Screening libraries of circularly permuted proteins by phage display to manipulate protein topographies

Proceedings of the Institution of Mechanical Engineers, Part N: Journal of Nanoengineering and Nanosystems

Volumn 219, Issue 2, 2005, Pages 45-55

  Van Valkenburgh, C D ^a   Merlin, S ^a   Rowold, E ^a   Adams, J ^a   Ibdah, R ^a   Pegg, L E ^a   Donelly, A ^a   Klover, J ^a   Eteshola, E ^b   Lee, S C ^c  

^a Ohio State University   (United States)

^b OHIO STATE UNIVERSITY   (United States)

^c OHIO STATE UNIVERSITY   (United States)

Author keywords

circularly permuted proteins; hG CSF; hIL 3; MPO; permutein; phage display; sensors

Indexed keywords

EID: 84990350737     PISSN: 17403499     EISSN: 20413092     Source Type: Journal    
DOI: 10.1243/17403499JNN38     Document Type: Article

References (53)

1. Lee S. C. The nanobiological strategy for construction of nanodevices In Biological molecules in nano-technology: the convergence of biotechnology, polymer chemistry and materials science (Eds Lee S. C. Savage L. ) 1998, pp. 3–14 (IBC Press, Southborough, MA, USA).
2. Lee S. C. Reugsegger M. Barnes P. D. Smith B. R. Ferrari M. Therapeutic nanodevices In The nano-technology handbook (Ed. Bhushan B. ) 2004, pp. 279–322 (Springer-Verlag, Heidelberg, Germany).
3. Lee S. C. Reugsegger M. Ferrari M. Biomolecules and nanodevices In The encyclopedia of nanoscience and nanotechnology, Vol. 1 (Ed. Nalwa H. S. ) 2004, pp. 309–327 (American Scientific Publishers, Stevenson Ranch, CA).
4. Holliday L. S. Lee S. C. Lee B. S. M. Mechanoenzymes in nanodevices Biomed. Microdevices: Biomems and Biomed. Nanotechnol., 2003, 5, 269–280.
5. Ross S. A. Srinivas P. R. Clifford A. J. Lee S. C. Philbert M. A. Hetich R. L. New technologies for nutrition research J. Nutr., 2004, 134, 681–685.
6. Buxton D. B. Lee S. C. Wickline S. A. Ferrari M. Recommendations of the National Heart, Lung, and Blood Institute Nanotechnology Working Group Circulation, 2003, 108, 2737–2742.
7. Lemieux G. A. Bertozzi C. R. Chemoselective ligation reactions with proteins, oligosaccharides and cells Trends Biotechnol., 1998, 16, 506–512.
8. Lee S. C. Parthasarathy R. Duffin T. Botwin K. Beck T. Lange G. Zobel J. Kunneman D. Rowold E. Voliva C. F. Recognition properties of antibodies to PAMAM dendrimers and their use in immune detection of dendrimers Biomed. Microdevices: Biomems and Biomed. Nanotechnol., 2001, 3, 51–57.
9. Lee S. C. Parthasarathy R. Botwin K. Kunneman D. Rowold E. Lange G. Zobel J. Beck T. Miller T. Hood W. Monahan J. Jansson R. McKearn J. P. Voliva C. F. 2004. Biochemical and immunological properties of cytokines conjugated to dendritic polymers Biomed. Microdevices: Biomems and Biomed. Nanotechnol., 2004, 6, 191–201.
10. Goldenberg D. P. Creighton T. E. Folding pathway of a circular form of bovine pancreatic trypsin inhibitor J. Molecular Biol., 1984, 179, 527–45.
11. Thornton J. M. Sibanda J. M. Amino and carboxy-terminal regions in globular proteins J. Molecular Biol., 1983, 167, 443–460.
12. Topell S. Glockshuber R. Circular permutation of the green fluorescent protein Meth. in Molecular Biol. (Totowa, NJ, United States), 2002, 183, 31–48.
13. Rojas A. Garcia-Vallve S. Palau J. Romeu A. Circular permutations in proteins Biologia (Bratislava), 1999, 54, 255–277.
14. Lee S. C. Method of producing permutiens by scanning permutagenesis. International Patent Application # WO 20000/18905, 1998.
15. Schwartz T. U. Walczak R. Blobel G. Circular permutation as a tool to reduce surface entropy triggers crystallization of the signal recognition particle receptor beta subunit Protein Sci., 2004, 13, 2814–18.
16. Heinemann U. Hahn M. Circular permutation of polypeptide chains: implications for protein folding and stability Prog. Biophys. Molecular Biol., 1996, 64, 121–143.
17. Zhang T. Bertelsen E. Benvegnu D. Alber T. Circular permutation of T4 lysozyme Biochem., 1993, 32, 12311–12318.
18. Zhang T. Bertelsen E. Alber T. Entropic effects of disulphide bonds on protein stability Nature Struct. Molecular Biol., 1994, 1, 434–438.
19. Buchwalder A. Szadkoski H. Kirschner K. A fully active variant of dihydrofolate reductase with a circularly permuted sequence Biochem., 1992, 31, 1621–1630.
20. Protasova N. Yu., Kireeva, M. L., Murzina, N. V., Murzin, A. G., Uversky, V. N., Gryaznova, O. I., and Gudkov, A. T. Circularly permuted dihydrofolate reductase of E. coli has functional activity and a destabilized tertiary structure Protein Engng, 1994, 7, 1373–1377.
21. Mullins L. S. Wesseling K. Kuo J. M. Garrett J. B. Raushel F. M. Transposition of protein sequences: circular permutation of ribonuclease T1 J. Am. Chem. Soc., 1994, 116, 5529–5533.
22. Garrett J. B. Mullins L. S. Raushel F. M. Are turns required for the folding of ribonuclease T1? Protein Sci., 1996, 5, 204–211.
23. Hahn M. Piotukh K. Borriss R. Heinemann U. Native-like in vivo folding of a circularly permuted jellyroll protein shown by crystal structure analysis Proc. Natl. Acad. Sci. USA, 1994, 91, 10417–10421.
24. Yang Y. R. Schachznan H. K. Aspartate transcar-bamoylase containing circularly permuted catalytic polypeptide chains Proc. Natl. Acad. Sci. USA, 1993, 90, 11980–11984.
25. Luger K. Hommel U. Herold M. Hofsteenge J. Kirschner K. Correct folding of circularly permuted variants of a beta alpha barrel enzyme in vivo. Sci., 1989, 243, 206–210.
26. Luger K. Szadkowski H. Kirschner K. An 8-fold beta alpha barrel protein with redundant folding possibilities Protein Engng, 1990, 3, 249–258.
27. Lin X. Koelsch G. Loy J. A. Tang J. Rearranging the domains of pepsinogen Protein Sci., 1995, 4, 159–166.
28. Vignais M. L. Corbier C. Mulliert G. Branlant C. Branlant G. Circular permutation within the coenzyme binding domain of the tetrameric glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus Protein Sci., 1995, 4, 994–1000.
29. Li X. Coffino P. Degradation of ornithine decarboxylase: exposure of the C-terminal target by a polyamine-inducible inhibitory protein Molecular Cellular Biol., 1993, 13, 2377–2383.
30. Ritco-Vonsovici M. Minard P. Desmadril M. Yon J. M. Is the continuity of the domains required for the correct folding of a two-domain protein? Biochem., 1995, 34, 16543–16551.
31. Goldenberg D. P. Creighton T. E. Circular and circularly permuted forms of bovine pancreatic trypsin inhibitor J. Molecular Biol., 1983, 165, 407–413.
32. Horlick R. A. George H. J. Cooke G. M. Tritch R. J. Newton R. C. Dwivedi A. Lischwe M. Salemme F. R. Weber P. C. Horuk R. Permuteins of interleukin 1 beta - a simplified approach for the construction of permutated proteins having new termini Protein Engng, 1992, 5, 427–431.
33. Kreitman R. J. Puri R. K. McPhie P. Pastan I. Circularly permuted interleukin 4 retains proliferative and binding activity Cytokine, 1995, 7, 311–318.
34. Viguera A. R. Blanco F. J. Serrano L. The order of secondary structure elements does not determine the structure of a protein but does affect its folding kinetics J. Molecular Biol., 1995, 247, 670–681.
35. Koebnik R. Kramer L. Membrane assembly of circularly permuted variants of the E. coli outer membrane protein OmpA J. Molecular Biol., 1995, 250, 617–626.
36. Kreitman R. J. Puri R. K. Pastan I. A circularly permuted recombinant interleukin 4 toxin with increased activity Proc. Natl. Acad. Sci. USA, 1994, 91, 6889–6893.
37. Graf R. Schachman H. K. Random circular permutation of genes and expressed polypeptide chains: Application of the method to the catalytic chains of aspartate transcarbamoylase Proc. Natl. Acad. Sci. USA, 1996, 93, 11591–11596.
38. Hennecke J. Sebbel P. Glockshuber R. Random circular permutation of DsbA reveals segments that are essential for protein folding and stability J. Molecular Biol., 1999, 286, 1197–1215.
39. Chunhai F. Kevin P. Heeger W. Alan J. Biosensors based on binding-modulated donor-acceptor distances Trends in Biotechnol., 2005, 23, 186–92.
40. Kay B. K. Winter J. McCofferty J. Phage display of peptides and proteins, 1996 (Academic Press, San Diego, CA).
41. Lee S. C. Ibdah R. VanValkenburgh C. Rowold E. Donnelly A. Abegg A. Klover J. Merlin S. McKearn J. Phage display mutagenesis of the chimeric dual cytokine receptor agonist myelopoietin Leukemia, 2001, 15, 1277–1285.
42. McWherter C. A. Feng Y. Zurfluh L. L. Klein B. K. Baganoff M. P. Polazzi J. O. Hood W. F. Paik K. Abegg A. L. Grabbe E. S. Shieh J. J. Donnelly A. M. McKearn J. P. Circular permutation of the granulocyte colony-stimulating factor receptor agonist domain of myelopoietin Biochem., 1999, 38, 4564–71.
43. MacVittie T. J. Farese A. M. Smith W. G. Baum C. M. Burton E. McKearn J.P. Myelopoietin, an engineered chimeric IL-3 and G-CSF receptor agonist, stimulates multilineage hematopoietic recovery in a nonhuman primate model of radiation-induced myelosuppression Blood, 2000, 95, 837–845.
44. Merlin S. Rowold E. Abegg A. Berglund C. Klover J. Staten N. McKearn J. P. Lee S. C. Phage presentation and affinity selection of a deletion mutant of human interleukin-3 Appl. Biochem. Biotechnol., 1997, 67, 199–214.
45. Chang A. C. Cohen S. N. Construction and characterization of amplifiable multicopy DNA cloning vehicles derived from the P15A cryptic miniplasmid J. Bact., 1978, 134, 1141–1156.
46. Prober J. M. Trainor G. L. Dam R. J. Hobbs F. W. Robertson C. W. Zagursky R. J. Cocuzza A. J. Jensen M. A. Baumeister K. A system for rapid DNA sequencing with fluorescent chain-terminating dideoxynucleotides Sci., 1987, 238, 336–341.
47. Sambrook J. Fritsch E. F. Maniatis T. Molecular cloning: a laboratory manual, 2nd edition, 1989 (Cold Spring Harbor Laboratory Press, New York).
48. Horlick R. A. George H. J. Cooke G. M. Tritch R. J. Newton R. C. Dwivedi A. Lischwe M. Salemme F. R. Weber P. C. Horuk R. Permuteins of interleukin 1 beta - a simplified approach for the construction of permutated proteins having new termini Protein Engng, 1992, 5, 427–31.
49. Layton J. E. Shimamoto G. Osslund T. Hammacher A. Smith D. K. Treutlein H. R. Boone T. Interaction of granulocyte colony-stimulating factor (G-CSF) with its receptor. Evidence that Glu19 of G-CSF interacts with Arg288 of the receptor J. Biol. Chem., 1999, 274, 17445–51.
50. Young D. C. Zhan H. Cheng Q-L. Hou J. Matthews D. J. Characterization of the receptor binding determinants of granulocyte colony stimulating factor Protein Sci., 1997, 6, 1228–1236.
51. Reidhaar-Olson J. F. De Souza-Hart J. A. Selick H. E. Identification of residues critical to the activity of human granulocyte colony-stimulating factor. Biochem., 1996, 35, 9034–41.
52. Clackson T. Wells J. A. In vitro selection from protein and peptide libraries Trends Biotechnol., 1994, 12, 173–184.
53. Hill C. P. Osslund T. D. Eisenberg D. The structure of granulocyte-colony-stimulating factor and its relationship to other growth factors Proc. Natl. Acad. Sci. USA, 1993, 90, 5167–5171.