Research Progress in Conformational Epitope Mapping Approaches for Food Allergens

Abstract

Abstract: Conformational epitope is an important type of epitope and plays a critical role in allergy. Epitope mapping is the core of allergen research. Today, there are three main conformational epitope mapping approaches, including conformational epitope prediction based on the amino acid composition and characteristics of linear epitopes, epitope mapping by phage display technique and bioinformatics, and conformational epitope mapping by spectroscopic analysis and parameters related to coupling with antibodies. The first two approaches are commonly used in conformational epitope mapping. As a more accurate approach, spectroscopy has not been used in this field until recently. These approaches allow for a better knowledge and understanding of conformational epitopes in allergen research and also provide theoretical evidence for the mechanisms of action of conformational epitopes in allergy.

Key words: food allergen, conformational epitope, mapping

CLC Number:

TS201.6

Hong-bing CHEN. Research Progress in Conformational Epitope Mapping Approaches for Food Allergens[J]. FOOD SCIENCE, 2012, 33(17): 279-283.

References

[1]Van Regenmortel M. What is a B-cell epitope?[J] Methods Mol Bio, 2009,524:3.
[2]Barre A, Borges JP, Culerrier R, et al. Homology modelling of the major peanut allergen Ara h 2 and surface mapping of IgE-binding epitopes[J]. Immunol Lett, 2005, 100(2):153-158.
[3]Rougé P, Culerrier R, Sabatier V, et al. Mapping and conformational analysis of IgE-binding epitopic regions on the molecular surface of the major Ara h 3 legumin allergen of peanut (Arachis hypogaea) [J]. Mol Immunol, 2009, 46(6): 1067-1075.
[4]Midoro-Horiuti T, Schein CH, Mathura V, et al. Structural basis for epitope sharing between group 1 allergens of cedar pollen[J]. Mol Immunol, 2006, 43(6): 509-518.
[5]López-Torrejón G, Díaz-Perales A, Rodríguez J, et al. An experimental and modeling-based approach to locate IgE epitopes of plant profilin allergens[J]. J Allergy Clin Immunol 2007, 119(6):1481-1488.
[6]Pali-Scholl I, Jensen-Jarolim E. Biopanning for the Characterization of Allergen Mimotopes[J]. Methods Mol Med, 2008, 138:271.
[7]Leitner A, Vogel M, Radauer C, et al. A mimotope defined by phage display inhibits IgE binding to the plant panallergen profilin[J]. Eur J Immunol, 1998, 28(9): 2921-2927.
[8]Ganglberger E, Grunberger K, Sponer B, et al. Allergen mimotopes for 3-dimensional epitope search and induction of antibodies inhibiting human IgE[J]. Faseb J, 2000, 14(14): 2177-2184.
[9]Hantusch B, Krieger S, Untersmayr E, et al. Mapping of conformational IgE epitopes on Phl p 5a by using mimotopes from a phage display library[J]. J Allergy Clin Immunol, 2004, 114 (6):1294-1300.
[10]Szalai K, Fuhrmann J, Pavkov T, et al. Mimotopes identify conformational B-cell epitopes on the two major house dust mite allergens Der p 1 and Der p 2[J]. Mol Immunol, 2008, 45(5): 1308-1317.
[11]Yang H, Liu ZH, Zhang LT, et al. Selection and application of peptide mimotopes of MPT64 protein in Mycobacterium tuberculosis[J]. J Med Microbiol, 2011, 60(Pt 1):69-74.
[12]Untersmayr E, Szalai K, Riemer AB, et al. Mimotopes identify conformational epitopes on parvalbumin, the major fish allergen[J]. Mol Immunol, 2006, 43(9): 1454-1461.
[13]Pacios LF, Tordesillas L, Cuesta-Herranz J, et al. Mimotope mapping as a complementary strategy to define allergen IgE-epitopes: peach Pru p 3 allergen as a model[J]. Mol Immunol, 2008, 45(8):2269-2276.
[14]Tordesillas L, Pacios LF, Palacin A, et al. Molecular basis of allergen cross-reactivity: non-specific lipid transfer proteins from wheat flour and peach fruit as models[J]. Mol Immunol, 2009, 47(2-3): 534-540.
[15]Tordesillas L, Pacios L, Palacín A, et al. Characterization of IgE epitopes of Cuc m 2, the major melon allergen, and their role in cross‐reactivity with pollen[J]. Clin Exp Allergy, 2010, 40(1): 174-181.
[16]Schreiber A, Humbert M, Benz A, et al. 3D-Epitope-Explorer (3DEX): localization of conformational epitopes within three-dimensional structures of proteins[J]. J Comput Chem, 2005, 26(9): 879-887.
[17]. Huang J, Gutteridge A, Honda W, et al. MIMOX: a web tool for phage display based epitope mapping [J] BMC Bioinformatics, 2006, 7: 451.
[18] Mayrose I, Penn O, Erez E, et al. Pepitope: epitope mapping from affinity-selected peptides [J]. Bioinformatics, 2007, 23: 3244-3246.
[19]王静云, 刘丹, 唐乾, 等. 圆二色谱研究Asp44 在稳定肌红蛋白结构中的作用[J]. 光谱学与光谱分析, 2008, 28(2): 426-429.
[20]万琳, 周立. 小麦PGIP 圆二色性与生物活性关系[J]. 应用与环境生物学报, 2001, 7(5): 434-437.
[21] Zsila F, Hazai E, Sawyer L. Binding of the pepper alkaloid piperine to bovine beta-lactoglobulin: circular dichroism spectroscopy and molecular modeling study[J]. J Agric Food Chem, 2005，53(26):10179-10185.
[22]刘志刚, 朱健琦, 黄海珍, 等. 真核表达与原核表达的德国小蠊变应原Bla g 2蛋白结构的光谱学研究[J]. 光谱学与光谱分析 2006;26(5):879-883.
[23]Koppelman SJ, van Koningsveld GA, Knulst AC, et al. Effect of heat-induced aggregation on the IgE binding of patatin (Sol t 1) is dominated by other potato proteins[J]. J Agric Food Chem 2002, 50(6): 1562-1568.
[24]Hu CQ, Gao JY, Chen HB, et al. Effect of heat treatment on the antigenicity and conformation of peanut allergen Ara h 2[J]. Guang Pu Xue Yu Guang Pu Fen Xi, 2010, 30(9): 2550-2554.
[25]Navarra G, Leone M, Militello V. Thermal aggregation of beta-lactoglobulin in presence of metal ions[J]. Biophys Chem, 2007,131(1-3):52-61.
[26]Rigby NM, Marsh J, Sancho AI, et al. The purification and characterisation of allergenic hazelnut seed proteins[J]. Mol Nutr Food Res, 2008, 52 Suppl 2:S251-261.
[27]Rosen O, Anglister J. Epitope mapping of antibody-antigen complexes by nuclear magnetic resonance spectroscopy[J]. Methods Mol Biol 2009, 524:37-57.
[28]Trevi o Má, García-Mayoral MF, Barral P, et al. NMR solution structure of Ole e 6, a major allergen from olive tree pollen[J]. J BIOL CHEM 2004;279(37):39035.
[29]Chan SL, Ong ST, Ong SY, et al. Nuclear magnetic resonance structure-based epitope mapping and modulation of dust mite group 13 allergen as a hypoallergen[J]. J Immunol, 2006, 176(8): 4852-4860.
[30]Chan SL, Ong TC, Gao YF, et al. Nuclear magnetic resonance structure and IgE epitopes of Blo t 5, a major dust mite allergen[J]. J Immunol, 2008, 181(4): 2586-2596.
[31]Naik MT, Chang C, Kuo IC, et al. Roles of structure and structural dynamics in the antibody recognition of the allergen proteins: an NMR study on Blomia tropicalis major allergen[J]. Structure, 2008, 16(1): 125-136.
[32]Padavattan S, Flicker S, Schirmer T, et al. High-affinity IgE recognition of a conformational epitope of the major respiratory allergen Phl p 2 as revealed by X-ray crystallography[J]. J Immunol, 2009, 182(4): 2141-2151.
[33]Chavane N, Jacquemart R, Hoemann CD, et al. At-line quantification of bioactive antibody in bioreactor by surface plasmon resonance using epitope detection[J]. Anal Biochem, 2008, 378(2): 158-165.
[34]Venien A, Levieux D, Dufour E. Oil/Alkanethiol Layers for the Study of Emulsified Protein Conformation by Surface Plasmon Resonance Using Monoclonal Antibodies[J]. J Colloid Interface Sci, 2000, 223(2): 215-222.
[35]Dhungana S, Fessler MB, Tomer KB. Epitope mapping by differential chemical modification of antigens[J]. Methods Mol Biol, 2009, 524:119-134.