Versatile microbial surface-display for environmental remediation and biofuels production

Trends in Microbiology

Volumn 16, Issue 4, 2008, Pages 181-188

  Wu, Cindy H ^a   Mulchandani, Ashok ^b   Chen, Wilfred ^b  

^a LAWRENCE BERKELEY NATIONAL LABORATORY   (United States)

^b University of California Riverside   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOFUEL;

BACILLUS SUBTILIS; BACTERIAL SPORE; BIOFUEL PRODUCTION; BIOREMEDIATION; COMBINATORIAL CHEMISTRY; DETOXIFICATION; DISPLAY SYSTEM; GRAM NEGATIVE BACTERIUM; GRAM POSITIVE BACTERIUM; MAGNETOSPIRILLUM; METAL BINDING; ORGANIC POLLUTION; PLASMODIUM BERGHEI; POLLUTION CONTROL; PRIORITY JOURNAL; PROTEIN ENGINEERING; PROTEIN MOTIF; REVIEW; SURFACE DISPLAY; XENOBIOTIC METABOLISM;

BACTERIAL PROTEINS; BIOTECHNOLOGY; BUTANOLS; COMBINATORIAL CHEMISTRY TECHNIQUES; ENVIRONMENTAL REMEDIATION; ETHANOL; FUNGAL PROTEINS; GRAM-NEGATIVE BACTERIA; GRAM-POSITIVE BACTERIA; MEMBRANE PROTEINS; PROTEIN ENGINEERING; RECOMBINANT PROTEINS; YEASTS;

NEGIBACTERIA; POSIBACTERIA;

EID: 41549136380     PISSN: 0966842X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tim.2008.01.003     Document Type: Review

References (80)

1. Smith G.P. Filamentous fusion phage: novel expression vectors that display cloned antigens on the virion surface. Science 228 (1985) 1315-1317
2. Charbit A., et al. Probing the topology of a bacterial membrane protein by genetic insertion of a foreign epitope; expression at the cell surface. EMBO J. 5 (1986) 3029-3037
3. Becker S., et al. Ultra-high-throughput screening based on cell-surface display and fluorescence-activated cell sorting for the identification of novel biocatalysts. Curr. Opin. Biotechnol. 15 (2004) 323-329
4. Desvaux M., et al. Protein cell surface display in Gram-positive bacteria from single protein to macromolecular protein structure. FEMS Microbiol. Lett. 256 (2006) 1-15
5. Jose J. Autodisplay: efficient bacterial surface display of recombinant proteins. Appl. Microbiol. Biotechnol. 69 (2006) 607-614
6. Lee S.Y., et al. Microbial cell-surface display. Trends Biotechnol. 21 (2003) 45-52
7. Paterson G.K., and Mitchell T.J. The biology of Gram-positive sortase enzymes. Trends Microbiol. 12 (2007) 89-95
8. Wernerus H., and Stahl S. Biotechnological applications for surface-engineered bacteria. Biotechnol. Appl. Biochem. 40 (2004) 209-228
9. Bae W., et al. Enhanced bioaccumulation of heavy metals by bacterial cells displaying synthetic phytochelatins. Biotechnol. Bioeng. 70 (2000) 518-524
10. Bae W., et al. Genetic engineering of Escherichia coli for enhanced uptake and bioaccumulation of mercury. Appl. Environ. Microbiol. 67 (2001) 5335-5338
11. Bontidean I., et al. Detection of heavy metal ions at femtomolar levels using protein-based biosensors. Anal. Chem. 70 (1998) 4162-4169
12. O'Halloran T.V., et al. The MerR heavy metal receptor mediates positive activation in a topologically novel transcription complex. Cell 56 (1989) 119-129
13. Bae W., et al. Enhanced mercury biosorption by bacterial cells with surface-displayed MerR. Appl. Environ. Microbiol. 69 (2003) 3176-3180
14. Qin J., et al. Hg(II) sequestration and protection by the MerR metal-binding domain (MBD). Microbiology 152 (2006) 709-719
15. Dong J., et al. Selection of novel nickel-binding peptides from flagella displayed secondary peptide library. Chem Biol Drug Des. 68 (2006) 107-112
16. Kuroda K., and Ueda M. Effective display of metallothionein tandem repeats on the bioadsorption of cadmium ion. Appl. Microbiol. Biotechnol. 70 (2006) 458-463
17. Richins R.D., et al. Biodegradation of organophosphorus pesticides by surface-expressed organophosphorus hydrolase. Nat. Biotechnol. 15 (1997) 984-987
18. Takayama K., et al. Surface display of organophosphorus hydrolase on Saccharomyces cerevisiae. Biotechnol. Prog. 22 (2006) 939-943
19. Shimazu M., et al. Simultaneous degradation of organophosphorus pesticides and p-nitrophenol by a genetically engineered Moraxella sp with surface-expressed organophosphorus hydrolase. Biotechnol. Bioeng. 76 (2001) 318-324
20. Zhang J., et al. Bioremediation of organophosphorus pesticides by surface-expressed carboxylesterase from mosquito on Escherichia coli. Biotechnol. Prog. 20 (2004) 1567-1571
21. Cho C.M.H., et al. Altering the substrate specificity of organophosphorus hydrolase for enhanced hydrolysis of chlorpyrifos. Appl. Environ. Microbiol. 70 (2004) 4681-4685
22. Lei Y., et al. Improved degradation of organophosphorus nerve agents and p-nitrophenol by Pseudomonas putida JS444 with surface-expressed organophosphorus hydrolase. Biotechnol. Prog. 21 (2005) 678-681
23. Shimazu M., et al. Cell surface display of organophosphorus hydrolase in Pseudomonas putida using an ice-nucleation protein anchor. Biotechnol. Prog. 19 (2003) 1612-1614
24. Yang C., et al. Surface display of MPH on Pseudomonas putida JS 4444 using ice nucleation protein and its application in detoxification of organophosphate. Biotechnol. Bioeng. 99 (2008) 30-37
25. Shimazu M., et al. Simultaneous degradation of organophosphorus pesticides and p-nitrophenol by a genetically engineered Moraxella sp. with surface-expressed organophosphorus hydrolase. Biotechnol. Bioeng. 76 (2001) 318-324
26. Yee D.C., et al. Rhizoremediation of trichloroethylene by a recombinant root-colonizing Pseudomonas fluorescens strain expressing toluene ortho-monooxygenase constitutively. Appl. Environ. Microbiol. 64 (1998) 112-118
27. Lee W., et al. Engineering TCE-degrading rhizobacteria for heavy metal accumulation and enhanced TCE degradation. Biotechnol. Bioeng. 95 (2006) 399-403
28. Wu C.H., et al. Engineering plant-microbe symbiosis for rhizoremediation of heavy metal. Appl. Environ. Microbiol. 72 (2006) 1129-1134
29. Wang Z., et al. Engineering of cyclodextrin glucanotransferase on the cell surface of Saccharomyces cerevisiae for improved cyclodextrin production. Appl. Environ. Microbiol. 72 (2006) 1873-1877
30. Biwer A., et al. Enzymatic production of cyclodextrins. Appl. Microbiol. Biotechnol. 59 (2002) 609-617
31. Ehsan S., et al. Simultaneous mobilization of heavy metals and polychlorinated biphenyl (PCB) compounds from soil with cyclodextrin and EDTA in admixture. Chemosphere 68 (2007) 150-158
32. Goldemberg J. Ethanol for a sustainable energy future. Science 315 (2007) 808-810
33. Stephanopoulos G. Challenges in engineering microbes for biofuels production. Science 315 (2007) 801-804
34. Keller F.A., et al. Microbial pretreatment of biomass. Appl. Biochem. Biotechnol. 105 (2003) 27-41
35. Lynd L.R., et al. Consolidated bioprocessing of cellulosic biomass: an update. Curr. Opin. Biotechnol. 16 (2005) 577-583
36. Pack S.P., et al. Enhancement of β-glucosidase stability and cellobiose-usage using surface-engineered recombinant Saccharomyces cerevisiae in ethanol production. Biotechnol. Lett. 24 (2002) 1919-1925
37. Fujita Y., et al. Direct and efficient production of ethanol from cellulosic material with a yeast strain displaying cellulolytic enzymes. Appl. Environ. Microbiol. 68 (2002) 5136-5141
38. Katahira S., et al. Ethanol fermentation from lignocellulosic hydrolysate by a recombinant xylose- and celluloligosaccharide-assimilating yeast strain. Appl. Microbiol. Biotechnol. 72 (2006) 1136-1143
39. Kondo A., et al. High-level ethanol production from starch by a flocculent Saccharomyces cerevisiae strain displaying cell-surface glucoamylase. Appl. Microbiol. Biotechnol. 58 (2002) 291-296
40. Shigechi H., et al. Efficient ethanol production from starch through development of novel flocculent yeast strains displaying glucoamylase and co-displaying or secreting α-amylase. J. Mol. Catal. B: Enzym. 17 (2002) 179-187
41. Shigechi H., et al. Energy-saving direct ethanol production from low-temperature-cooked corn starch using a cell-surface engineered yeast strain co-displaying glucoamylase and α-amylase. Biochem. Eng. J. 18 (2004) 149-153
42. Fujita Y., et al. Construction of whole-cell biocatalyst for xylan degradation through cell-surface xylanase display in Saccharomyces cerevisiae. J. Mol. Catal. B: Enzym. 17 (2002) 189-195
43. Katahira S., 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. 70 (2004) 5407-5414
44. Shigechi H., 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. 70 (2004) 5037-5040
45. Yanase H., et al. Genetic engineering of Zymobacter palmae for production of ethanol from xylose. Appl. Environ. Microbiol. 73 (2007) 2592-2599
46. Pohlner J., et al. Gene structure and extracellular secretion of Neisseria gonorrhoeae IgA protease. Nature 325 (1987) 458-462
47. Jose J., et al. Bacterial surface display library screening by target enzyme labeling: identification of new human cathepsin G inhibitors. Anal. Biochem. 346 (2005) 258-267
48. Becker S., et al. A generic system for the Escherichia coli cell-surface display of lipolytic enzymes. FEBS Lett. 579 (2005) 1177-1182
49. Wilhelm S., et al. Functional cell-surface display of a lipase-specific chaperone. ChemBioChem. 8 (2007) 55-60
50. Li C.M., et al. Presentation of functional organophosphorus hydrolase fusions on the surface of Escherichia coli by the AIDA-I autotransporter pathway. Biotechnol. Bioeng. 99 (2008) 485-490
51. Majander K., et al. Simultaneous display of multiple foreign peptides in the FliD capping and FliC filament proteins of the Escherichia coli flagellum. Appl. Environ. Microbiol. 71 (2005) 4263-4268
52. Bingle W.H., et al. The extreme N-terminus of the Caulobacter crescentus surface-layer protein directs export of passenger proteins from the cytoplasm but is not required for secretion of the native protein. Can. J. Microbiol. 42 (1996) 672-684
53. Nomellini J.F., et al. S-layer-mediated display of the immunoglobulin G-binding domain of streptococcal protein G on the surface of Caulobacter crescentus: development of an immunoactive reagent. Appl. Environ. Microbiol. 73 (2007) 3245-3253
54. Breinig F., et al. Cell surface expression of bacterial esterase A by Saccharomyces cerevisiae and its enhancement by constitutive activation of the cellular unfolded protein response. Appl. Environ. Microbiol. 72 (2006) 7140-7147
55. Breinig F., et al. Kre1p, the plasma membrane receptor for the yeast K1 viral toxin. Cell 108 (2002) 395-405
56. Dielbandhoesing S.K., et al. Specific cell wall proteins confer resistance to nisin upon yeast cells. Appl. Environ. Microbiol. 64 (1998) 4047-4052
57. Bony M., et al. Localization and cell surface anchoring of the Saccharomyces cerevisiae flocculation protein Flo1p. J. Bacteriol. 179 (1997) 4929-4936
58. Rice J.J., et al. Bacterial display using circularly permuted outer membrane protein OmpX yields high affinity peptide ligands. Protein Sci. 15 (2006) 825-836
59. Oh S.H., et al. Microfluidic protein detection through genetically engineered bacterial cells. J. Proteome Res. 5 (2006) 3433-3437
60. Tanaka T., et al. Spontaneous integration of transmembrane peptides into a bacterial magnetic particle membrane and its application to display of useful proteins. Anal. Chem. 76 (2004) 3764-3769
61. Sadamoto R., et al. Control of bacteria adhesion by cell-wall engineering. J. Am. Chem. Soc. 126 (2004) 3755-3761
62. Isticato R., et al. Surface display of recombinant proteins on Bacillus subtilis spores. J. Bacteriol. 183 (2001) 6294-6301
63. Uyen N.Q., et al. Enhanced immunization and expression strategies using bacterial spores as heat-stable vaccine delivery vehicles. Vaccine 25 (2007) 356-365
64. Kim J.H., et al. Spore-displayed streptavidin: a live diagnostic tool in biotechnology. Biochem. Biophys. Res. Commun. 331 (2005) 210-214
65. Bosma T., et al. Novel surface display system for proteins on non-genetically modified Gram-positive bacteria. Appl. Environ. Microbiol. 72 (2006) 880-889
66. Yoshino T., et al. Assembly of G protein-coupled receptors onto nanosized bacterial magnetic particles using Mms16 as an anchor molecule. Appl. Environ. Microbiol. 70 (2004) 2880-2885
67. Yoshino T., and Matsunaga T. Efficient and stable display of functional proteins on bacterial magnetic particles using Mms13 as a novel anchor molecule. Appl. Environ. Microbiol. 72 (2006) 465-471
68. Arakaki A., et al. A novel protein tightly bound to bacterial magnetic particles in Magnetospirillum magneticum strain AMB-1. J. Biol. Chem. 278 (2003) 8745-8750
69. Yoshino T., and Matsunaga T. Development of efficient expression system for protein display on bacterial magnetic particles. Biochem. Biophys. Res. Commun. 338 (2005) 1678-1681
70. Wackett L.P. Biocatalysts from environmental microbes. Environ. Microbiol. 8 (2006) 566-567
71. Stemmer W.P.C. Rapid evolution of a protein in vitro by DNA shuffling. Nature 370 (1994) 389-391
72. Lee S.H., et al. Display of bacterial lipase on the Escherichia coli cell surface by using FadL as and anchoring motif and use of the enzyme in enantioselective biocatalysis. Appl. Environ. Microbiol. 70 (2004) 5074-5080
73. van den Berg B. The FadL family: unusual transporters for unusual substrates. Curr. Opin. Struct. Biol. 15 (2005) 401-407
74. Shen H., et al. The mechanism by which over expression of Gts1p induces flocculation in a FLO8-inactive strain of the yeast Saccharomyces cerevisiae. FEMS Yeast Res. 6 (2006) 914-923
75. Li C.M., et al. Type III secretion system-associated pilus of Pseudomonas syringae as an epitope display tool. FEMS Microbiol. Lett. 269 (2007) 104-109
76. Lee S.H., et al. Cell surface display of lipase in Pseudomonas putida KT2442 using OprF as an anchoring motif and its biocatalytic applications. Appl. Environ. Microbiol. 71 (2005) 8581-8586
77. Narita J., et al. Display of α-amylase on the surface of Lactobacillus casei cells by use of the PgsA anchor protein, and production of lactic acid from starch. Appl. Environ. Microbiol. 72 (2006) 269-275
78. Nguyen H.D., and Schumann W. Establishment of an experimental system allowing immobilization of proteins on the surface of Bacillus subtilis cells. J. Biotechnol. 122 (2006) 473-482
79. Swaminathan A., et al. Housekeeping sortase facilitates the cell wall anchoring of pilus polymers in Corynebacterium diphtheriae. Mol. Microbiol. 66 (2007) 961-974
80. Maresso A.W., et al. Surface protein IsdC and sortase B are required for heme-iron scavenging of Bacillus anthracis. J. Bacteriol. 188 (2006) 8145-8152