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

Mol Immunol. 2011 Sep;48(15-16):1983-92. doi: 10.1016/j.molimm.2011.06.216. Epub 2011 Jul 23.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adolescent
  • Adult
  • Aged
  • Allergens / chemistry
  • Allergens / immunology*
  • Allergens / isolation & purification*
  • Amino Acid Sequence
  • Animals
  • Blotting, Western
  • Child
  • Crangonidae / chemistry
  • Crangonidae / immunology*
  • Electrophoresis, Polyacrylamide Gel
  • Female
  • Food Hypersensitivity / diagnosis*
  • Food Hypersensitivity / immunology*
  • Humans
  • Immunoglobulin E / blood
  • Male
  • Mass Spectrometry
  • Middle Aged
  • Recombinant Proteins / immunology
  • Sensitivity and Specificity
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
  • Young Adult


  • Allergens
  • Recombinant Proteins
  • Immunoglobulin E