Skip to main content
SpringerLink
Log in

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

  • Original Article
  • Published:
Journal of Food Science and Technology Aims and scope Submit manuscript

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.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Fig. 1
Fig. 2
Fig. 3

Similar content being viewed by others

References

  • AOAC International (2000) Official methods of analysis of AOAC international, 17th edn. Association of Analytical Communities, Gaithersburg

    Google Scholar 

  • 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):38–48

    Article  CAS  Google Scholar 

  • 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 122:795–802

    Article  CAS  Google Scholar 

  • 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):1286–1293

    Article  CAS  Google Scholar 

  • 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):1182–1188

    CAS  PubMed  Google Scholar 

  • 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 

  • Chuo KH, Wong SH, Leung PSC (2000) Tropomyosin is the major mollusk allergen: reverse transcriptase polymerase chain reaction, expression and IgE reactivity. Mar Biotechnol 2:499–509

    Google Scholar 

  • 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):49–55

    Article  CAS  Google Scholar 

  • Emoto A, Ishizaki S, Shiomi K (2009) Tropomyosins in gastropods and bivalves: identification as major allergens and amino acid sequence features. Food Chem 114:634–641

    Article  CAS  Google Scholar 

  • FAO (2014) World aquaculture and fisheries statistics. FAO Publication, Rome

    Google Scholar 

  • 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 124:1055–1061

    Article  CAS  Google Scholar 

  • Gornall AG, Bardawill CJ, David MM (1949) Determination of serum proteins by means of biuret reaction. J Biol Chem 177(2):751–766

    CAS  PubMed  Google Scholar 

  • Hashimoto K, Watabe S, Kono M, Skiro K (1979) Muscle protein composition of sardine and mackerel. Bull Jpn Soc Sci Fish 45:1435–1441

    Article  CAS  Google Scholar 

  • Ishikawa M, Shimakura K, Nagashima Y, Shiomi K (1997) Isolation and properties of allergenic proteins in the oyster Crassostrea gigas. Fish Sci 63:610–614

    Article  CAS  Google Scholar 

  • Karakoltsidis PA, Zotos A, Constantinides SM (1995) Composition of the commercially important Mediterranean finfish, crustaceans, and mollusks. J Food Compos Anal 8:258–273

    Article  Google Scholar 

  • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head ofbacteriophageT4. Nature 227:680–685

    Article  CAS  Google Scholar 

  • Lehrer SB, Ayuso R, Reese G (2003) Seafood allergy and allergens: a review. Mar Biotechnol (NY) 5:339–348

    Article  CAS  Google Scholar 

  • 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 98:954–961

    Article  CAS  Google Scholar 

  • 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):998–1003

    Article  CAS  Google Scholar 

  • Lopata A, O'hehir R, Lehrer S (2010) Shellfish allergy. Clin Exp Allergy 40(6):850–858

    Article  CAS  Google Scholar 

  • Motoyama K, Ishizaki S, Nagashima Y, Shiomi K (2006) Cephalopod tropomyosins: identification as major allergens and molecular cloning. Food Chem Toxicol 44:1997–2002

    Article  CAS  Google Scholar 

  • 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 55:985–991

    Article  CAS  Google Scholar 

  • 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 10:709–718

    Article  CAS  Google Scholar 

  • Nakano S, Yoshinuma T, Yamada T (2008) Reactivity of shrimp allergy-related IgE antibodies to krill tropomyosin. Int Arch Allergy Immunol 145:175–181

    Article  CAS  Google Scholar 

  • Peng J, Gygi SP (2001) Proteomics: the move to mixtures. Int J Mass Spectrom 36:1083–1091

    Article  CAS  Google Scholar 

  • Reese G, Ayuso R, Lehrer SB (1999) Tropomyosin an invertebrate panallergen. Int Arch Allergy Immunol 119(4):247–258

    Article  CAS  Google Scholar 

  • 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):225–232

    Article  CAS  Google Scholar 

  • 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 133:225–232

    Article  CAS  Google Scholar 

  • Sathe SK, Teuber SS, Roux KH (2005) Effects of food processing on the stability of food allergens. Biotechnol Adv 23(6):423–429

    Article  CAS  Google Scholar 

  • Shamsundar BA, Prakash V (1994) Physicochemical and functional properties of proteins from prawns (Metapenaeus dobsoni). J Agric Food Chem 42:169–174

    Article  Google Scholar 

  • 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):5354–5363

    CAS  PubMed  Google Scholar 

  • 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):247–253

    Article  CAS  Google Scholar 

  • 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 146:91–98

    Article  Google Scholar 

  • Sicherer SH (2011) Epidemiology of food allergy. J Allergy Clin Immunol 127(3):594–602

    Article  Google Scholar 

  • Sicherer SH, Sampson HA (2010) Food allergy. J Allergy Clin Immunol 125(2):S116–S125

    Article  Google Scholar 

  • 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 103:1199–1207

    Article  CAS  Google Scholar 

  • 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):50–54

    Article  CAS  Google Scholar 

  • 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 94:33–36

    Article  CAS  Google Scholar 

  • Yu CJ, Lin YF, Chiang BL, Chow LP (2003) Proteomics and immunological analysis of a novel shrimp allergen, Pen m 2. J Immunol 170:445–453

    Article  CAS  Google Scholar 

Download references

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.

Author information

Authors and Affiliations

  1. ICAR - Mumbai Research Center of Central Institute of Fisheries Technology, Vashi, Navi Mumbai, India

    S. J. Laly

  2. Kerala University of Fisheries and Ocean Studies, Cochin, India

    T. V. Sankar

  3. ICAR-Central Institute of Fisheries Technology, P.O. Matsyapuri, Cochin, 682 029, India

    Satyen Kumar Panda

Authors
  1. S. J. Laly
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. T. V. Sankar
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Satyen Kumar Panda
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to S. J. Laly.

Additional information

Publisher's Note

Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.

Rights and permissions

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

Laly, S.J., Sankar, T.V. & Panda, S.K. Identification of allergic proteins of Flower tail shrimp (Metapenaeus dobsonii). J Food Sci Technol 56, 5415–5421 (2019). https://doi.org/10.1007/s13197-019-04012-0

Download citation

  • Revised:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s13197-019-04012-0

Keywords

Search

Navigation