Monoclonal antibody specific to a major fish allergen: Parvalbumin

Journal of Food Protection

Volumn 72, Issue 4, 2009, Pages 818-825

  Gajewski, Kamil G ^a   Hsieh, Yun Hwa P ^a  

^a FLORIDA STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALIA; ANURA; ORYCTOLAGUS CUNICULUS; RATTUS;

EID: 64049094761     PISSN: 0362028X     EISSN: None     Source Type: Journal    
DOI: 10.4315/0362-028X-72.4.818     Document Type: Article

References (41)

1. Aas, K., and S. Elsayed. 1975. Physico-chemical properties and specific activity of a purified allergen (codfish). Dev. Biol. Stand. 29: 90-98.
2. Bahna, S. L. 2004. You can have fish allergy and eat it too! J. Allergy Clin. Immunol. 114:125-126.
3. 2+-binding proteins parvalbumin and oncomod-ulin. Biochem. Biophys. Acta 1009:201-215.
4. Bugajska-Schretter, A., M. Grote, L. Vangelista, P. Valent, W. R. Sperr, H. Rumpold, A. Pastore, R. Reichelt, R. Valenta, and S. Spit-zauer. 2000. Purification, biochemical, and immunological characterisation of a major food allergen: different immunoglobulin E recognition of the apo-and calcium-bound forms of carp parvalbumin. Gut 46:661-669.
5. Chen, L., S. L. Hefle, S. L. Taylor, I. Swoboda, and R. E. Goodman. 2006. Detecting fish parvalbumin with commercial mouse monoclonal anti-frog parvalbumin IgG. J. Agric. Food Chem. 54:5577-5582.
6. Crick, F. H. C. 1953. The packing of alpha-helices-simple coiled-coils. Acta Crystallogr. 6:689-697.
7. de Martino, M., E. Novembre, L. Galli, A. de Marco, P. Botarelli, E. Marano, and A. Vierucci. 1990. Allergy to different fish species in cod-allergic children: in vivo and in vitro studies. . Allergy Clin. Immunol. 86:909-914.
8. Elsayed, S., and K. Aas. 1971. Characterization of a major allergen (cod): observations on effect of denaturation on the allergenic activity. J. Allergy 47:283-291.
9. Elsayed, S., and H. Bennich. 1975. The primary structure of allergen M from cod. Scand. J. Immunol. 4:203-208.
10. Friguet, B., L. Djavadi-Ohaniance, J. Pages, A. Bussard, and M. Goldberg. 1983. A convenient enzyme-linked immunosorbent assay for testing whether monoclonal antibodies recognize the same anti-genic site. Application to hybridomas specific for the beta 2-subunit of Escherichia coli tryptophan synthase. J. Immunol. Methods 60: 351-358.
11. Gerday, C. 1982. Soluble calcium-binding proteins from fish and invertebrate muscle. Mol. Physiol. 2:63-87.
12. Goodman, M., J. F. Pechere, J. Haiech, and J. G. Demaille. 1979. Evolutionary diversification of structure and function in the family of intracellular calcium-binding proteins. J. Mol. Evol. 13:331-352.
13. Hamada, Y., H. Tanaka, S. Ishίzaki, M. Ishida, Y. Nagashima, and K. Shiomi. 2003. Purification, reactivity with IgE and cDNA cloning of parvalbumin as the major allergen of mackerels. Food Chem. Toxicol. 41:1149-1156.
14. Heeley, D. H., T. Bieger, D. M. Waddleton, C. Hong, D. M. Jackman, C. Mcgowan, W. S. Davidson, and R. C. Beavis. 1995. Characterization of fast, slow and cardiac-muscle tropomyosins from salmonid fish. Eur. J. Biochem. 232:226-234.
15. Heeley. D. H., and C. Hong. 1994. Isolation and characterization of tropomyosin from fish muscle. Comp. Biochem. Physiol. Biochem. Mol. Biol. 108:95-106.
16. Heizmann, C. W., M. W. Berchtold, and A. M. Rowlerson. 1982. Correlation of parvalbumin concentration with relaxation speed in mammalian muscles. Proc. Natl. Acad. Sci. USA 79:7243-7247.
17. Hilger, C, L. Thill, F. Grigioni, C. Lehners, P. Falagiani, A. Ferrara, C. Romano, W. Stevens, and F. Hentges. 2004. IgE antibodies of fish allergic patients cross-react with frog parvalbumin. Allergy 59:653-660.
18. Huriaux, F., P. Vandewalle, and B. Focant. 2002. Immunological study of muscle parvalbumin isotypes in three African catfish during development. Comp. Biochem. Physiol. Biochem. Mol. Biol. 132: 579-584.
19. Ikura, M. 1996. Calcium binding and conformational response in EF-hand proteins. Trends Biochem. Sci. 21:14-17.
20. King, T. P., D. Hoffman, H. Lowenstein, D. G. Marsh, T. A. Platts-Mills, and W. Thomas. 1994. Allergen nomenclature. WHO/IUIS allergen nomenclature subcommittee. Int. Arch. Allergy Immunol. 105:224-233.
21. Kobayashi, A., H. Tanaka, Y. Hamada, S. Ishizaki, Y. Nagashima, and K. Shiomi. 2006. Comparison of allergenicity and allergens between fish white and dark muscles. Allergy 61:357-363.
22. Köhler, G., and C. Milstein. 1975. Continuous cultures of fused cells secreting antibody of predefined specificity. Nature 256:495-497.
23. Laemmli, U. K. 1970. Cleavage of structural proteins during assembly of head of bacteriophage-T4. Nature 227:680-685.
24. Lehrer, S, B., R. Ayuso, and G. Reese. 2003. Seafood allergy and allergens: a review. Mar. Biotechnol. (NY) 5:339-348.
25. Lehrer, S. B., W. E. Horner, and G. Reese. 1996. Why are some proteins allergenic? Implications for biotechnology. Crit. Rev. Food Sci. Nutr. 36:553-564.
26. Leung, P. S. C, Y. C. Chen, D. L. Mykles, W. K. Chow, C. P. Li, and K. H. Chu. 1998. Molecular identification of the lobster muscle protein tropomyosin as a seafood allergen. Mol. Mar. Biol. Biotech-nol. 7:12-20.
27. Lindstrom, C. D., T. van Do, I. Hordvik, C. Endresen, and S. Elsay-ed. 1996. Cloning of two distinct cDNAs encoding parvalbumin, the major allergen of Atlantic salmon (Salmo salar). Scand. J. Immunol. 44:335-344.
28. Muntener, M., L. Kaser, J. Weber, and M. W. Berchtold. 1995. Increase of skeletal muscle relaxation speed by direct injection of par-valbumin cDNA. Proc. Natl. Acad. Sci. USA 92:6504-6508.
29. Naqpal, S., L. Rajappa, D. D. Metcalfe, and P. V. Rao. 1989. Isolation and characterization of heat-stable allergens from shrimp (Penaeus indicus). J. Allergy Clin. Immunol. 83:26-36.
30. O'Neil, C, A. A. Helbling, and S. B. Lehrer. 1993. Allergic reactions to fish. Clin. Rev. Allergy 11:183-200.
31. Pechere, J. F., J. P. Capony, and J. Demaille. 1973. Evolutionary aspects of structure of muscular parvalbumins. Syst. Zool. 22:533-548.
32. Rehbeίn, H., and R. Kundiger. 1984. Comparison of the isoelectric-focusing patterns of the sarcoplasmic proteins from red and white muscle of various fish species. Arch. Fischwiss. 35:7-16.
33. Sampson, H. A. 1999. Food allergy. Part 1: immunopathogenesis and clinical disorders. J. Allergy Clin. Immunol. 103:717-728.
34. 2+. EMBO J. 13:3481-3486.
35. Sicherer, S. H., A. Munoz-Furlong, and H. A. Sampson. 2004. Prevalence of seafood allergy in the United States determined by a random telephone survey. J. Allergy Clin. Immunol. 114:159-165.
36. Sicherer, S. H., and H. A. Sampson. 2006. 9. Food allergy. J. Allergy Clin. Immunol. 117:S470-S475.
37. Swoboda, I., A. Bugajska-Schretter, P. Verdino, W. Keller, W. R. Sperr, P. Valent, R. Valenta, and S. Spitzauer. 2002. Recombίnant carp parvalbumin, the major cross-reactive fish allergen: a tool for diagnosis and therapy of fish allergy. J. Immunol. 168:4576-4584.
38. Thatcher, D. R., and J. F. Pechere. 1977. The amino acid sequence of the major parvalbumin from thornback-ray muscle. Eur. J. Bio-chem. 75:121-132.
39. Towbin, H., T. Staehelin, and J. Gordon. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76: 4350-4354.
40. U.S. Food and Drug Administration. 2005. Questions and answers regarding food allergens, including the Food Allergen Labeling and Consumer Protection Act of 2004. Available at: http://www.cfsan.fda.gov/~dms/alrguid.html. Accessed 10 November 2008.
41. Van Do, T., I. Hordvik, C. Endresen, and S. Elsayed. 2005. Characterization of parvalbumin, the major allergen in Alaska pollack, and comparison with codfish Allergen M. Mol. Immunol. 42:345-353.