Pathway of detergent-mediated and peptide ligand-mediated refolding of heterodimeric class II major histocompatibility complex (MHC) molecules

European Journal of Biochemistry

Volumn 248, Issue 3, 1997, Pages 684-691

  Stöckel, Johannes ^a   Döring, Klaus ^b   Malotka, Joachim ^a   Jähnig, Fritz ^b   Dornmair, Klaus ^a  

^a MAX PLANCK INSTITUTE OF PSYCHIATRY   (Germany)

^b MAX PLANCK INST FÜR BIOLOGIE   (Germany)

Author keywords

Detergent; Folding intermediate; Heterodimer formation; Major histocompatibility complex; Protein folding

Indexed keywords

HLA DR5 ANTIGEN; RECOMBINANT PROTEIN;

ARTICLE; CIRCULAR DICHROISM; ESCHERICHIA COLI; FLUORESCENCE; HISTOCOMPATIBILITY COMPLEX; LIGAND BINDING; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN PURIFICATION; PROTEIN STRUCTURE;

ESCHERICHIA COLI;

EID: 0030804221     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.t01-2-00684.x     Document Type: Article

References (42)

1. Arand, M., Friedberg, T. & Oesch, F. (1992) Colorimetric quantitation of trace amounts of sodium lauryl sulfate in the presence of nucleic acids and proteins, Anal. Biochem. 207, 73-75.
2. Buchner, J. & Rudolph, R. (1991) Renaturation, purification and characterization of recombinant Fab fragments produced in Escherichia coli, Bio-technology (NY) 9, 157-162.
3. Chien, Y. H. & Davis, M. M. (1993) How αβ T cell receptors 'see' MHC/peptide complexes, Immunol. Today 14, 597-602.
4. Cleland, J. L., Builder, S. E., Swartz, J. R., Winkler, M., Chang, J. Y. & Wang D. I. C. (1992) Polyethylene glycol enhanced protein refolding, Bio-technology (NY) 10, 1013-1019.
5. Dornmair, K., Rothenhäusler, B. & McConnell, H. M. (1989) Stuctural intermediates in the reactions of antigenic peptides with MHC molecules, Cold Spring Harbor Symp. Quant. Biol. 54, 409-416.
6. Dornmair, K., Kiefer, H. & Jähnig, F. (1990) Refolding of an integral membrane protein. OmpA of Escherichia coli, J. Biol. Chem. 265, 18907-18911.
7. Dornmair, K. & McConnell, H. M. (1990) Refolding and reassembly of separate α and β chains of class II molecules of major histocompatibility complex leads to increased peptide-binding capacity, Proc. Natl Acad. Sci. USA 87, 4134-4138.
8. Döring, K., Konermann, L., Surrey, T. & Jähnig, F. (1995) A long lifetime component in the tryptophan fluorescence of some proteins, Eur. Biophys. J. 23, 423-432.
9. Eisele, J. L. & Rosenbusch, J. P. (1990) In vitro folding and oligomerization of a membrane protein, J. Biol. Chem. 265, 10217-10220.
10. Ellis, R. J. & Hartl, F. U. (1996) Protein folding in the cell: competing models of chaperonin function, FASEB J. 10, 20-26.
11. Engelhard, M. & Evans, P. A. (1996) Experimental investigations of sidechain interactions in early folding intermediates, Folding & Design 1, R31-R37.
12. Fink, A. L. (1995) Compact intermediate states in protein folding, Annu. Rev. Biophys. Biomol. Struct. 24, 495-522.
13. Germain, R. N. & Margulies, D. H. (1993) The biochemistry and cell biology of antigen processing and presentation, Annu. Rev. Immunol. 11, 403-450.
14. Huang, K. S., Bayley, H., Liao, M. J., London, E. & Khorana, H. G. (1981) Refolding of an integral membrane protein, J. Biol. Chem. 256, 3802-3809.
15. Jaenicke, R. (1991) Protein folding: local structures, domains, subunits, and assemblies, Biochemistry 30, 3147-3161.
16. Jirgensons, B. (1966) Effect of anionic detergents on the optical rotatory dispersion of proteins, J. Biol. Chem. 241, 4855-4860.
17. Jones, B. E., Beechem, J. M. & Matthews, C. R. (1995) Local and global dynamics during the folding of Escherichia coli dihydrofolate reductase by time-resolved fluorescence spectroscopy, Biochemistry 34, 1867-1877.
18. Kropshofer, H., Bohlinger, I., Max, H. & Kalbacher, H. (1991) Self and foreign peptides internet with disassembled MHC Class II antigen HLA-DR via tryptophan pockets, Biochemistry 30, 9177-9187.
19. Matthews, C. R. (1993) Pathways of protein folding, Annu. Rev. Biochem. 62, 653-683.
20. Munro, I., Pecht, I. & Stryer, L. (1979) Subnanosecond motions of tryptophan residues in proteins, Proc. Natl Acad. Sci. USA 78, 56-60.
21. Nag, B., Wada, H. G., Deshpande, S. V., Passmore, D., Kendrick, T., Sharma, S. D., Clark, B. R. & McConnell, H. M. (1993) Stimulation of T cells by antigenic peptide complexed with isolated chains of major histocompatibility complex class II molecules, Proc. Natl Acad. Sci. USA 90, 1604-1608.
22. Paulsen, H., Rümler, U. & Rüdiger, W. (1990) Reconstitution of pigment-containing complexes from light-harvesting chlorophyll α/β-binding protein overexpressed in Escherichia coli, Planta (Heidelb.) 181, 204-211.
23. Peterson, G. L. (1977) A simplification of the protein assay method of Lowry et al., which is more generally applicable, Anal. Biochem. 83, 346-356.
24. Rothenhüusler, B., Dornmair, K. & McConnell, H. M. (1990) Specific binding of antigenic peptides to separate α and β chains of class II molecules of the major histocompatibility complex, Proc. Natl Acad. Sci. USA 87, 352-354.
25. Rozema, D. & Gellman, S. H. (1996) Artificial chaperone-assisted refolding of carbonic anhydrase B, J. Biol. Chem. 271, 3478-3487.
26. Rudolph, R. & Lilie, H. (1996) In vitro folding of inclusion body proteins, FASEB J. 10, 49-56.
27. Sawano, H., Koumoto, Y., Ohta, K., Sasaki, Y., Segawa, S. & Tachibana, H. (1992) Efficient in vitro folding of the three-disulfide derivatives of hen lysozyme in the presence of glycerol, FEBS Lett. 303, 11-14.
28. Sinclair, J. F., Waddle, J. J., Waddill, E. F. & Baldwin, T. O. (1993) Purified native subunits of bacterial luciferase are active in the bioluminescence reaction but fail to assemble into the αβ structure, J. Biol. Chem. 32, 5036-5044.
29. Sirokmán, G. & Fasman, G. D. (1993) Refolding and proton pumping activity of a polyethylene glycol-bacteriorhodopsin water-soluble conjugate, Protein Sci. 2, 1161-1170.
30. Springer, T. A., Kaufman, J. F., Terhorst, C. & Strominger, J. L. (1977) Purification and structural characterization of human HLA linked B-cell antigens, Nature 268, 213-218.
31. Stern, L. J., Brown, J. H., Jardetzky, T. S., Gorga, J. C., Urban, R. G., Strominger, J. L. & Wiley, D. C. (1994) Crystal structure of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptide, Nature 368, 215-221.
32. Stöckel, J., Meinl, E., Hahnel, C., Malotka, J., Seitz, R., Drexler, K., Wekerle, H. & Dornmair, K. (1994) Refolding of human class II major histocompatibility complex molecules isolated from Escherichia coli: assembly of peptide-free heterodimers and increased refolding-yield in the presence of antigenic peptide, J. Biol. Chem. 269, 29571-29578.
33. Sun, M., Li. L., Gao, Q. S. & Paul, S. (1994) Antigen recognition by an antigen light chain, J. Biol. Chem. 269, 734-738.
34. Tandon, S. & Horowitz, P. M. (1987) Detergent assisted refolding of guanidinium chloride denatured rhodanase, J. Biol. Chem. 262, 4486-4491.
35. Tanford, C. (1980) The hydrophobic effect: formation of micelles and biological membranes, J. Wiley & Sons, New York.
36. Timasheff, S. N. (1993) The control of protein stability and association by weak interactions with water: how do solvents affect these processes? Annu. Rev. Biophys. Biomol. Struct. 22, 67-97.
37. Valli, A., Sette, A., Kappos, L., Oseroff, C., Sidney, J., Miescher, G., Albert, E. D. & Adorini, L. (1993) Binding of myelin basic protein peptides to human histocompatibility leukocyte antigen class II molecules and their recognition by T cells from multiple sclerosis patients, J. Clin. Invest. 91, 616-622.
38. Waldmann, T. A. (1991) The interleukin-2 receptor, J. Biol. Chem. 266, 2681-2684.
39. Ward, E. S., Güssow, D., Griffiths, A. D., Jones, P. T. & Winter, G. (1989) Binding activities of a repertoire of single immunoglobulin variable domains secreted from Escherichia coli, Nature 341, 544-546.
40. Wetlaufer, D. B. & Xie, Y. (1995) Control of aggregation in protein refolding: a variety of surfactants promote renaturation of carbonic anhydrase II, Protein Sci. 4, 1535-1543.
41. Wolynes, P. G., Onuchic, J. N. & Thirumalai, D. (1995) Navigating the folding routes, Science 267, 1619-1620.
42. Zardeneta, G. & Horowitz, P. M. (1992) Micelle-assisted protein folding, J. Biol. Chem. 267, 5811-5816.