Advertisement

Identification of allergic proteins of Flower tail shrimp (Metapenaeus dobsonii)

  • S. J. LalyEmail author
  • T. V. Sankar
  • Satyen Kumar Panda
Original Article
  • 2 Downloads

Abstract

Allergy to seafood mainly fish and shellfish has been reported. Tropomyosin is recognized as a major allergen in many crustaceans especially shrimps. A study was carried out to identify the IgE reactive proteins of allergic nature in Flower tail shrimp (Metapenaeus dobsonii), a frequently consumed shrimp in India mainly in dried form. Protein profiling and identification of IgE reactive proteins in raw and cooked extracts of Flower tail shrimp was carried out by SDS-PAGE and immunoblotting using sera of 13 patients having allergic reactions on consumption of shrimp and positive to skin prick test. The IgE binding ability was determined by ELISA and it was found higher in the case of cooked extracts ranging from 0.244 to 0.440 at 490 nm. The SDS-PAGE of raw extract revealed many protein bands between 205 and 6.5 KDa, while in the case of cooked extracts bands of 36, 20, 29 and 70 KDa were prominent. Heat resistant protein of 37 KDa, tropomyosin was showing a clear immune reaction both in the case of raw and cooked extracts was identified as the major allergen by all the patient sera. The minor proteins of raw extract identified by immune reaction are 50, 75 and 100 KDa. The identified allergen can be used for the diagnosis and management of shrimp allergy.

Keywords

Food allergen Flower tail shrimp Immunoblotting Tropomyosin 

Notes

Acknowledgements

This research work was completed with the support of Indian Council of Agricultural Research, New Delhi, India. The authors are extremely thankful to the Director, Indian council of Agriculture Research-Central Institute of Fisheries Technology (ICAR-CIFT), Cochin for providing facilities and support to undertake this work.

References

  1. AOAC International (2000) Official methods of analysis of AOAC international, 17th edn. Association of Analytical Communities, GaithersburgGoogle Scholar
  2. Ayuso R, Reese G, Leong-Kee S, Plante M, Lehrer SB (2002) Molecular basis of arthropod cross-reactivity: IgE-binding cross-reactive epitopes of shrimp, house dust mite and cockroach tropomyosins. Int Arch Allergy Immunol 129(1):38–48CrossRefGoogle Scholar
  3. Ayuso R, Grishina G, Bardina I, Carrillo T, Blanco C, Ibanez MD, Sampson HA, Beyer K (2008) Myosin light chain is a novel shrimp allergen Lit, v 3. J Allergy Clin Immunol 122:795–802CrossRefGoogle Scholar
  4. Ayuso R, Sánchez-Garcia S, Lin J, Fu Z, Ibáñez MD, Carrillo T, Blanco C, Goldis M, Bardina L, Sastre J, Sampson HA (2010) Greater epitope recognition of shrimp allergens by children than by adults suggests that shrimp sensitization decreases with age. J Allergy Clin Immunol 125(6):1286–1293CrossRefGoogle Scholar
  5. Burney P, Summers C, Chinn S, Hooper R, Van Ree R, Lidholm J (2010) Prevalence and distribution of sensitization to foods in the European community respiratory health survey: a EuroPrevall analysis. Allergy 65(9):1182–1188Google Scholar
  6. Chakraborty RD, Nandakumar G, Maheswarudu G, Chellapan K (2014) Fishery, biology and population dynamics of Metapenaeus dobsoni (Miers 1878) from Kerala, south-west coast of India. Indian J Fish 61(4):42–47 Google Scholar
  7. Chuo KH, Wong SH, Leung PSC (2000) Tropomyosin is the major mollusk allergen: reverse transcriptase polymerase chain reaction, expression and IgE reactivity. Mar Biotechnol 2:499–509Google Scholar
  8. Daul C, Slattery M, Reese G, Lehrer S (1994) Identification of the major brown shrimp (Penaeus aztecus) allergen as the muscle protein tropomyosin. Int Arch Allergy Immunol 105(1):49–55CrossRefGoogle Scholar
  9. Emoto A, Ishizaki S, Shiomi K (2009) Tropomyosins in gastropods and bivalves: identification as major allergens and amino acid sequence features. Food Chem 114:634–641CrossRefGoogle Scholar
  10. FAO (2014) World aquaculture and fisheries statistics. FAO Publication, RomeGoogle Scholar
  11. Gill BV, Rice TR, Cartier A, Gautrin D, Neis B, Horth-Susin L, Jong M, Swanson M, Lehrer SB (2009) Identification of crab proteins that elicit IgE reactivity in snow crab-processing workers. J Allergy Clin Immunol 124:1055–1061CrossRefGoogle Scholar
  12. Gornall AG, Bardawill CJ, David MM (1949) Determination of serum proteins by means of biuret reaction. J Biol Chem 177(2):751–766 Google Scholar
  13. Hashimoto K, Watabe S, Kono M, Skiro K (1979) Muscle protein composition of sardine and mackerel. Bull Jpn Soc Sci Fish 45:1435–1441CrossRefGoogle Scholar
  14. Ishikawa M, Shimakura K, Nagashima Y, Shiomi K (1997) Isolation and properties of allergenic proteins in the oyster Crassostrea gigas. Fish Sci 63:610–614CrossRefGoogle Scholar
  15. Karakoltsidis PA, Zotos A, Constantinides SM (1995) Composition of the commercially important Mediterranean finfish, crustaceans, and mollusks. J Food Compos Anal 8:258–273CrossRefGoogle Scholar
  16. Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head ofbacteriophageT4. Nature 227:680–685CrossRefGoogle Scholar
  17. Lehrer SB, Ayuso R, Reese G (2003) Seafood allergy and allergens: a review. Mar Biotechnol (NY) 5:339–348CrossRefGoogle Scholar
  18. Leung PSC, Chow WK, Duffey S, Kwan HS, Gershwin ME, Chu KH (1996) IgE reactivity against a cross-reactive allergen in crustacea and mollusca: evidence for tropomyosin as the common allergen. J Allergy Clin Immunol 98:954–961CrossRefGoogle Scholar
  19. Liang Y, Cao M, Su W, Zhang L, Huang Y, Liu G (2008) Identification and characterisation of the major allergen of Chinese mitten crab (Eriocheir sinensis). Food Chem 111(4):998–1003CrossRefGoogle Scholar
  20. Lopata A, O'hehir R, Lehrer S (2010) Shellfish allergy. Clin Exp Allergy 40(6):850–858CrossRefGoogle Scholar
  21. Motoyama K, Ishizaki S, Nagashima Y, Shiomi K (2006) Cephalopod tropomyosins: identification as major allergens and molecular cloning. Food Chem Toxicol 44:1997–2002CrossRefGoogle Scholar
  22. Motoyama K, Suma Y, Ishizaki S, Nagashima Y, Shiomi K (2007) Molecular cloning of tropomyosins identified as allergens in six species of crustaceans. J Agric Food Chem 55:985–991CrossRefGoogle Scholar
  23. Motoyama K, Suma Y, Ishizaki S, Nagashima Y, Lu Y, Ushio H, Shiomi K (2008) Identification of tropomyosins as major allergens in Antarctic Krill and Mantis Shrimp and their amino acid sequence characteristics. Mar Biotechnol 10:709–718CrossRefGoogle Scholar
  24. Nakano S, Yoshinuma T, Yamada T (2008) Reactivity of shrimp allergy-related IgE antibodies to krill tropomyosin. Int Arch Allergy Immunol 145:175–181CrossRefGoogle Scholar
  25. Peng J, Gygi SP (2001) Proteomics: the move to mixtures. Int J Mass Spectrom 36:1083–1091CrossRefGoogle Scholar
  26. Reese G, Ayuso R, Lehrer SB (1999) Tropomyosin an invertebrate panallergen. Int Arch Allergy Immunol 119(4):247–258CrossRefGoogle Scholar
  27. Samson KT, Chen FH, Miura K, Odajima Y, Iikura Y, Naval Rivas M et al (2004a) IgE binding to raw and boiled shrimp proteins in atopic and nonatopic patients with adverse reaction to shrimp. Int Arch Allergy Immunol 133(3):225–232CrossRefGoogle Scholar
  28. Samson KTR, Chen FH, Miura K, Odajima Y, Iikura Y, Rivas MN, Minoguchi K, Adachi M (2004b) IgE binding to raw and boiled shrimp proteins in atopic and nonatopic patients with adverse reactions to shrimp. Int Arch Allergy Immunol 133:225–232CrossRefGoogle Scholar
  29. Sathe SK, Teuber SS, Roux KH (2005) Effects of food processing on the stability of food allergens. Biotechnol Adv 23(6):423–429CrossRefGoogle Scholar
  30. Shamsundar BA, Prakash V (1994) Physicochemical and functional properties of proteins from prawns (Metapenaeus dobsoni). J Agric Food Chem 42:169–174CrossRefGoogle Scholar
  31. Shanti KN, Martin BM, Nagpal S, Metcalfe DD, Rao PV (1993) Identification of tropomyosin as the major shrimp allergen and characterization of its IgE-binding epitopes. J Immunol 151(10):5354–5363Google Scholar
  32. Shimakura K, Tonomura Y, Hamada Y, Nagashima Y, Shiomi K (2005) Allergenicity of crustacean extractives and its reduction by protease digestion. Food Chem 91(2):247–253CrossRefGoogle Scholar
  33. Shioni K, Sato Y, Hamamoto S, Mita H, Shimakura K (2008) Sarcoplamic calcium-binding protein: identification of a new allergen of the black tiger shrimp Penaeus monodon. Int Arch Allergy Immunol 146:91–98CrossRefGoogle Scholar
  34. Sicherer SH (2011) Epidemiology of food allergy. J Allergy Clin Immunol 127(3):594–602CrossRefGoogle Scholar
  35. Sicherer SH, Sampson HA (2010) Food allergy. J Allergy Clin Immunol 125(2):S116–S125CrossRefGoogle Scholar
  36. Sriket Pisal, Benjakul Soottawat, Visessaguan Wonnop, Kijroongrojana Kongkarn (2007) Comparative studies on chemical composition and thermal properties of black tiger shrimp (Penaeus monodon) and white shrimp (Litopenaeus vannamei) meats. Food chem 103:1199–1207CrossRefGoogle Scholar
  37. Yadzir ZHM, Misnan R, Abdullah N, Bakhtiar F, Arip M, Murad S (2012) Identification of the major allergen of Macrobrachium rosenbergii (giant freshwater prawn). Asian Pac J Trop Biomed 2(1):50–54CrossRefGoogle Scholar
  38. Yanar Y, Celik M (2006) Seasonal amoni acid profiles and mineral contents of green tiger shrimp (Penaeus semisulcatus De Haan, 844) and speckled shrimp (Metapenaeus monoceros Fabricus, 1789) from the Eastern Mediterranean. Food Chem 94:33–36CrossRefGoogle Scholar
  39. Yu CJ, Lin YF, Chiang BL, Chow LP (2003) Proteomics and immunological analysis of a novel shrimp allergen, Pen m 2. J Immunol 170:445–453CrossRefGoogle Scholar

Copyright information

© Association of Food Scientists & Technologists (India) 2019

Authors and Affiliations

  1. 1.ICAR - Mumbai Research Center of Central Institute of Fisheries TechnologyVashi, Navi MumbaiIndia
  2. 2.Kerala University of Fisheries and Ocean StudiesCochinIndia
  3. 3.ICAR-Central Institute of Fisheries TechnologyCochinIndia

Personalised recommendations