949–953.10.1021/bp060130x
   PubMed Web of Science ®Google Scholar
• Shigemori T, Nagayama M, Yamada J, et al. Construction of a convenient system for easily screening inhibitors of mutated influenza virus neuraminidases. FEBSOpenBio. 2013;3:484–489.
   Google Scholar
• Yamada J, Miura N, Shigemori T, et al Application of cell surface engineered yeast for the development of drugs against influenza virus infection. In Bishop RH, editor. Influenza viruses: epidemiology, detection and management. New York (NY): Nova Science Publisher; 2014. p. 91–110.
   Google Scholar
• Wasilenko JL, Sarmento L, Spatz S, et al. Cell surface display of highly pathogenic avian influenza virus hemagglutinin on the surface of Pichia pastoris cells using α-agglutinin for production of oral vaccines. Biotechnol. Prog. 2010;26:542–547.
   PubMed Web of Science ®Google Scholar
• Lin Y, Tsumuraya T, Wakabayashi T, et al. Display of a functional hetero-oligomeric catalytic antibody on the yeast cell surface. Appl. Microbiol. Biotechnol. 2003;62:226–232.10.1007/s00253-003-1283-x
   PubMed Web of Science ®Google Scholar
• Lin Y, Shiraga S, Tsumuraya T, et al. Comparison of two forms of catalytic antibody displayed on yeast-cell surface. J. Mol. Catal. B. 2004;28:241–246.10.1016/j.molcatb.2003.12.021
   Web of Science ®Google Scholar
• Okochi N, Kato M, Kadonosono T, et al. Design of a serine protease-like catalytic triad on an antibody light chain displayed on the yeast cell surface. Appl. Microbiol. Biotechnol. 2007;77:597–603.10.1007/s00253-007-1197-0
   PubMed Web of Science ®Google Scholar
• Nakamura Y, Shibasaki S, Ueda M, et al. Development of novel whole-cell immunoadsorbents by yeast surface display of the IgG-binding domain. Appl. Microbiol. Biotechnol. 2001;57:500–505.
   PubMed Web of Science ®Google Scholar
• Matsui K, Kuroda K, Ueda M. Creation of a novel peptide endowing yeasts with acid tolerance using yeast cell-surface engineering. Appl. Microbiol. Biotechnol. 2009;82:105–113.10.1007/s00253-008-1761-2
   PubMed Web of Science ®Google Scholar
• Zou W, Ueda M, Yamanaka H, et al. Construction of a combinatorial protein library displayed on yeast cell surface using DNA random priming method. J. Biosci. Bioeng. 2001;92:393–396.10.1016/S1389-1723(01)80246-2
   PubMed Web of Science ®Google Scholar
• Zou W, Ueda M, Tanaka A. Screening of a molecule endowing Saccharomyces cerevisiae with n-nonane-tolerance from a combinatorial random protein library. Appl. Microbiol. Biotechnol. 2002;58:806–812.
   PubMed Web of Science ®Google Scholar
• Andreu C, del Olmo M. Yeast arming by the Aga2p system: effect of growth conditions in galactose on the efficiency of the display and influence of expressing leucine-containing peptides. Appl. Microbiol. Biotechnol. 2013;97:9055–9069.10.1007/s00253-013-5086-4
   PubMed Web of Science ®Google Scholar
• Shiraga S, Ishiguro M, Fukami H, et al. Creation of Rhizopus oryzae lipase having a unique oxyanion hole by combinatorial mutagenesis in the lid domain. Appl. Microbiol. Biotechnol. 2005;68:779–785.10.1007/s00253-005-1935-0
   PubMed Web of Science ®Google Scholar
• Kadonosono T, Kato M, Ueda M. Alteration of substrate specificity of rat neurolysin from matrix metalloproteinase-2/9-type to -3-type specificity by comprehensive mutation. Protein Eng. Des. Sel. 2008;21:507–513.10.1093/protein/gzn026
   PubMed Web of Science ®Google Scholar
• Fushimi T, Miura N, Shintani H, et al. Mutant firefly luciferases with improved specific activity and dATP discrimination constructed by yeast cell surface engineering. Appl. Microbiol. Biotechnol. 2013;97:4003–4011.10.1007/s00253-012-4467-4
   PubMed Web of Science ®Google Scholar
• Miura N, Kuroda K, Ueda M. Enzyme evolution by yeast cell surface engineering. Methods Mol. Biol. 2015;217–232.10.1007/978-1-4939-2748-7
   PubMedGoogle Scholar
• Fukuda T, Kato M, Suye S, et al. Development of high-throughput screening system by single cell reaction using microchamber array chip. J. Biosci. Bioeng. 2007;104:241–243.10.1263/jbb.104.241
   PubMed Web of Science ®Google Scholar
• van den Beucken T, Pieters H, Steukers M, et al. Affinity maturation of Fab antibody fragments by fluorescent-activated cell sorting of yeast-displayed libraries. FEBS Lett. 2003;546:288–294.10.1016/S0014-5793(03)00602-1
   PubMed Web of Science ®Google Scholar
• Rajpal A, Beyaz N, Haber L, et al. A general method for greatly improving the affinity of antibodies by using combinatorial libraries. Proc. Natl. Acad. Sci. USA. 2005;102:8466–8471.10.1073/pnas.0503543102
   PubMed Web of Science ®Google Scholar
• Graff CP, Chester K, Begent R, et al. Directed evolution of an anti-carcinoembryonic antigen scFv with a 4-day monovalent dissociation half-time at 37oC. Protein Eng. Des. Sel. 2004;17:293–304.10.1093/protein/gzh038
   PubMed Web of Science ®Google Scholar
• Razai A, Garcia-Rodriguez C, Lou J, et al. Molecular evolution of antibody affinity for sensitive detection of botulinum neurotoxin type A. J. Mol. Biol. 2005;351:158–169.10.1016/j.jmb.2005.06.003
   PubMed Web of Science ®Google Scholar
• VanAntwerp JJ, Wittrup KD. Thermodynamic characterization of affinity maturation: the D1.3 antibody and a higher-affinity mutant. J. Mol. Recognit. 1998;11:10–13.10.1002/(ISSN)1099-1352
   PubMed Web of Science ®Google Scholar
• Wang Z, Kim GB, Woo JH, et al. Improvement of a recombinant anti-monkey anti-CD3 diphtheria toxin based immunotoxin by yeast display affinity maturation of the scFv. Bioconjug. Chem. 2007;18:947–955.10.1021/bc0603438
   PubMed Web of Science ®Google Scholar
• Ueda M. Revolutionary protein engineering using molecular display. In: Protein engineering: design, selection, and applications. New York (NY): Nova Science Publisher; 2011. p. 73–80.
   Google Scholar
• Kuroda K, Ueda M. Arming technology in yeast—novel strategy for whole-cell biocatalyst and protein engineering. Biomolecules. 2013;3:632–650.10.3390/biom3030632
   PubMedGoogle Scholar