TY - JOUR
T1 - Generation of a comprehensive panel of crustacean allergens from the North Sea Shrimp Crangon crangon
AU - Bauermeister, Kerstin
AU - Wangorsch, Andrea
AU - Garoffo, Lorenza Perono
AU - Reuter, Andreas
AU - Conti, Amedeo
AU - Taylor, Steve L.
AU - Lidholm, Jonas
AU - DeWitt, Åsa Marknell
AU - Enrique, Ernesto
AU - Vieths, Stefan
AU - Holzhauser, Thomas
AU - Ballmer-Weber, Barbara
AU - Reese, Gerald
N1 - Funding Information:
Kerstin Bauermeister, Lorenza Perono Garoffo, and Andrea Wangorsch have received grant support from the European Commission, EuroPrevall “The Prevalence, Cost and Basis of Food Allergy across Europe”, contract no. 514000.
Funding Information:
Barbara Ballmer-Weber has received grant support from the Food Allergy Research and Resource Program (FARRP), University of Nebraska, Lincoln, NE, USA. The clinical part of the study was financially supported by “Stiftung für wissenschaftliche Forschung an der Universität Zürich” (contribution to Barbara Ballmer-Weber).
Funding Information:
Funded by the European Commission, EuroPrevall “The Prevalence, Cost and Basis of Food Allergy across Europe”, contract no. 514000, and the Food Allergy Research and Resource Program (FARRP), University of Nebraska, Lincoln, NE, USA. The authors additionally thank Sabine Falk for technical assistance in the identification of C. crangon protein fractions, Yvonne Kuehne for performing the FPLC purification of Cra c 6, Renate Höppner for performing the ImmunoCAP measurements, and Marco Krefter, Dlab Diagnose GmbH, for kindly providing sera of shrimp-allergic individuals.
PY - 2011/9
Y1 - 2011/9
N2 - 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.
AB - 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.
KW - Arginine kinase
KW - Crangon crangon
KW - Crustacean allergy
KW - EuroPrevall
KW - Myosin light chain
KW - Sarcoplasmic Ca-binding protein
KW - Triosephosphate isomerase
KW - Tropomyosin
KW - Troponin C
UR - http://www.scopus.com/inward/record.url?scp=80051938257&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=80051938257&partnerID=8YFLogxK
U2 - 10.1016/j.molimm.2011.06.216
DO - 10.1016/j.molimm.2011.06.216
M3 - Article
C2 - 21784530
AN - SCOPUS:80051938257
SN - 0161-5890
VL - 48
SP - 1983
EP - 1992
JO - Immunochemistry
JF - Immunochemistry
IS - 15-16
ER -