Molecular Interactions between a Recombinant IgE Antibody and the β-Lactoglobulin Allergen

Structure

Volumn 15, Issue 11, 2007, Pages 1413-1421

  Niemi, Merja ^a   Jylhä, Sirpa ^b   Laukkanen, Marja Leena ^b   Söderlund, Hans ^b   Mäkinen Kiljunen, Soili ^c   Kallio, Johanna M ^a   Hakulinen, Nina ^a   Haahtela, Tari ^c   Takkinen, Kristiina ^b   Rouvinen, Juha ^a  

^a UNIVERSITY OF EASTERN FINLAND   (Finland)

^b VTT TECHNICAL RESEARCH CENTRE OF FINLAND   (Finland)

^c HELSINKI UNIVERSITY CENTRAL HOSPITAL   (Finland)

Author keywords

MOLIMMUNO

Indexed keywords

BETA LACTOGLOBULIN; IMMUNOGLOBULIN E ANTIBODY; POLYPEPTIDE;

ALLERGY; ARTICLE; CRYSTAL STRUCTURE; EPITOPE MAPPING; IMMUNITY; MOLECULAR INTERACTION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN STRUCTURE;

ALLERGENS; AMINO ACID SEQUENCE; ANIMALS; CATTLE; CRYSTALLOGRAPHY, X-RAY; EPITOPES; IMMUNOGLOBULIN E; LACTOGLOBULINS; MOLECULAR SEQUENCE DATA; RECOMBINANT PROTEINS;

BOVINAE;

EID: 35748953107     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2007.09.012     Document Type: Article

References (51)

1. Aalberse R.C. Structural biology of allergens. J. Allergy Clin. Immunol. 106 (2000) 228-238
2. Al-Lazikani B., Lesk A.M., and Chothia C. Standard conformations for the canonical structures of immunoglobulins. J. Mol. Biol. 273 (1997) 927-948
3. Andersen P.H., Nielsen M., and Lund O. Prediction of residues in discontinuous B-cell epitopes using protein 3D structures. Protein Sci. 15 (2006) 2558-2567
4. Bannon G.A., and Ogawa T. Evaluation of available IgE-binding epitope data and its utility in bioinformatics. Mol. Nutr. Food Res. 50 (2006) 638-644
5. Böcskei Z., Groom C.R., Flower D.R., Wright C.E., Phillips S.E.V., Cavaggioni A., Findlay J.B.C., and North A.C.T. Pheromone binding to two rodent urinary proteins revealed by X-ray crystallography. Nature 360 (1992) 186-188
6. Brownlow S., Cabral J.H.M., Cooper R., Flower D.R., Yewdall S.J., Polikarpov I., North A.C.T., and Sawyer L. Bovine β-lactoglobulin at 1.8 Å resolution-still an enigmatic lipocalin. Structure 5 (1997) 481-495
7. Brünger A.T., Adams P.D., Clore G.M., DeLano W.L., Gros P., Grosse-Kunstleve R.W., Jiang J.-S., Kuszewski J., Nilges M., Pannu N.S., et al. Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr. D Biol. Crystallogr. 54 (1998) 905-921
8. CCP4 (Collaborative Computational Project, Number 4). The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50 (1994) 760-763
9. Clement G., Boquet D., Frobert Y., Bernard H., Negroni L., Chatel J.-M., Adel-Patient K., Creminon C., Wal J.-M., and Grassi J. Epitopic characterization of native bovine β-lactoglobulin. J. Immunol. Methods 266 (2002) 67-78
10. Davies D.R., and Cohen G.H. Interactions of protein antigens with antibodies. Proc. Natl. Acad. Sci. USA 93 (1996) 7-12
11. De Genst E., Silence K., Decanniere K., Conrath K., Loris R., Kinne J., Muyldermans S., and Wyns L. Molecular basis for the preferential cleft recognition by dromedary heavy-chain antibodies. Proc. Natl. Acad. Sci. USA 103 (2006) 4586-4591
12. DeLano, W.L. (2002) The PyMol Molecular Graphics System (http://www.pymol.org).
13. H antibody fragment in complex with lysozyme. Nat. Struct. Biol. 3 (1996) 803-811
14. Eriksson T.L.J., Whitley P., Johansson E., van Hage-Hamsten M., and Gafvelin G. Identification and characterisation of two allergens from the dust mite Acarus siro, homologous with fatty acid-binding proteins. Int. Arch. Allergy Immunol. 119 (1999) 275-281
15. Evans E.J., Esnouf R.M., Manso-Sancho R., Gilbert R.J.C., James J.R., Yu C., Fennelly J.A., Vowles C., Hanke T., Walse B., et al. Crystal structure of a soluble CD28-Fab complex. Nat. Immunol. 6 (2005) 271-279
16. Fahlbusch B., Rudeschko O., Schlott B., Henzgen M., Schlenvoigt G., Schubert H., and Kinne R.W. Further characterization of IgE-binding antigens from guinea pig hair as new members of the lipocalin family. Allergy 58 (2003) 629-634
17. Flicker S., Steinberger P., Nordenhaug L., Sperr W.R., Majlesi Y., Valent P., Kraft D., and Valenta R. Conversion of grass pollen allergen-specific human IgE into a protective IgG1 antibody. Eur. J. Immunol. 32 (2002) 2156-2162
18. Flicker S., Steinberger P., Ball T., Krauth M.-T., Verdino P., Valent P., Almo S., and Valenta R. Spatial clustering of the IgE epitopes on the major timothy grass pollen allergen Phl p 1, importance for allergenic activity. J. Allergy Clin. Immunol. 117 (2006) 1336-1343
19. α. Nature 406 (2000) 259-266
20. Hantusch B., Schöll I., Harwanegg C., Krieger S., Becker W.-M., Spitzauer S., Boltz-Nitulescu G., and Jensen-Jarolim E. Affinity determinations of purified IgE and IgG antibodies against the major pollen allergens Phl p 5a and Bet v 1a: discrepancy between IgE and IgG binding strength. Immunol. Lett. 97 (2005) 81-89
21. James L.C., Roversi P., and Tawfik D.S. Antibody multispecificity mediated by conformational diversity. Science 299 (2003) 1362-1367
22. Järvinen K.-M., Chatchatee P., Bardina L., Beyer K., and Sampson H.A. IgE and IgG binding epitopes on α-lactalbumin and β-lactoglobulin in cow's milk allergy. Int. Arch. Allergy Immunol. 126 (2001) 111-118
23. Jenkins J.A., Griffiths-Jones S., Shewry P.R., Breiteneder H., and Mills E.N.C. Structural relatedness of plant food allergens with specific reference to cross-reactive allergens: an in silico analysis. J. Allergy Clin. Immunol. 115 (2005) 163-170
24. Jones T.A., Zou J.-Y., Cowan S.W., and Kjeldgaard M. Improved methods for building protein models on electron density maps and the location of errors in these models. Acta Crystallogr. A 47 (1991) 110-119
25. Kamata Y., Miyanomae A., Nakayama E., Miyanomae T., Tajima T., Nishimura K., Tada T., and Hoshi H. Characterization of dog allergens Can f 1 and Can f 2. A comparison of Can f 1 with Can f 2 regarding their biochemical and immunological properties. Int. Arch. Allergy Immunol. 142 (2007) 301-308
26. Larché M., Akdis C.A., and Valenta R. Immunological mechanisms of allergen-specific immunotherapy. Nat. Rev. Immunol. 6 (2006) 761-771
27. Lascombe M.-B., Grégoire C., Poncet P., Tavares G.A., Rosinski-Chupin I., Rabillon J., Goubran-Botros H., Mazie J.-C., David B., and Alzari P.M. Crystal structure of the allergen Equ c 1. A dimeric lipocalin with restricted IgE-reactive epitopes. J. Biol. Chem. 275 (2000) 21572-21577
28. Laukkanen M.-L., Mäkinen-Kiljunen S., Isoherranen K., Haahtela T., Söderlund H., and Takkinen K. Hevein-specific recombinant IgE antibodies from human single-chain antibody phage display libraries. J. Immunol. Methods 278 (2003) 271-281
29. Laver W.G., Air G.M., Webster R.G., and Smith-Gill S.J. Epitopes on protein antigens: misconceptions and realities. Cell 61 (1990) 553-556
30. Mirza O., Henriksen A., Ipsen H., Larsen J.N., Wissenbach M., Spangfort M.D., and Gajhede M. Dominant epitopes and allergic cross-reactivity: complex formation between a Fab fragment of a monoclonal murine IgG antibody and the major allergen from birch pollen Bet v 1. J. Immunol. 165 (2000) 331-338
31. Morea V., Tramontano A., Rustici M., Chothia C., and Lesk A.M. Conformations of the third hypervariable region in the VH domain of immunoglobulins. J. Mol. Biol. 275 (1998) 269-294
32. Nevanen T.K., Söderholm L., Kukkonen K., Suortti T., Teerinen T., Linder M., Söderlund H., and Teeri T.T. Efficient enantioselective separation of drug enantiomers by immobilised antibody fragments. J. Chromatogr. A. 925 (2001) 89-97
33. Oksanen E., Jaakola V.-P., Tolonen T., Valkonen K., Åkerström B., Kalkkinen N., Virtanen V., and Goldman A. Reindeer β-lactoglobulin crystal structure with pseudo-body-centred noncrystallographic symmetry. Acta Crystallogr. D Biol. Crystallogr. 62 (2006) 1369-1374
34. Padavattan S., Schirmer T., Schmidt M., Akdis C., Valenta R., Mittermann I., Soldatova L., Slater J., Mueller U., and Markovic-Housley Z. Identification of a B-cell epitope of hyaluronidase, a major bee venom allergen, from its crystal structure in complex with a specific Fab. J. Mol. Biol. 368 (2007) 742-752
35. Padlan E.A., Silverton E.W., Sheriff S., Cohen G.H., Smith-Gill S.J., and Davies D.R. Structure of an antibody-antigen complex: crystal structure of the HyHEL-10 Fab-lysozyme complex. Proc. Natl. Acad. Sci. USA 86 (1989) 5938-5942
36. Pierson-Mullany L.K., Jackola D.R., Blumenthal M.N., and Rosenberg A. Characterization of polyclonal allergen-specific IgE responses by affinity distributions. Mol. Immunol. 37 (2000) 613-620
37. Radauer C., and Breiteneder H. Pollen allergens are restricted to few protein families and show distinct patterns of species distribution. J. Allergy Clin. Immunol. 117 (2006) 141-147
38. Riemer A., Scheiner O., and Jensen-Jarolim E. Allergen mimotopes. Methods 32 (2004) 321-327
39. Rouvinen J., Rautiainen J., Virtanen T., Zeiler T., Kauppinen J., Taivainen A., and Mäntyjärvi R. Probing the molecular basis of allergy. Three-dimensional structure of the bovine lipocalin allergen Bos d 2. J. Biol. Chem. 274 (1999) 2337-2343
40. Saarelainen S., Zeiler T., Rautiainen J., Närvänen A., Rytkönen-Nissinen M., Mäntyjärvi R., Vilja P., and Virtanen T. Lipocalin allergen Bos d 2 is a weak immunogen. Int. Immunol. 14 (2002) 401-409
41. Sakurai K., and Goto Y. Manipulating monomer-dimer equilibrium of bovine β-lactoglobulin by amino acid substitution. J. Biol. Chem. 277 (2002) 25735-25740
42. Saphire E.O., Parren P.W., Pantophlet R., Zwick M.B., Morris G.M., Rudd P.M., Dwek R.A., Stanfield R.L., Burton D.R., and Wilson I.A. Crystal structure of a neutralizing human IgG against HIV-1: a template for vaccine design. Science 293 (2001) 1155-1159
43. Schöll I., Kalkura N., Shedziankova Y., Bergmann A., Verdino P., Knittelfelder R., Kopp T., Hantusch B., Betzel C., Dierks K., et al. Dimerization of the major birch pollen allergen Bet v 1 is important for its in vivo IgE-cross-linking potential in mice. J. Immunol. 175 (2005) 6645-6650
44. Stanfield R.L., Dooley H., Flajnik M.F., and Wilson I.A. Crystal structure of a shark single-domain antibody V region in complex with lysozyme. Science 305 (2004) 1770-1773
45. Stanfield R.L., Zemla A., Wilson I.A., and Rupp B. Antibody elbow angles are influenced by their light chain class. J. Mol. Biol. 357 (2006) 1566-1574
46. Steinberger P., Kraft D., and Valenta R. Construction of a combinatorial IgE library from an allergic patient. J. Biol. Chem. 271 (1996) 10967-10972
47. Thornton J.M., Edwards M.S., Taylor W.R., and Barlow D.J. Location of 'continuous' antigenic determinants in the protruding regions of proteins. EMBO J. 5 (1986) 409-413
48. Wal J.-M. Cow's milk allergens. Allergy 53 (1998) 1013-1022
49. Wan T., Beavil R.L., Fabiane S.M., Beavil A.J., Sohi M.K., Keown M., Young R.J., Henry A.J., Owens R.J., Gould H.J., et al. The crystal structure of IgE Fc reveals an asymmetrically bent conformation. Nat. Immunol. 3 (2002) 681-686
50. Williams S.C., Badley R.A., Davis P.J., Puijk W.C., and Meloen R.H. Identification of epitopes within beta lactoglobulin recognised by polyclonal antibodies using phage display and PEPSCAN. J. Immunol. Methods 213 (1998) 1-17
51. Yazdanbakhsh M., Kremsner P.G., and van Ree R. Allergy, parasites, and the hygiene hypothesis. Science 296 (2002) 490-494