Packaging protein drugs as bacterial inclusion bodies for therapeutic applications

Microbial Cell Factories

Volumn 11, Issue , 2012, Pages

  Villaverde, Antonio ^a,b   García Fruitós, Elena ^a,b   Rinas, Ursula ^c,d   Seras Franzoso, Joaquin ^a,b   Kosoy, Ana ^e   Corchero, José L ^a,b   Vazquez, Esther ^a,b  

^a UNIVERSITAT AUTÒNOMA DE BARCELONA   (Spain)

^b BIOMATERIALES Y NANOMEDICINA CIBER BBN   (Spain)

^c LEIBNIZ UNIVERSITY HANNOVER   (Germany)

^d HELMHOLTZ CENTRE FOR INFECTION RESEARCH   (Germany)

^e Janus Development SL   (Spain)

Author keywords

[No Author keywords available]

Indexed keywords

CATALASE; CYTOKERATIN 14; DIHYDROFOLATE REDUCTASE; HEAT SHOCK PROTEIN 70; LEUKEMIA INHIBITORY FACTOR; NANOPARTICLE; PROTEIN;

BACTERIAL INCLUSION BODY; BIOCATALYSIS; BIOCOMPATIBILITY; CELL FUNCTION; CELL INCLUSION; CELL MEMBRANE PERMEABILITY; CELL THERAPY; CYTOPLASM; DRUG DELIVERY SYSTEM; DRUG PACKAGING; NONHUMAN; NOTE; NUCLEUS ACCUMBENS; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN TRANSPORT;

BACTERIA; CATALASE; DRUG DELIVERY SYSTEMS; HELA CELLS; HSP70 HEAT-SHOCK PROTEINS; HUMANS; INCLUSION BODIES; KERATIN-14; LEUKEMIA INHIBITORY FACTOR; PROTEINS; RECOMBINANT PROTEINS; TETRAHYDROFOLATE DEHYDROGENASE;

BACTERIA (MICROORGANISMS); MAMMALIA;

EID: 84861975854     PISSN: None     EISSN: 14752859     Source Type: Journal    
DOI: 10.1186/1475-2859-11-76     Document Type: Note

References (44)

1. Jevsevar S, Gaberc-Porekar V, Fonda I, Podobnik B, Grdadolnik J, Menart V. Production of nonclassical inclusion bodies from which correctly folded protein can be extracted. Biotechnol Prog 2005, 21:632-639.
2. Garcia-Fruitos E, Gonzalez-Montalban N, Morell M, Vera A, Ferraz RM, Aris A, et al. Aggregation as bacterial inclusion bodies does not imply inactivation of enzymes and fluorescent proteins. Microb Cell Fact 2005, 4:27.
3. Garcia-Fruitos E, Vazquez E, Diez-Gil C, Corchero JL, Seras-Franzoso J, Ratera I, et al. Bacterial inclusion bodies: making gold from waste. Trends Biotechnol 2012, 30:65-70.
4. Garcia-Fruitos E, Villaverde A. Friendly production of bacterial inclusion bodies. Korean J Chem Eng 2010, 27:385-389.
5. Nahalka J, Nidetzky B. Fusion to a pull-down domain: a novel approach of producingTrigonopsis variabilisD-amino acid oxidase as insoluble enzyme aggregates. Biotechnol Bioeng 2007, 97:454-461.
6. Wu W, Xing L, Zhou B, Lin Z. Active protein aggregates induced by terminally attached self-assembling peptide ELK16 inEscherichia coli. Microb Cell Fact 2011, 10:9.
7. Zhou B, Xing L, Wu W, Zhang XE, Lin Z. Small surfactant-like peptides can drive soluble proteins into active aggregates. Microb Cell Fact 2012, 11:10.
8. Peternel S, Grdadolnik J, Gaberc-Porekar V, Komel R. Engineering inclusion bodies for non denaturing extraction of functional proteins. Microb Cell Fact 2008, 7:34.
9. Vera A, Gonzalez-Montalban N, Aris A, Villaverde A. The conformational quality of insoluble recombinant proteins is enhanced at low growth temperatures. Biotechnol Bioeng 2007, 96:1101-1106.
10. Gonzalez-Montalban N, Garcia-Fruitos E, Villaverde A. Recombinant protein solubility-does more mean better?. Nat Biotechnol 2007, 25:718-720.
11. García-Fruitós E, Rodríguez-Carmona E, Díez-Gil C, Ferraz RM, Vázquez E, Corchero JL, et al. Surface Cell Growth Engineering Assisted by a Novel Bacterial Nanomaterial. Advanced Materials 2009, 21:4249-4253.
12. Mitraki A. Protein aggregation from inclusion bodies to amyloid and biomaterials. Adv Protein Chem Struct Biol 2010, 79:89-125.
13. Peternel S, Komel R. Active Protein Aggregates Produced inEscherichia coli. Int J Mol Sci 2011, 12:8275-8287.
14. Rodriguez-Carmona E, Villaverde A. Nanostructured bacterial materials for innovative medicines. Trends Microbiol 2010, 18:423-430.
15. Villaverde A. Nanotechnology, bionanotechnology and microbial cell factories. Microb Cell Fact 2010, 9:53.
16. Vazquez E, Villaverde A. Engineering building blocks for self-assembling protein nanoparticles. Microb Cell Fact 2010, 9:101.
17. Seras-Franzoso J, Diez-Gil C, Vazquez E, Garcia-Fruitos E, Cubarsi R, Ratera I, et al. Bioadhesiveness and efficient mechanotransduction stimuli synergistically provided by bacterial inclusion bodies as scaffolds for tissue engineering. Nanomedicine (Lond) 2012, 7:79-93.
18. Garcia-Fruitos E, Seras-Franzoso J, Vazquez E, Villaverde A. Tunable geometry of bacterial inclusion bodies as substrate materials for tissue engineering. Nanotechnology 2010, 21:205101.
19. Diez-Gil C, Krabbenborg S, Garcia-Fruitos E, Vazquez E, Rodriguez-Carmona E, Ratera I, et al. The nanoscale properties of bacterial inclusion bodies and their effect on mammalian cell proliferation. Biomaterials 2010, 31:5805-5812.
20. Gonzalez-Montalban N, Villaverde A, Aris A. Amyloid-linked cellular toxicity triggered by bacterial inclusion bodies. Biochem Biophys Res Commun 2007, 355:637-642.
21. Gonzalez P, Peluffo H, Acarin L, Villaverde A, Gonzalez B, Castellano B. Interleukin-10 overexpression does not synergize with the neuroprotective action of RGD-containing vectors after postnatal brain excitotoxicity but modulates the main inflammatory cell responses. J Neurosci Res 2012, 90:143-159.
22. Garcia-Fruitos E, Aris A, Villaverde A. Localization of functional polypeptides in bacterial inclusion bodies. Appl Environ Microbiol 2007, 73:289-294.
23. Villaverde A, Carrio MM. Protein aggregation in recombinant bacteria: biological role of inclusion bodies. Biotechnol Lett 2003, 25:1385-1395.
24. García-Fruitós E, Vazquez E, Corchero JL, Villaverde A. Use of inclusion bodies as therapeutic agents [WO2010131117A1]. 18-11-2010.
25. Vazquez E, Corchero JL, Burgueno JF, Seras-Franzoso J, Kosoy A, Bosser R, et al. Functional inclusion bodies produced in bacteria as naturally occurring nanopills for advanced cell therapies. Adv Mater 2012, 24:1742-1747.
26. Liovic M, Ozir M, Bedina ZA, Peternel S, Komel R, Zupancic T. Inclusion bodies as potential vehicles for recombinant protein delivery into epithelial cells. Microb Cell Fact 2012, 11:67.
27. Ferrer-Miralles N, Vazquez E, Villaverde A. Membrane-active peptides for non-viral gene therapy: making the safest easier. Trends Biotechnol 2008, 26:267-275.
28. Garcia-Fruitos E, Sabate R, de Groot NS, Villaverde A, Ventura S. Biological role of bacterial inclusion bodies: a model for amyloid aggregation. FEBS J 2011, 278:2419-2427.
29. Carrio M, Gonzalez-Montalban N, Vera A, Villaverde A, Ventura S. Amyloid-like properties of bacterial inclusion bodies. J Mol Biol 2005, 347:1025-1037.
30. Speed MA, Wang DI, King J. Specific aggregation of partially folded polypeptide chains: the molecular basis of inclusion body composition. Nat Biotechnol 1996, 14:1283-1287.
31. Morell M, Bravo R, Espargaro A, Sisquella X, Aviles FX, Fernandez-Busquets X, et al. Inclusion bodies: specificity in their aggregation process and amyloid-like structure. Biochim Biophys Acta 2008, 1783:1815-1825.
32. Rinas U, Boone TC, Bailey JE. Characterization of inclusion bodies in recombinantEscherichia coliproducing high levels of porcine somatotropin. J Biotechnol 1993, 28:313-320.
33. Rinas U, Bailey JE. Protein compositional analysis of inclusion bodies produced in recombinantEscherichia coli. Appl Microbiol Biotechnol 1992, 37:609-614.
34. Hart RA, Rinas U, Bailey JE. Protein composition ofVitreoscillahemoglobin inclusion bodies produced inEscherichia coli. J Biol Chem 1990, 265:12728-12733.
35. Neubauer A, Soini J, Bollok M, Zenker M, Sandqvist J, Myllyharju J, et al. Fermentation process for tetrameric human collagen prolyl 4-hydroxylase inEscherichia coli: Improvement by gene optimisation of the PDI/beta subunit and repeated addition of the inducer anhydrotetracycline. J Biotechnol 2007, 128:308-321.
36. Rinas U, Hoffmann F, Betiku E, Estape D, Marten S. Inclusion body anatomy and functioning of chaperone-mediated in vivo inclusion body disassembly during high-level recombinant protein production inEscherichia coli. J Biotechnol 2007, 127:244-257.
37. Allen SP, Polazzi JO, Gierse JK, Easton AM. Two novel heat shock genes encoding proteins produced in response to heterologous protein expression inEscherichia coli. J Bacteriol 1992, 174:6938-6947.
38. Carrio MM, Villaverde A. Construction and deconstruction of bacterial inclusion bodies. J Biotechnol 2002, 96:3-12.
39. Carrio MM, Villaverde A. Localization of chaperones DnaK and GroEL in bacterial inclusion bodies. J Bacteriol 2005, 187:3599-3601.
40. Estape D, Rinas U. Folding kinetics of the all-beta-sheet protein human basic fibroblast growth factor, a structural homolog of interleukin-1beta. J Biol Chem 1999, 274:34083-34088.
41. Peternel S, Komel R. Isolation of biologically active nanomaterial (inclusion bodies) from bacterial cells. Microb Cell Fact 2010, 9:66.
42. Rodriguez-Carmona E, Cano-Garrido O, Seras-Franzoso J, Villaverde A, Garcia-Fruitos E. Isolation of cell-free bacterial inclusion bodies. Microb Cell Fact 2010, 9:71.
43. Maji SK, Perrin MH, Sawaya MR, Jessberger S, Vadodaria K, Rissman RA, et al. Functional amyloids as natural storage of peptide hormones in pituitary secretory granules. Science 2009, 325:328-332.
44. Maji SK, Schubert D, Rivier C, Lee S, Rivier JE, Riek R. Amyloid as a depot for the formulation of long-acting drugs. PLoS Biol 2008, 6:e17.