Hydrostatic pressure rescues native protein from aggregates

Biotechnology and Bioengineering

Volumn 63, Issue 5, 1999, Pages 552-558

  Foguel, Debora ^a   Robinson, Clifford R ^b,c,d   De Sousa Jr , Pedro Caetano ^a   Silva, Jerson L ^a   Robinson, Anne Skaja ^b,c  

^a FEDERAL UNIVERSITY OF RIO DE JANEIRO   (Brazil)

^b MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

^c University of Delaware   (United States)

^d 3 Dimensional Pharmaceuticals   (United States)

Author keywords

Hydrostatic pressure; Inclusion body; p22 tailspike; Protein aggregation; Protein folding; Size exclusion HPLC

Indexed keywords

AGGLOMERATION; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HYDROSTATIC PRESSURE; PRESSURE EFFECTS; PROTEINS; SIZE EXCLUSION CHROMATOGRAPHY;

PROTEIN AGGREGATION; PROTEIN FOLDING;

BIOTECHNOLOGY;

BACTERIAL PROTEIN; OLIGOMER; TAILSPIKE PROTEIN; UNCLASSIFIED DRUG;

ANALYTIC METHOD; ARTICLE; HYDROSTATIC PRESSURE; MOLECULAR MODEL; MOLECULAR RECOGNITION; PROTEIN AGGREGATION; PROTEIN FOLDING; PROTEIN TERTIARY STRUCTURE; REGULATORY MECHANISM; RELIABILITY; STRUCTURE ACTIVITY RELATION; VALIDATION PROCESS;

CHROMATOGRAPHY, GEL; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; ELECTROPHORESIS, POLYACRYLAMIDE GEL; GLYCOSIDE HYDROLASES; HYDROSTATIC PRESSURE; PROTEIN CONFORMATION; PROTEIN FOLDING; SPECTROMETRY, FLUORESCENCE; VIRAL TAIL PROTEINS;

BACTERIA (MICROORGANISMS);

EID: 0033526550     PISSN: 00063592     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0290(19990605)63:5<552::AID-BIT5>3.0.CO;2-8     Document Type: Article

References (45)

1. Berget PB, Poteete AR. 1980. Structure and functions of the bacteriophage P22 tail protein. J Virol 34:234-243.
2. Betts S, Haase-Pettingell C, King J. 1997. Mutational effects on inclusion body formation. Adv Prot Chem 50:243-264.
3. Builder S, Hart R, Lester P, Reifsnyder D. 1997. Refolding of misfolded insulin-like growth factor-1. US Patent 5663304.
4. Bychkova VE, Ptitsyn OB. 1995. Folding intermediates are involved in genetic diseases? FEBS Letters 359:6-8.
5. Cleland JL. 1993. Impact of protein folding on biotechnology. In: Protein folding: In vivo and in vitro. Cleland JL, editor. vol. 526. ACS Symposium Series, Washington, DC: American Chemical Society. p 1-21.
6. Davis BJ. 1964. Disk electrophoresis - II. Methods and application to human serum proteins. Ann NY Acad Sci 121:404-427.
7. De Bernardez Clark E. 1998. Refolding of recombinant proteins. Curr Opin Biotechnol 9:157-163.
8. De Bernardez-Clark E, Georgiou G. 1991. Inclusion bodies and recovery of proteins from the aggregated state. In: Protein Refolding. Georgiou G, De Bernardez-Clark E, editors. vol. 470. ACS Symposium Series, Washington, DC: American Chemical Society. p 1-20.
9. Foguel D, Silva JL, Prat-Gay G. 1998. Characterization of a partially folded monomer of the DNA-binding domain of human Papillomavirus E2 obtained at high pressure. J Biol Chem 273:9050-9057.
10. Fuchs A, Seiderer C, Seckler R. 1991. In vitro folding pathway of phage P22 tailspike protein. Biochemistry 30:6598-6604.
11. Goldenberg D, Berget P, King J. 1982. Maturation of the tailspike endorhamnosidase of Salmonella phage P22. J Biol Chem 257:7864-7871.
12. Goldenberg D, King J. 1982. Trimeric intermediate in the in vivo folding and subunit assembly of the tail spike endorhamnosidase of bacteriophage P22. Proc Natl Acad Sci USA 79:3403-3407.
13. Goldenberg DP, Smith DH, King J. 1983. Genetic analysis of the folding pathway for the tail spike protein of phage P22. Proc Natl Acad Sci USA 80:7060-7064.
14. Gorovits BM, Horowitz PM. 1998. High hydrostatic pressure can reverse aggregation of protein folding intermediates and facilitate acquisition of native structure. Biochemistry 37:6132-6135.
15. Haase-Pettingell CA, King J. 1988. Formation of aggregates from a thermolabile in vivo folding intermediate in P22 tailspike maturation: A model for inclusion body formation. J Biol Chem 263:4977-4983.
16. Heremans K. 1997. High pressure research in the biosciences and biotechnology. Leuven: Leuven University Press.
17. Israel JV, Anderson, TF, Levine M. 1967. In vitro morphogenesis of phage P22 from heads and base-plate parts. Proc Natl Acad Sci USA 57: 284-291.
18. Iwashita S, Kanegasaki S. 1976. Enzymic and molecular properties of base-plate parts of bacteriophage P22. Eur J Biochem 65:87-94.
19. Jarrett JT, Berger EP, Lansbury PT Jr. 1993. The C-terminus of the beta protein is critical in amyloidogenesis. Ann NY Acad Sci 695:144-148.
20. Jurkiewicz E, Villas-Boas M, Silva JL, Weber G, Hunsmann G, Clegg RM. 1995. Inactivation of simian immunodeficiency virus by hydrostatic pressure. Proc Natl Acad Sci USA 92:6935-6937.
21. Maachupalli-Reddy J, Kelley BD, De Bernardez Clark E. 1997. Effect of inclusion body contaminants on the oxidative renaturation of hen egg white lysozyme. Biotechnol Progr 13:144-150.
22. Ornstein L. 1964. Disc electrophoresis - I. Background and theory. Ann NY Acad Sci 121:321-349.
23. Pontes L, Fornells LA, Giongo V, Araujo JRV, Sepulveda A, Villas-Boas M, Bonafe CFS, Silva JL. 1997. Pressure inactivation of animal viruses: Potential biotechnological applications. In: High-pressure research in the biosciences and biotechnology. Heremans K, editor. Leuven: Leuven University Press. p 91-94.
24. Robinson AS, King J. 1997. Disulphide-bonded intermediate on the folding and assembly pathway of a non-disulphide bonded protein. Nature Struct Biol 4:450-455.
25. Robinson CR, Sligar SG. 1995. Hydrostatic and osmotic pressure as tools to study macromolecular recognition. Meth Enzymol 259:395-427.
26. Rudolph R, Lilie H. 1996. In vitro folding of inclusion body proteins. FASEB J 10:49-56.
27. Sambrook J, Fritsch EF, Maniatis T. 1989. Molecular cloning, a laboratory manual. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press.
28. Sauer RT, Krovatin W, Poteete AR, Berget PB. 1982. Phage P22 tail protein: Gene and amino acid sequence. Biochemistry 21:5811-5815.
29. Seckler R, Fuchs A, King J, Jaenicke R. 1989. Reconstitution of the thermostable trimeric phage P22 tailspike protein from denatured chains in vitro. J Biol Chem 264:11750-11753.
30. Shigehisa T, Ohmori T, Saito A, Taji S, Hayashi R. 1991. Effects of high hydrostatic pressure on characteristics of pork slurries and inactivation of microorganisms associated with meat and meat products. Int J Food Microbiol 12:207-215.
31. Silva JL, Foguel D, Da Poian AT, Prevelige PE. 1996. The use of hydrostatic pressure as a tool to study viruses and other macromolecular assemblages. Curr Opin Struct Biol 6:166-175.
32. Silva JL, Luan P, Glaser M, Voss EW, Weber G. 1992a. Effects of hydrostatic pressure on a membrane-enveloped virus: High immunogenicity of the pressure-inactivated virus. J Virol 66:2111-2117.
33. Silva JL, Silveira CF, Correa A, Pontes L. 1992b. Dissociation of a native dimer to a molten globule monomer. Effects of pressure and dilution on the association equilibrium constant of Arc repressor. J Molec Biol 223:545-555.
34. Silva JL, Weber G. 1993. Pressure stability of proteins. Annu Rev Phys Chem 44:89-113.
35. Simmons T, Newhouse YM, Arnold KS, Innerarity TL, Weisgraber KH. 1997. Human low density lipoprotein receptor fragment. Successful refolding of a functionally active ligand-binding domain produced in Escherichia coli. J Biol Chem 272:25531-25536.
36. Speed MA, Morshead T, Wang DI, King J. 1997. Conformation of P22 tailspike folding and aggregation intermediates probed by monoclonal antibodies. Prot Sci 6:99-108.
37. Speed MA, Wang DIC, King J. 1995. Multimeric intermediates in the pathway to the aggregated inclusion body state for P22 tailspike polypeptide chains. Prot Sci 4:900-908.
38. Speed MA, Wang DIC, King J. 1996. Specific aggregation of partially folded polypeptide chains: The molecular basis of inclusion body composition. Nature Biotechnol 14:1283-1287.
39. Steinbacher S, Seckler R, Miller S, Steipe B, Huber R, Reinemer P. 1994. Crystal structure of P22 tailspike protein: Interdigitated subunits in a thermostable trimer. Science 265:383-386.
40. Stempfer G, Holl-Neugebauer B, Rudolph R. 1996. Improved refolding of an immobilized fusion protein. Nature Biotechnol 14:329-334.
41. Stoyan T, Michaelis U, Schooltink H, Van Dam M, Rudolph R, Heinrich PC, Rose-John S. 1993. Recombinant soluble human interleukin-6 receptor. Expression in Escherichia coli, renaturation and purification. Eur J Biochem 216:239-245.
42. Tauscher B. 1995. Pasteurization of food by hydrostatic high pressure: Chemical aspects. Z Lebensm Unters Forsch 200:3-13.
43. Thomas PJ, Ko YH, Pedersen PL. 1992. Altered protein folding may be the molecular basis of most cases of cystic fibrosis. FEBS Lett 312:7-9.
44. Thomas PJ, Qu BH, Pedersen PL. 1995. Defective protein folding as a basis of human disease. Trends Biochem Sci 20:456-459.
45. Winston R, Botstein D, Miller J. 1979. Characterization of amber and ochre suppressors in Salmonella typhimurium. J Bacteriol 137:433-439.