Comparative biophysical characterization of chicken β2-microglobulin

Biophysical Chemistry

Volumn 167, Issue , 2012, Pages 26-35

  Hee, Chee Seng ^a   Fabian, Heinz ^b   Uchanska Ziegler, Barbara ^a   Ziegler, Andreas ^a   Loll, Bernhard ^c  

^a CHARITÉ UNIVERSITÄTSMEDIZIN BERLIN   (Germany)

^b ROBERT KOCH INSTITUTE   (Germany)

^c FREIE UNIVERSITÄT BERLIN   (Germany)

Author keywords

Differential scanning calorimetry; Immune system; IR spectroscopy; Major histocompatibility complex; X ray crystallography; 2 microglobulin

Indexed keywords

AVIAN PROTEIN; BETA 2 MICROGLOBULIN; HLA B27 ANTIGEN; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; MONOMER;

ARTICLE; BACTERIAL CELL; BIOPHYSICS; CHICKEN; COMPARATIVE STUDY; CRYSTAL STRUCTURE; DIFFERENTIAL SCANNING CALORIMETRY; ESCHERICHIA COLI; INFRARED SPECTROSCOPY; MAJOR HISTOCOMPATIBILITY COMPLEX; MELTING POINT; MELTING TEMPERATURE; NONHUMAN; PERIPLASM; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN EXPRESSION; PROTEIN SECONDARY STRUCTURE; THERMODYNAMICS; THERMOSTABILITY; X RAY CRYSTALLOGRAPHY; ANIMAL; CARP; CATTLE; CHEMISTRY; DEUTERIUM HYDROGEN EXCHANGE; HUMAN; PROTEIN SUBUNIT; PROTEIN TERTIARY STRUCTURE;

ANIMALS; BETA 2-MICROGLOBULIN; CALORIMETRY, DIFFERENTIAL SCANNING; CARPS; CATTLE; CHICKENS; CRYSTALLOGRAPHY, X-RAY; DEUTERIUM EXCHANGE MEASUREMENT; HUMANS; PROTEIN STRUCTURE, TERTIARY; PROTEIN SUBUNITS; THERMODYNAMICS;

EID: 84861969750     PISSN: 03014622     EISSN: 18734200     Source Type: Journal    
DOI: 10.1016/j.bpc.2012.04.001     Document Type: Article

References (53)

1. 2-microglobulin. Proceedings of the National Academy of Sciences of the United States of America 82 (1985), 4225–4229.
2. Hunkapiller, T., Hood, L., Diversity of the immunoglobulin gene superfamily. Advances in Immunology 44 (1989), 1–63.
3. Saper, M.A., Bjorkman, P.J., Wiley, D.C., Refined structure of the human histocompatibility antigen HLA-A2 at 2.6 A resolution. Journal of Molecular Biology 219 (1991), 277–319.
4. Zeng, Z., Castano, A.R., Segelke, B.W., Stura, E.A., Peterson, P.A., Wilson, I.A., Crystal structure of mouse CD1: an MHC-like fold with a large hydrophobic binding groove. Science 277 (1997), 339–345.
5. Otten, G.R., Bikoff, E., Ribaudo, R.K., Kozlowski, S., Margulies, D.H., Germain, R.N., Peptide and beta 2-microglobulin regulation of cell surface MHC class I conformation and expression. Journal of Immunology 148 (1992), 3723–3732.
6. Lancet, D., Parham, P., Strominger, J.L., Heavy chain of HLA-A and HLA-B antigens is conformationally labile: a possible role for beta 2-microglobulin. Proceedings of the National Academy of Sciences of the United States of America 76 (1979), 3844–3848.
7. Krangel, M.S., Orr, H.T., Strominger, J.L., Assembly and maturation of HLA-A and HLA-B antigens in vivo. Cell 18 (1979), 979–991.
8. Fellous, M., Gerbal, A., Nobillot, G., Weils, J., Studies on the biosynthetic pathway of human P erythrocyte antigen using genetic complementation tests between fibroblasts from rare p and Pk phenotype donors. Vox Sanguinis 32 (1977), 262–268.
9. Dobberstein, B., Kvist, S., Roberts, L., Structure and biosynthesis of histocompatibility antigens (H-2, HLA). Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences 300 (1982), 161–172.
10. Williams, D.B., Barber, B.H., Flavell, R.A., Allen, H., Role of Beta-2-microglobulin in the intracellular-transport and surface expression of murine class-I histocompatibility molecules. Journal of Immunology 142 (1989), 2796–2806.
11. Zijlstra, M., Bix, M., Simister, N.E., Loring, J.M., Raulet, D.H., Jaenisch, R., Beta 2-microglobulin deficient mice lack CD4-8 + cytolytic T cells. Nature 344 (1990), 742–746.
12. Peterson, P.A., Rask, L., Ostberg, L., beta2-microglobulin and the major histocompatibility complex. Advances in Cancer Research 24 (1977), 115–163.
13. Vincent, C., Revillard, J.P., Charpentier, B., Presence of glycoproteins binding human beta 2 microglobulin in rat serum. Comptes Rendus des Séances de l'Académie des sciences. Série III 292 (1981), 755–758.
14. Cejka, J., Van Nieuwkoo, J.A., Mood, D.W., Kithier, K., Radl, J., Beta2-microglobulin in human colostrum and milk: effect of breast feeding and physico-chemical characterization. Clinica Chimica Acta 67 (1976), 71–78.
15. Winchester, J.F., Salsberg, J.A., Levin, N.W., Beta-2 microglobulin in ESRD: an in-depth review. Advances in Renal Replacement Therapy 10 (2003), 279–309.
16. Heegaard, N.H., beta(2)-microglobulin: from physiology to amyloidosis. Amyloid 16 (2009), 151–173.
17. Platt, G.W., Radford, S.E., Glimpses of the molecular mechanisms of beta2-microglobulin fibril formation in vitro: aggregation on a complex energy landscape. FEBS Letters 583 (2009), 2623–2629.
18. Landman, W.J., Amyloid arthropathy in chickens. Veterinary Quarterly 21 (1999), 78–82.
19. Hee, C.S., Gao, S., Loll, B., Miller, M.M., Uchanska-Ziegler, B., Daumke, O., Ziegler, A., Structure of a classical MHC Class I molecule that binds “non-classical” ligands. PLoS Biology, 8, 2010, e1000557.
20. Koch, M., Camp, S., Collen, T., Avila, D., Salomonsen, J., Wallny, H.J., van Hateren, A., Hunt, L., Jacob, J.P., Johnston, F., Marston, D.A., Shaw, I., Dunbar, P.R., Cerundolo, V., Jones, E.Y., Kaufman, J., Structures of an MHC class I molecule from B21 chickens illustrate promiscuous peptide binding. Immunity 27 (2007), 885–899.
21. Dvir, H., Wang, J., Ly, N., Dascher, C.C., Zajonc, D.M., Structural basis for lipid-antigen recognition in avian immunity. Journal of Immunology 184 (2010), 2504–2511.
22. Garboczi, D.N., Hung, D.T., Wiley, D.C., HLA-A2-peptide complexes—refolding and crystallization of molecules expressed in Escherichia coli and complexed with single antigenic peptides. Proceedings of the National Academy of Sciences of the United States of America 89 (1992), 3429–3433.
23. Hee, C.S., Gao, S., Miller, M.M., Goto, R.M., Ziegler, A., Daumke, O., Uchanska-Ziegler, B., Expression, purification and preliminary X-ray crystallographic analysis of the chicken MHC class I molecule YF1*7.1. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications 65 (2009), 422–425.
24. Sherman, M.A., Goto, R.M., Moore, R.E., Hunt, H.D., Lee, T.D., Miller, M.M., Mass spectral data for 64 eluted peptides and structural modeling define peptide binding preferences for class I alleles in two chicken MHC-B haplotypes associated with opposite responses to Marek's disease. Immunogenetics 60 (2008), 527–541.
25. Hillig, R.C., Hülsmeyer, M., Saenger, W., Welfle, K., Misselwitz, R., Welfle, H., Kozerski, C., Volz, A., Uchanska-Ziegler, B., Ziegler, A., Thermodynamic and structural analysis of peptide- and allele-dependent properties of two HLA-B27 subtypes exhibiting differential disease association. Journal of Biological Chemistry 279 (2004), 652–663.
26. Fabian, H., Gast, K., Laue, M., Misselwitz, R., Uchanska-Ziegler, B., Ziegler, A., Naumann, D., Early stages of misfolding and association of beta2-microglobulin: insights from infrared spectroscopy and dynamic light scattering. Biochemistry 47 (2008), 6895–6906.
27. Kabsch, W., XDS. Acta Crystallographica. Section D, Biological Crystallography 66 (2010), 125–132.
28. McCoy, A.J., Grosse-Kunstleve, R.W., Adams, P.D., Winn, M.D., Storoni, L.C., Read, R.J., Phaser crystallographic software. Journal of Applied Crystallography 40 (2007), 658–674.
29. Murshudov, G.N., Vagin, A.A., Lebedev, A., Wilson, K.S., Dodson, E.J., Efficient anisotropic refinement of macromolecular structures using FFT. Acta Crystallographica. Section D, Biological Crystallography 55:Pt 1 (1999), 247–255.
30. Emsley, P., Lohkamp, B., Scott, W.G., Cowtan, K., Features and development of Coot. Acta Crystallographica. Section D, Biological Crystallography 66 (2010), 486–501.
31. Winn, M.D., Isupov, M.N., Murshudov, G.N., Use of TLS parameters to model anisotropic displacements in macromolecular refinement. Acta Crystallographica. Section D, Biological Crystallography 57 (2001), 122–133.
32. Laskowski, R.A., McArthur, M.W., Moss, D.S., Thornton, J.M., PROCHECK: a program to check the stereochemical quality of protein structures. Journal of Applied Crystallography 26 (1993), 283–291.
33. Chen, V.B., Arendall, W.B. III, Headd, J.J., Keedy, D.A., Immormino, R.M., Kapral, G.J., Murray, L.W., Richardson, J.S., Richardson, D.C., MolProbity: all-atom structure validation for macromolecular crystallography. Acta Crystallographica. Section D, Biological Crystallography 66 (2010), 12–21.
34. Kabsch, W., Sander, C., Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22 (1983), 2577–2637.
35. Krissinel, E., Henrick, K., Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallographica. Section D, Biological Crystallography 60 (2004), 2256–2268.
36. Dundas, J., Ouyang, Z., Tseng, J., Binkowski, A., Turpaz, Y., Liang, J., CASTp: computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues. Nucleic Acids Research 34 (2006), W116–W118.
37. DeLano, W.L., The PyMOL Molecular Graphics System on World Wide Web, 2002 http://www.pymol.org.
38. Lawrence, M.C., Colman, P.M., Shape complementarity at protein/protein interfaces. Journal of Molecular Biology 234 (1993), 946–950.
39. Kumar, P., Ziegler, A., Grahn, A., Hee, C.S., Ziegler, A., Leaving the structural ivory tower, assisted by interactive 3D PDF. Trends in Biochemical Sciences 35 (2010), 419–422.
40. Englander, S.W., Kallenbach, N.R., Hydrogen exchange and structural dynamics of proteins and nucleic acids. Quarterly Reviews of Biophysics 16 (1983), 521–655.
41. Bolzani, R., Ruggeri, F., Olivo, O.M., Average normal temperature of the chicken in the morning and after 1–2 days of fasting. Bollettino della Società Italiana di Biologia Sperimentale 55 (1979), 1618–1622.
42. Wallny, H.J., Avila, D., Hunt, L.G., Powell, T.J., Riegert, P., Salomonsen, J., Skjodt, K., Vainio, O., Vilbois, F., Wiles, M.V., Kaufman, J., Peptide motifs of the single dominantly expressed class I molecule explain the striking MHC-determined response to Rous sarcoma virus in chickens. Proceedings of the National Academy of Sciences of the United States of America 103 (2006), 1434–1439.
43. Ziegler, A., Loll, B., Misselwitz, R., Uchanska-Ziegler, B., Implications of structural and thermodynamic studies of HLA-B27 subtypes exhibiting differential association with ankylosing spondylitis. Advances in Experimental Medicine and Biology 649 (2009), 177–195.
44. Verdone, G., Corazza, A., Viglino, P., Pettirossi, F., Giorgetti, S., Mangione, P., Andreola, A., Stoppini, M., Bellotti, V., Esposito, G., The solution structure of human β2-microglobulin reveals the prodromes of its amyloid transition. Protein Science 11 (2002), 487–499.
45. Trinh, C.H., Smith, D.P., Kalverda, A.P., Phillips, S.E., Radford, S.E., Crystal structure of monomeric human β-2-microglobulin reveals clues to its amyloidogenic properties. Proceedings of the National Academy of Sciences of the United States of America 99 (2002), 9771–9776.
46. 2-microglobulin formed at pH 7.0. Journal of Biochemistry 142 (2007), 413–419.
47. 2-microglobulin: insights into the evolutionary origin of immunoglobulin superfamily constant molecules. Journal of Biological Chemistry 285 (2010), 22505–22512.
48. 1H NMR assignments and secondary structure of human β2-microglobulin in solution. Biochemistry 31 (1992), 8906–8915.
49. Ricagno, S., Raimondi, S., Giorgetti, S., Bellotti, V., Bolognesi, M., Human beta-2 microglobulin W60V mutant structure: implications for stability and amyloid aggregation. Biochemical and Biophysical Research Communications 380 (2009), 543–547.
50. Macdonald, I.K., Harkiolaki, M., Hunt, L., Connelley, T., Carroll, A.V., MacHugh, N.D., Graham, S.P., Jones, E.Y., Morrison, W.I., Flower, D.R., Ellis, S.A., MHC class I bound to an immunodominant Theileria parva epitope demonstrates unconventional presentation to T cell receptors. PLoS Pathogens, 6, 2010, e1001149.
51. Girardi, E., Wang, J., Mac, T.T., Versluis, C., Bhowruth, V., Besra, G., Heck, A.J., Van Rhijn, I., Zajonc, D.M., Crystal structure of bovine CD1b3 with endogenously bound ligands. Journal of Immunology 185 (2010), 376–386.
52. Rückert, C., Fiorillo, M.T., Loll, B., Moretti, R., Biesiadka, J., Saenger, W., Ziegler, A., Sorrentino, R., Uchanska-Ziegler, B., Conformational dimorphism of self-peptides and molecular mimicry in a disease-associated HLA-B27 subtype. Journal of Biological Chemistry 281 (2006), 2306–2316.
53. Bjorkman, P.J., Saper, M.A., Samraoui, B., Bennett, W.S., Strominger, J.L., Wiley, D.C., Structure of the human class I histocompatibility antigen, HLA-A2. Nature 329 (1987), 506–512.