Generation of a comprehensive panel of crustacean allergens from the North Sea Shrimp Crangon crangon

Kerstin Bauermeister, Andrea Wangorsch, Lorenza Perono Garoffo, Andreas Reuter, Amedeo Conti, Steve L. Taylor, Jonas Lidholm, Åsa Marknell DeWitt, Ernesto Enrique, Stefan Vieths, Thomas Holzhauser, Barbara Ballmer-Weber, Gerald Reese

Research output: Contribution to journalArticlepeer-review

83 Scopus citations

Abstract

Background: Published data on crustacean allergens are incomplete. The identification of tropomyosin (TM), arginine kinase (AK), sarcoplasmic Ca-binding protein (SCP) and myosin light chain (MLC) as shrimp allergens are all important contributions but additional allergens are required for the development of a complete set of reagents for component resolved diagnosis and the exploration of novel vaccination strategies. Methods: The North Sea shrimp (Crangon crangon), which is frequently consumed in Europe, served as a model organism in this study. TM and AK were directly cloned from mRNA based on sequence homology and produced as recombinant proteins. Additional IgE-reactive proteins were isolated by preparative SDS-PAGE and identified by mass spectrometry and corresponding cDNAs were cloned and expressed in E. coli. The relevance of the 6 cloned crustacean allergens was confirmed with sera of 31 shrimp-allergic subjects, 12 of which had a positive double-blind, placebo-controlled food challenge (DBPCFC) to shrimp and 19 a convincing history of food allergy to shrimp, including 5 cases of anaphylaxis. Quantitative IgE measurements were performed by ImmunoCAP. Results: Six recombinant crustacean proteins: TM, AK, SCP, a novel MLC, troponin C (TnC), and triosephosphate isomerase (TIM) bound IgE in ImmunoCAP analysis. Specific IgE to at least one of these single shrimp allergens was detected in 90% of the study population, thus the in vitro diagnostic sensitivity was comparable to that of shrimp extract (97%). In 75% of the subjects, the combined technical sensitivity was similar to or greater with single shrimp allergens than with natural shrimp extract. Conclusions: We identified six IgE-binding proteins from C. crangon, three of which have not before been described as allergens in crustaceans. This extensive panel of shrimp allergens forms a valuable asset for future efforts towards the identification of clinically relevant biomarkers and as a basis to approach patient-tailored immunotherapeutic strategies.

Original languageEnglish (US)
Pages (from-to)1983-1992
Number of pages10
JournalMolecular Immunology
Volume48
Issue number15-16
DOIs
StatePublished - Sep 2011

Keywords

  • Arginine kinase
  • Crangon crangon
  • Crustacean allergy
  • EuroPrevall
  • Myosin light chain
  • Sarcoplasmic Ca-binding protein
  • Triosephosphate isomerase
  • Tropomyosin
  • Troponin C

ASJC Scopus subject areas

  • Immunology
  • Molecular Biology

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