Original Article

Impacts of Thermal Treatments on Major and Minor Allergens of Sea Snail, Cerithidea obtusa (Obtuse Horn Shell)


Snail is one of the worst causes of food allergy. Thus, the aim of this study was to identify the major and minor allergens of the local marine snail (Cerithidea obtusa) and subsequently to investigate the impacts of heat treatment on the IgE-binding activity of snail allergens. Proteins from raw and heat-treated snails (boiled, roasted and fried) were extracted and then resolved by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). Immunoblotting of all extracts were then performed using sera from patients with snail allergy. The results showed that the raw extract contains numerous protein bands between 12 to>250 kDa. Some thermostable proteins, predominantly the 33 and 42 kDa bands, remained detected in all cooked extracts with decreasing intensities from boiled to roasted to fried extracts, while the majority of thermolabile bands denatured after heating. Boiled snail had more protein bands compared to roasted and fried snails. Immunoblotting of raw extract demostrated 19 IgE-binding bands ranging from 15 to 240 kDa. The thermostable bands of 33 and 42 kDa and a thermolabile of 30 kDa band were identified as the major allergens of this snail. The cooked extracts yielded less allergenic bands. The boiled extract yielded approximately 14 IgE-binding bands with some smeared bands at high molecular weight regions. The roasted extract had lesser IgE-binding bands and the majority appeared as smears, while the IgE-reactivity in the fried extract was less visible and appeared as weak smears. This study indicated that both raw and cooked snails played a crucial role in snail allergenicity, as this species of snail contains both thermostable and thermolabile major allergens. The degree of snail allergenicity was revealed in the order: raw> boiled > roasted> fried. Thus, the results would facilitate in the development of effective diagnosis and management strategies of snail allergy in this country

  1. Purwaningsih S. Aktivitas antioksidan dan komposisi kimia keong matah merah (Cerithidea obtusa). Indonesian J Marine Sci. 2012; 7(1):39-48.
  2. Taylor SL. Molluscan shellfish allergy. Adv Food Nutr Res. 2008; 54:140-77.
  3. Martins L, Pires E, Ináicio F. CD4 T-Cell Cytokine response to mite recombinant tropomyosin in mite, snail and shrimp allergic patients. Internet J Asthma Allergy Immunol. 2009; 7(1):1-22.
  4. Bessot JC, Metz-Favre C, Rame JM, De Blay F, Pauli G. Tropomyosin or not tropomyosin, what is the relevant allergen in house dust mite and snail cross allergies?. Eur Ann Allergy Clin Immunol. 2010; 42(1):3-10.
  5. Lopata AL, Lehrer SB. New insights into seafood allergy. Curr Opin Allergy Clin Immunol. 2009; 9:270-7.
  6. Kamath SD, Abdel Rahman AM, Komoda T, Lopata AL. Impact of heat processing on the detection of the major shellfish allergen in crustaceans and mollusks using specific monoclonal antibodies. Food Chem. 2013; 141(4):4031-9.
  7. Ishikawa M, Ishida M, Shimakura K, Nagashima Y, Shiomi K. Purification and IgE-binding epitopes of a major allergen in the gastropod Turbo cornutus. Biosci Biotechnol Biochem. 1998; 62(7):1337-43.
  8. Asturias JA, Eraso E, Arilla MC, Gomez-Bayon N, Inacio F, Martinez A. Cloning, isolation and IgE-binding properties of Helix aspersa (brown garden snail) tropomyosin. Int Arch Allergy Immunol. 2002; 128:90-96.
  9. Zailatul HMY, Rosmilah M, Faizal B, Noormalin A, Shahnaz M. Malaysian cockle (Anadara granosa) allergy: Identification of IgE-binding proteins and effects of different cooking methods. Trop Biomed. 2015; 32(2):323-34.
  10. Winder SJ, Ayscough KR. Actin-binding proteins. J Cell Sci. 2005; 118(Pt 4):651-4.
  11. Reisler E, Egelman EH. Actin structure and function: what we still do not understand. J Biol Chem. 2007; 282(50):36133–7.
  12. Povarova OI, Sulatskaya AI, Kuznetsova IM, Turoverov KK. Actin folding, structure and function: Is it a globular or an intrinsically disordered protein? In Current Frontiers and Perspectives in Cell Biology. (pp.57-80). 2012; Croatia: Intech.
  13. Chhabra D, dos Remedios CG. Actin: An Overview of Its Structure and Function. In. Remedios, CG, Chhabra D. Protein reviews: Actin-binding proteins and disease. (pp.1-15). 2008; New York: Springerlink.
  14. Abramovitch JB, Kamath S, Varese N, Zubrinich C, Lopata AL, O'Hehir RE, Rolland JM. IgE reactivity of blue swimmer crab Portunus pelagicus tropomyosin, Por p 1, and other allergens; cross-reactivity with black tiger prawn and effects of heating. PLoS One. 2013; 8(6):e67487.
  15. Paschke A, Besler M. Stability of bovine allergens during food processing. Ann Allergy Asthma Immunol. 2002; 89(6 Suppl 1):16-20.
  16. Samson KT, Chen FH, Miura K, Odajima Y, Iikura Y, Naval Rivas M, Minoguchi K, Adachi M. IgE binding to raw and boiled shrimp proteins in atopic and nonatopic patients with adverse reactions to shrimp. Int Arch Allergy Immunol. 2004; 133(3):225-32.
  17. Rosmilah M, Shahnaz M, Zailatul Hani MY, Noormalin A. Identification of tropomyosin and arginine kinase as major allergens of Portunus pelagicus (blue swimming crab). Trop Biomed. 2012; 29(3):467-78.
  18. Rosmilah M, Shahnaz M, Zailatul Hani MY, Noormalin A. Identification of the major allergens of Charybdis feriatus (red crab) and its cross-reactivity with Portunus pelagicus (blue crab). Asian Pac J Allergy Immunol. 2012; 30(4):285-93.
  19. Davis PJ, Williams SC. Protein modification by thermal processing. Allergy. 1998; 53(46 Suppl):102-5.
  20. Beyer K, Morrow E, Li XM, Bardina L, Bannon GA, Burks AW, Sampson HA. Effects of cooking methods on peanut allerginicity. J Allergy Clin Immunol. 2001; 107(6):1077-81.
  21. Yadzir ZH, Misnan R, Abdullah N, Bakhtiar F, Arip M, Murad S. Identification of IgE-binding proteins of raw and cooked extracts of Loligo edulis (white squid). Southest Asian J Trop Med Public Health 2010; 41(3): 653-9.
  22. Velickovic TC, Jankulovic MG, Jankov RM. Overview of the most commonly used methods in allergen characterization. J Serb Chem Soc. 2005; 70(3):347-360.
  23. Lopata AL, O’Hehir RE, Lehrer SB. Shellfish Allergy. Clin Exp Allergy. 2010; 40(6):850-8.
  24. Kamath SD, Rahman AM, Voskamp A, Komoda T, Rolland JM, O’Hehir RE, Lopata AL. Effect of heat processing on antibody reactivity to allergen variants and fragments of black tiger prawn: a comprehensive allergenomic approach. Mol Nutr Food Res. 2014; 58(5):1144-55.
  25. Matsuo H, Yokooji T, Taogoshi T. Common food allergens and their IgE-binding epitopes. Allergol Int. 2015; 64(4):332-43.
  26. Koppelman SJ, Bruijnzeel-Koomen CA, Hessling M, de Jongh HH. Heat-induced conformational changes of Ara h 1, a major peanut allergen, do not affect its allergenic properties. J Biol Chem. 1999; 274(8):4770-7.
  27. Gruber P, Becker WM, Hofmann T. Influence of the maillard reaction on the allergenicity of rAra h 2, a recombinant major allergen from peanut (Arachis hypogaea), its major epitopes and peanut agglutinin. J Agric Food Chem. 2005; 53(6):2289-96.
  28. Nakamura A, Watanabe K, Ojima T, Ahn DH, Saeki H. Effect of maillard reaction on allergenicity of scallop tropomyosin. J Agric Food Chem 2005; 53(19):7559-64.
  29. Nakamura A, Sasaki F, Watanabe K, Ojima T, Ahn DH, Saeki H. Changes in allergenicity and digestibility of squid tropomyosin during the maillard reaction with ribose. J Agric Food Chem. 2006; 54(25):9529-3.

IssueVol 15, No 4 (2016) QRcode
SectionOriginal Article(s)
Allergen Cerithidea obtusa Immunoblotting SDS-PAGE Snail Thermolabile Thermostable

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How to Cite
Misnan R, Salahudin Abd Aziz N, Mohamad Yadzir ZH, Bakhtiar F, Abdullah N, Murad S. Impacts of Thermal Treatments on Major and Minor Allergens of Sea Snail, Cerithidea obtusa (Obtuse Horn Shell). Iran J Allergy Asthma Immunol. 15(4):309-316.