Human IgG-crossreactive sarcoplasmic peptides in the freshwater catfish Rita rita
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Authors
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Santosh Kumar Gupta
-
Sasmita Mohanty
-
Arabinda Mahanty
-
Bimal Prasanna Mohanty
Head of Division (FREM)
Principal Scientist
ICAR-CIFRI, Barrackpore
Abstract
The prevalence and magnitude of clinical
allergy caused by crossreacting proteins and
panallergens appears to be increasing and reflects an
increase in allergen sensitization. Fish is reported to be
one of the most common causes of food allergic
reactions. In general, clinically manifested food allergy
is regarded as IgE mediated. However, there are some
cases (~ 10%) in which IgE can not be proved. The
present investigation was undertaken to identify the
IgG-cross-reactive sarcoplasmic peptides in the Indian
freshwater catfish Rita rita and to study the effect of
boiling/ processing on their immunoreactivity. The
epaxial (white) muscle proteins were extracted in PBS
under three different conditions, viz. 'raw' (or uncooked,
UC), 'boiled' (or cooked, C) and 'cooked with spices' as
a normal ethnic preparation (CS). The protein profiles
were analyzed by SDS PAGE and 2-D PAGE. Titer of
human IgG-crossreactive sarcoplasmic peptides was
determined by ELISA and cross-reactive proteins/
peptides were identified by immunoblot. By silver
staining the SDS-polyacrylamide gel, ~23 protein bands
were visualized in the protein extract (UC). Four
'thermostable' or 'boiling resistant' bands, viz. 55, 45, 23,
& 20 kDa, were observed of which, the 23 kDa
(pI 5.5-5.9), followed by 45kDa (pI 5.1-5.5) were the major
ones. Muscle protein-specific IgG titers in the human
sera, from a randomly selected population (n = 18), that
included both fish-eating and fish-non-eating
individuals varied from 1/1000 to 1/8000. Variable
numbers of immunoreactive proteins were observed with different sera samples on immunoblot. In 'C' and 'CS' samples also immunoreactive bands were seen. There are cross-reactive proteins among the fish
sarcoplasmic peptides that are recognized by human IgG and some of them are 'boiling resistant' and retain the immunoreactivity even after boiling and complex processing reactions that might account, partly, for the non-IgE-mediated food allergy. We could identify a 41kDa boiling-resistant sarcoplasmic peptide (pI 5.9-6.6), which appears to be a major IgG-crossreactive peptide in the freshwater catfish Rita rita.
Keywords IgG-crossreactive, peptides, Fish food, allergy, hypersensitivity, catfish
References
1. Burks AW, Helm R, Stanley S, Bannon GA, Food Allergens. Curr. Opin. Allergy Clin. Immunol., 2001, 1, 343-348
2. Ebo DG, Stevens WJ, IgE-mediated food allergy- extensive review of the literature. Acta. Clin. Belg., 2001, 56, 234-247
3. Sampson HA, Food allergy. J. Allergy Clin. Immunol., 2003, 111 (2 Suppl), S 540-547
4. Breiteneder H, Ebner C, Molecular and biochemical classification of plant-derived food allergens. J. Allergy Clin. Immunol., 2000, 106, 27-36
5. Sicherer SH. Clinical implications of cross-reactive food allergens. J. Allergy Clin. Immunol., 2001, 108, 881-890
6. Aalberse RC, Structural biology of allergens. J. Allergy Clin. Immunol., 2000, 106, 228-238
7. Poulsen LK, Hansen TK, Norgaard A, Vestergaard H, Stahl Skov
8. P, Bindslev-Jensen, C Allergens, from fish and egg. Allergy, 2001, 56 Suppl 67, 39-42
9. Bernhisel-Broadbent J, Strause D, Sampson HA, Fish hypersensitivity II: Clinical relevance of altered fish allergenicity caused by various preparation methods J Allergy Clin Immunol, 90 (1992) 622
10. Niggemann B, Reibel S, Roehr C C, Felger D, Ziegert M, Sommerfeld C, Wahn U, Predictions of positive food challenge outcome in non-IgE mediated reactions to food in children with atopic dermatitis, J Allergy Clin Immunol, 108 (2001), 1053
11. James JM, Helm RM, Burks AW, Lehrer SB, Comparison of pediatric and adult IgE antibody binding to fish proteins. Ann. Allergy Asthma Immunol., 1997, 79: 131-137
12. Lowry O H, Rosebrough NJ, Farr AL, Randoll RJ, Protein measurement with the folin phenol reagent. J. Biol. Chem., 1951, 193: 265-275
13. O' Farrell, PH, High Resulation Two- Dimensional Electrophoresis of protein. J. Biol. Chem., 1975, 250:4007-4027
14. Laemmli UK, Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 1970, 227,680
15. Engvall E, Perlmann P, Enzyme linked immunosorbent assay, ELISA. III. Quantitation of specific antibodies by Enzyme-labeled anti-Immunoglobulin in antigen coated tubes. J. Immunol.,1972, 109: 129-135
16. Towbin H, Staehelin T, Gordon J, Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some application. Proc. Natl. Acad. Sci., 1979, USA 76: 4350-4354
17. Reddy PM, LingaReddy VS, Rao ZS, Krishnamurthy G, Identification of species origin of fresh, cooked and decomposed meats using brain antigens. J. Food Sci. Technol., 2000, 37: 201-203
18. Bugajska- Schretter A, Grote M, Vangelista L, Valenta P, Spitzauer S, Purification, biochemical, and immunological characterization of major food allergen; different Immunoglobin E recognition of the apo-and calcium-bound forms of carp parvalbumin. Gut, 2000, 4,
19. -669
20. Das Dores S, Chopim C, Villaume C, Fleurence J, Gueant JLA New Oligomeric Parvalbumin allergen of Atlantic cod (Gad m I) encoded by a gene distinct from that of Gad I. Allergy, 2002a, 57 Suppl. 72, 79-83
21. Swoboda I, Bugajska-Schretter A, Valenta R, Spitzauer S, Recombinant fish parvalbumins: candidates for diagnosis and treatment of fish allergy. Allergy, 2002a, 57 Suppl. 72, 94-96
22. Swoboda I, Bugajska-Schretter A, Verdino P, Keller W, Sperr WR, Valent P, Valenta R, Spitzauer S, Recombinant carp parvalbumin, The major cross-reactive fish allergen: a tool for diagnosis and therapy of fish allergy. J. Immunol., 2002b, 168, 4576-4584
23. Van Do T, Hordvik I, Endresen C, Elsayed S, Expression and
24. analysis of recombinant salmon parvalbumin, the major
25. allergen in Atlantic salmon (Salmo salar). Scand. J. Immunol,. 1999, 50, 619-625
26. Van Do T, Hordvic I, Endresen C, Elsayed S, The major allergen
27. (Parvalbumin) of codfish is encoded by at two isotypic genes: cDNA cloning, expression and antibody binding of the recombinant allergens. Mol. Immunol., 2003, 39,595-602
28. Porcel S, León F, Cumplido J, Cuevas M, Guimaraens D, Condé-Salazar L, Contact urticaria caused by heatsensitive raw fish allergens. Contact Dermatitis, 2001, 45, 139
29. Sakaguchi M, Toda M, Ebihara T, Irie S, Hori H, Imai A, Yanagida M, Miyazawa H, Ohsuna H, Ikezawa Z, Inouye SJ, Allergy Clin. Immunol., 2000, 106: 579-584
30. Hamada Y, Nagashima Y, Shiomi K, Identification of collagen as a new fish allergen. Biosci. Biotechnol. Biochem., 2001, 65: 285-291
31. Hamada Y, Nagashima Y, Shiomi K, Shimojo N, Kohno Y, Shibata R, Nishima S, Ohsuna H, Ikezawa Z, Reactivity of IgE in fish-allergic patients to fish muscle collagen. Allergology International, 2003, 52: 139-147
32. Hayduk EJ, Choe LH, Lee KH, Curr. Sc., 2002, 83: 840-844
33. Galland AV, Dory D, Pous L, Chopin C, Rabesona H, Gueant JL, Fleurence J, Purification of a 41 kDa cod-allergenic protein. J. Chromatogr. B Biomed. Sci. Appl., 1998, 706, 63-71
34. Das Dores S, Chopin C, Romano A, GallandIrmouli AV, Quarrationo D, Pascual C, Fleurence J, Gueant JL, IgEbinding and cross-reactivity of new 41 kDa allergen of cod fish. Allergy, 2002b, 57 Suppl 77, 84-87
35. Kelso JM, Jones RT, Yunginger JW, Monospecific allergy to swordfish. Ann. Allergy Asthma Immunol., 1996, 77, 227-228
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