Reduced immunogenicity of β-lactoglobulin by conjugation with acidic oligosaccharides

Journal of Agricultural and Food Chemistry

Volumn 52, Issue 14, 2004, Pages 4546-4553

  Hattori, Makoto ^a   Miyakawa, Shunpei ^a   Ohama, Yukie ^a   Kawamura, Hiroyuki ^a   Yoshida, Tadashi ^a   To O, Kenji ^b   Kuriki, Takashi ^b   Takahashi, Koji ^a  

^a TOKYO UNIVERSITY OF AGRICULTURE AND TECHNOLOGY   (Japan)

^b EZAKI GLICO CO LTD   (Japan)

Author keywords

lactoglobulin; Acidic saccharide; Alginate lyase; Alginic acid; Emulsification; Functional improvement; Lipocalin; Neoglycoconjugate; Protein conjugation; Retinol binding; Solubility

Indexed keywords

ALGINIC ACID; ALGINIC ACID OLIGOSACCHARIDE; BETA LACTOGLOBULIN; EPITOPE; LYASE; MONOCLONAL ANTIBODY; OLIGOSACCHARIDE; RETINOL; UNCLASSIFIED DRUG;

ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL MODEL; ANTIBODY RESPONSE; ARTICLE; B LYMPHOCYTE; CIRCULAR DICHROISM; CONJUGATION; CONTROLLED STUDY; EMULSION; EPITOPE MAPPING; FEMALE; FOOD PROCESSING; IMMUNOGENICITY; ISOELECTRIC POINT; MILK ALLERGY; MOUSE; NONHUMAN; PROTEIN MODIFICATION; SOLUBILITY;

ALLERGENS; ANIMALS; BINDING SITES; CATTLE; DRUG STABILITY; EPITOPES; FEMALE; HEAT; IMMUNIZATION; LACTOGLOBULINS; MAILLARD REACTION; MICE; MICE, INBRED BALB C; MICE, INBRED C3H; MICE, INBRED C57BL; OLIGOSACCHARIDES; VITAMIN A;

ANIMALIA; BOVINAE;

EID: 3142581377     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf0353887     Document Type: Article

References (40)

1. Flower, D. R. The lipocalin protein family: structure and function. Biochem. J. 1996, 318, 1-14.
2. Sawyer, L.; Kontopidis, G. The core lipocalin, bovine β-lactoglobulin. Biochim. Biophys. Acta 2000, 1482, 136-148.
3. McKenzie, H. A.; β-Lactoglobulins. In Milk Proteins: Chemistry and Molecular Biology; McKenzie, H. A., Ed.; Academic Press: New York, 1971; Vol. 2, pp 257-330.
4. Pérez, M. D.; Calvo, M. Interaction of β-lactoglobulin with retinol and fatty acids and its role as a possible biological function for this protein. J. Dairy Sci. 1995, 78, 978-988.
5. Shimizu, M.; Saito, M.; Yamauchi, K. Emulsifying and structural properties of β-lactoglobulin at different pHs. Agric. Biol. Chem. 1985, 49, 189-194.
6. Waniska, R. D.; Kinsella, J. E. Foaming and Emulsifying properties of glycosylated β-lactoglobulin. Food Hydrocolloids 1988, 2, 439-449.
7. Foegeding, E. A.; Kuhn, P. R.; Hardin, C. C. Specific divalent cation-induced changes during gelation of β-lactoglobulin. J. Agric. Food Chem. 1992, 40, 2092-2097.
8. Spies, J. Milk allergy. J. Milk Food Technol. 1973, 36, 225-231.
9. Hattori, M. Functional improvements in food proteins in multiple aspects by conjugation with saccharides: Case studies of β-lactoglobulin-acidic polysaccharides conjugates. Food Sci. Technol. Res. 2002, 8, 291-299.
10. Hattori, M.; Nagasawa, K.; Ametani, A.; Kaminogawa, S.; Takahashi, K. Functional changes in β-lactoglobulin by conjugation with carboxymethyl dextran. J. Agric. Food Chem. 1994, 42, 2120-2125.
11. Nagasawa, K.; Takahashi, K.; Hattori, M. Improved emulsifying properties of β-lactoglobulin by conjugating with carboxymethyl dextran. Food Hydrocolloids 1996, 10, 63-67.
12. Hattori, M.; Nagasawa, K.; Ohgata, K.; Sone, N.; Fukuda, A.; Matsuda, H.; Takahashi, K. Reduced Immunogenicity of β-lactoglobulin by conjugation with carboxymethyl dextran. Bioconjugate Chem. 2000, 11, 84-93.
13. Kobayashi, K.; Hirano, A.; Ohta, A.; Yoshida, T.; Takahashi, K.; Hattori, M. Reduced immunogenicity of β-lactoglobulin by conjugation with carboxymethyl dextrans differing in molecular weight. J. Agric. Food Chem. 2001, 49, 823-831.
14. Kobayashi, K.; Yoshida, T.; Takahashi, K.; Hattori, M. Modulation of T cell response to β-lactoglobulin by conjugation with carboxymethyl dextran. Bioconjugate Chem. 2003, 14, 168-176.
15. Hattori, M.; Aiba, Y.; Nagasawa, K.; Takahashi, K. Functional improvements in alginic acid by conjugating with β-lactoglobulin. J. Food Sci. 1996, 61, 1171-1176.
16. Hattori, M.; Ogino, A.; Nakai, H.; Takahashi, K. Functional improvement of β-lactoglobulin by conjugating with alginate lyase-lysate. J. Agric. Food Chem. 1997, 45, 703-708.
17. Hattori, M.; Numamoto, K.; Kobayashi, K.; Takahashi, K. Functional changes in β-lactoglobulin by conjugation with cationic saccharides. J. Agric. Food Chem. 2000, 48, 2050-2056.
18. Hattori, M.; Okada, Y.; Takahashi, K. Functional changes in β-lactoglobulin upon conjugation with carboxymethyl cyclodextrin. J. Agric. Food Chem. 2000, 48, 3789-3794.
19. Sehon, A. H. Suppression of IgE antibody responses with tolerogenic conjugates of allergens and haptens. Prog. Allergy 1982, 32, 161-202.
20. Amit, A. G.; Mariuzza, R. A.; Phillips, S. E.; Poljak, R. J. Three-dimensional structure of an antigen-antibody complex at 2.8 Å resolution. Science 1986, 233, 747-753.
21. So, T.; Ito, H.; Hirata, M.; Ueda, T.; Imoto, T. Contribution of conformational stability of hen lysozyme to induction of type 2 T-helper immune responses. Immunology 2001, 104, 259-268.
22. Armstrong, J. M.; McKenzie, H. A.; Sawyer, W. H. On the fractionation of β-lactoglobulin and α-lactalbumin. Biochim. Biophys. Acta 1967, 147, 60-72.
23. Davis, B. J. Disc electrophoresis-II: Method and application to human serum proteins. Ann. N. Y. Acad. Sci. 1964, 121, 404-427.
24. Kaminogawa, S.; Shimizu, M.; Ametani, A.; Hattori, M.; Ando, O.; Hachimura, S.; Nakamura, Y.; Totsuka, M.; Yamauchi, K. Monoclonal antibodies as probes for monitoring the denaturation process of bovine β-lactoglobulin. Biochim. Biophys Acta 1989, 998, 50-56.
25. Kamasaka, H.; Uchida, M.; Kusaka, K.; Yoshikawa, K.; Yamamoto, K.; Okada, S.; Ichikawa, T. Inhibitory effect of phosphorylated oligosaccharides prepared from potato starch on the formation of calcium phosphate. Biosci., Biotechnol., Biochem. 1995, 59, 1412-1416.
26. Takahashi, K.; Shirai, K.; Wada, K. Melting behavior of gels prepared from isolated subunits of collagen. J. Food Sci. 1988, 53, 1920-1921.
27. Kaminogawa, S.; Hattori, M.; Ando, O.; Kurisaki, J.; Yamauchi, K. Preparation of monoclonal antibody against bovine β-lactoglobulin and its unique affinity. Agric. Biol. Chem. 1987, 51, 797-802.
28. Hattori, M.; Ametani, A.; Katakura, Y.; Shimizu, M.; Kaminogawa, S. Unfolding/refolding studies on bovine β-lactoglobulin with monoclonal antibodies as probes: does a renatured protein completely refold? J. Biol. Chem. 1993, 268, 22414-22419.
29. Hogg, P. J.; Johnson, S. C.; Bowles, M. R.; Pond, S. M.; Winzor, D. J. Evaluation of equilibrium constants for antigen-antibody interaction by solid-phase immunoassay: the binding of paraquant to its elicited mouse monoclonal antibody. Mol. Immunol. 1987, 24, 797-801.
30. Ball, G.; Shelton, M. J.; Walth, B. J.; Hill, D. J.; Hosking, C. S.; Howden, M. E. H. A major continuous allergenic epitope of bovine β-lactoglobulin recognized by human IgE binding. Clin. Exp. Allergy 1994, 24, 758-764.
31. Kohri, E.; Maurice, L.; Bourgeois, C.; Bour, J. B.; Pothier, P. Epitope mapping of the major inner capsid protein of group A rotavirus using peptide synthesis. Virology 1993, 194, 110-116.
32. Gammon, G.; Geysen, H. M.; Apple, R. J.; Pickett, E.; Palmer, M.; Ametani, A.; Sercarz, E. E. T cell determinant structure: cores and determinant envelopes in three mouse major histocompatibility complex haplotypes. J. Exp. Med. 1991, 173, 609-617.
33. Bradford, M. M. A rapid and sensitive method for the quantitation of misrogram quantities of of proteins utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72, 248-254.
34. Dubois, M.; Gilles, K. A.; Hamilton, J. K.; Rebers, P. A.; Smith, F. Colorimetric method for determination of sugars and related substances. Anal. Chem. 1956, 28, 350-356.
35. Fugate, R.; Song, P. Spectroscopic Characterization of β-lactoglobulin-retinol complex. Biochim. Biophys. Acta 1980, 625, 28-42.
36. Futterman, S.; Heller, J. The enhancement of fluorescence and decreased susceptibility to enzyme oxidation of retinol complexed with bovine serum albumin, β-lactoglobulin, and the retinol-binding protein of human plasma. J. Biol. Chem. 1972, 247, 5168-5172.
37. Cogan, U.; Kopelman, M.; Mokady, S.; Shintzky, M. Binding affinities of retinol and related compounds to retinol binding proteins. Eur. J. Biochem. 1976, 65, 71-78.
38. Takata, M.; Maiti, P. K.; Kubo, R. T.; Chen, Y. H.; Holford, S. V.; Rector, E. S.; Sehon, A. H. Cloned suppressor T cells derived from mice tolerized with conjugates of antigen and monomethoxypolyethylene glycol. Relationship between monoclonal T suppressor factor and the T cell receptor. J. Immunol. 1990, 145, 2846-2853.
39. So, T.; Ito, H. O.; Koga, T.; Watanabe, S.; Ueda, T.; Imoto, T. Depression of T-cell epitope generation by stabilizing hen lysozyme. J. Biol. Chem. 1997, 272, 32136-32140.
40. Ito, H. O.; So, T.; Hirata, M.; Koga, T.; Ueda, T.; Imoto, T. Tolerogenic activity of polyethylene glycol-conjugated lysozyme distinct from that of the native counterpart. Immunology 1998, 93, 200-207.