Virus scaffolds as enzyme nano-carriers

Trends in Biotechnology

Volumn 30, Issue 7, 2012, Pages 369-376

  Cardinale, Daniela ^a,b   Carette, Noëlle ^a,b   Michon, Thierry ^a,b  

^a Univ Bordeaux   (France)

^b UNIVERSITÉ DE BORDEAUX   (France)

Author keywords

Bacteriophage; Enzyme nano carrier; Enzyme selection; Virus scaffold; Virus like particle

Indexed keywords

BUILDING BLOCKES; COOPERATIVE ORGANIZATION; ENZYME SELECTION; KEY FEATURE; KINETICS STUDIES; LIVING SYSTEMS; MATERIAL PROCESSING; NANOCARRIERS; NANOSCALE RESOLUTIONS; PHAGE THERAPY; PLANT VIRUS; PROTEIN MONOMERS; SINGLE MOLECULE; SOLID SUPPORTS; VIRUS CAPSID; VIRUS-LIKE PARTICLES;

BACTERIOPHAGES; ENZYME KINETICS; NANOTECHNOLOGY;

SCAFFOLDS (BIOLOGY);

CAPSID PROTEIN; ENZYME; LIPASE B; MOLECULAR SCAFFOLD; NANOCARRIER; TISSUE PLASMINOGEN ACTIVATOR; UNCLASSIFIED DRUG; VIRUS SCAFFOLD;

BACILLUS LICHENIFORMIS; BACTERIOPHAGE; CANDIDA ANTARCTICA; CELL MEMBRANE; ENZYME KINETICS; MURINE LEUKEMIA VIRUS; NONHUMAN; PHAGE DISPLAY; PLANT VIRUS; POTEXVIRUS; PRIORITY JOURNAL; REVIEW; RNA SEQUENCE; VIRUS CAPSID; VIRUS LIKE AGENT; VIRUS PARTICLE; VIRUS RELEASE; WILD TYPE;

ANIMALS; BACTERIOPHAGES; BIOTECHNOLOGY; CAPSID; CLONING, MOLECULAR; ENZYMES; GENETIC ENGINEERING; HUMANS; NANOSTRUCTURES; NANOTECHNOLOGY; PLANT VIRUSES; VIRION;

MIRIDAE;

EID: 84862335730     PISSN: 01677799     EISSN: 18793096     Source Type: Journal    
DOI: 10.1016/j.tibtech.2012.04.001     Document Type: Review

References (42)

1. Lee K.B., et al. Protein nanostructures formed via direct-write dip-pen nanolithography. J. Am. Chem. Soc. 2003, 125:5588-5589.
2. Sacca B., et al. Orthogonal protein decoration of DNA origami. Angew Chem. Int. Ed. Engl. 2010, 49:9378-9383.
3. Bacteriophages: Genetics and Molecular Biology 2007, Caister Academic Press. S. McGrath, D. Sinderen (Eds.).
4. Phage Display: a Laboratory Manual 2001, Cold Spring Harbor Laboratory Press. C.F. Barbas (Ed.).
5. Fernandez-Gacio A., et al. Phage display as a tool for the directed evolution of enzymes. Trends Biotechnol. 2003, 21:408-414.
6. Boersma Y.L., et al. Selection strategies for improved biocatalysts. FEBS J. 2007, 274:2181-2195.
7. Sunbul M., et al. Enzyme-catalyzed substrate attachment to phage surfaces for the selection of catalytic activities. ChemBioChem 2011, 12:380-386.
8. Shukla G.S., Krag D.N. Cancer cell-specific internalizing ligands from phage displayed beta-lactamase-peptide fusion libraries. Protein Eng. Des. Sel. 2010, 23:431-440.
9. Shukla G.S., Krag D.N. Phage-displayed combinatorial peptide libraries in fusion to beta-lactamase as reporter for an accelerated clone screening: Potential uses of selected enzyme-linked affinity reagents in downstream applications. Comb. Chem. High Throughput Screen 2010, 13:75-87.
10. Shukla G.S., Krag D.N. Novel beta-lactamase-random peptide fusion libraries for phage display selection of cancer cell-targeting agents suitable for enzyme prodrug therapy. J. Drug Target 2010, 18:115-124.
11. Breidenstein E.B., et al. Pseudomonas aeruginosa: all roads lead to resistance. Trends Microbiol. 2011, 19:419-426.
12. Collins, J.J. et al. (2006) Engineered enzymatically active bacteriophages and methods of uses thereof, WO 2006/137847.
13. Sutherland I.W., et al. The interaction of phage and biofilms. FEMS Microbiol. Lett. 2004, 232:1-6.
14. Zachariou, M. et al. (2006) Bacteriophages displaying functional enzymes and uses thereof, WO/2006/034554.
15. Granieri L., et al. High-throughput screening of enzymes by retroviral display using droplet-based microfluidics. Chem. Biol. 2010, 17:229-235.
16. Canizares M.C., et al. Use of viral vectors for vaccine production in plants. Immunol. Cell Biol. 2005, 83:263-270.
17. Werner S., et al. Immunoabsorbent nanoparticles based on a tobamovirus displaying protein A. Proc. Natl. Acad. Sci. U.S.A. 2006, 103:17678-17683.
18. Donnelly M.L., et al. Analysis of the aphthovirus 2A/2B polyprotein 'cleavage' mechanism indicates not a proteolytic reaction, but a novel translational effect: a putative ribosomal 'skip'. J. Gen. Virol. 2001, 82:1013-1025.
19. Cruz S.S., et al. Assembly and movement of a plant virus carrying a green fluorescent protein overcoat. Proc. Natl. Acad. Sci. U.S.A. 1996, 93:6286-6290.
20. Uhde-Holzem K., et al. Immunogenic properties of chimeric potato virus X particles displaying the hepatitis C virus hypervariable region I peptide R9. J. Virol. Methods 2010, 166:12-20.
21. Carette N., et al. A virus-based biocatalyst. Nat. Nanotechnol. 2007, 2:226-229.
22. Smith M.L., et al. Modified tobacco mosaic virus particles as scaffolds for display of protein antigens for vaccine applications. Virology 2006, 348:475-488.
23. Fiedler J.D., et al. RNA-directed packaging of enzymes within virus-like particles. Angew Chem. Int. Ed. Engl. 2010, 49:9648-9651.
24. O'Neil A., et al. Genetically programmed in vivo packaging of protein cargo and its controlled release from bacteriophage P22. Angew Chem. Int. Ed. Engl. 2011, 50:7425-7428.
25. Ashley C.E., et al. Cell-specific delivery of diverse cargos by bacteriophage MS2 virus-like particles. ACS Nano 2011, 5:5729-5745.
26. Beauchemin C., et al. Simultaneous production of two foreign proteins from a polyvirus-based vector. Virus Res. 2005, 112:1-8.
27. Wang Z., et al. Positional effect of gene insertion on genetic stability of a clover yellow vein virus-based expression vector. J. Gen. Plant Pathol. 2003, 69:327-334.
28. Vega R.A., et al. Nanoarrays of single virus particles. Angew Chem. Int. Ed. Engl. 2005, 44:6013-6015.
29. Moon J.M., et al. Capture and alignment of phi29 viral particles in sub-40 nanometer porous alumina membranes. Biomed. Microdevices 2009, 11:135-142.
30. Dague E., et al. Assembly of live micro-organisms on microstructured PDMS stamps by convective/capillary deposition for AFM bio-experiments. Nanotechnology 2011, 22:395102.
31. Cerfa A., et al. A versatile method for generating single DNA molecule patterns: through the combination of directed capillary assembly and (micro/nano) contact printing. J. Mater. Res. 2011, 26:336-346.
32. Suttle C.A. Viruses in the sea. Nature 2005, 437:356-361.
33. Rice G., et al. The structure of a thermophilic archaeal virus shows a double-stranded DNA viral capsid type that spans all domains of life. Proc. Natl. Acad. Sci. U.S.A. 2004, 101:7716-7720.
34. Link A.J., et al. Non-canonical amino acids in protein engineering. Curr. Opin. Biotechnol. 2003, 14:603-609.
35. Strable E., et al. Unnatural amino acid incorporation into virus-like particles. Bioconjug. Chem. 2008, 19:866-875.
36. Steinmetz N.F., Evans D.J. Utilisation of plant viruses in bionanotechnology. Org. Biomol. Chem. 2007, 5:2891-2902.
37. Litowski J.R., Hodges R.S. Designing heterodimeric two-stranded alpha-helical coiled-coils. Effects of hydrophobicity and alpha-helical propensity on protein folding, stability, and specificity. J. Biol. Chem. 2002, 277:37272-37279.
38. Minten I.J., et al. Catalytic capsids: the art of confinement. Chem. Sci. 2011, 2:358-362.
39. Minten I.J., et al. Controlled encapsulation of multiple proteins in virus capsids. J. Am. Chem. Soc. 2009, 131:17771-17773.
40. Minten I.J., et al. Complex assembly behavior during the encapsulation of green fluorescent protein analogs in virus derived protein capsules. Macromol. Biosci. 2010, 10:539-545.
41. Henzler-Wildman K.A., et al. A hierarchy of timescales in protein dynamics is linked to enzyme catalysis. Nature 2007, 450:913-916.
42. Comellas-Aragonès M., et al. A virus-based single-enzyme nanoreactor. Nat. Nanotech. 2007, 2:635-639.