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Spartan Med Res J
Spartan Med Res J
1364
Spartan Medical Research Journal
2474-7629
MSU College of Osteopathic Medicine Statewide Campus System Website: Spartan Medical Research Journal

123077
10.51894/001c.123077
Research Symposium
CHARACTERIZATION OF FISH AND REPTILIAN PARVALBUMINS AS RELEVANT FOOD ALLERGENS
O’Malley Andrea PhD 1
1 College of Osteopathic Medicine Michigan State University https://ror.org/05hs6h993
30 8 2024
2024
9 2 ABSTRACTS FROM THE SECOND ANNUAL RESEARCH DAY HOSTED BY THE MICHIGAN STATE UNIVERSITY COLLEGE OF OSTEOPATHIC MEDICINE, NOVI, MICHIGAN, APRIL 11, 2024. 12307715 7 2024
30 7 2024
https://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
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pmc74

INTRODUCTION

Fish allergy affects up to 3% of the population, with the majority of fish-allergic individuals having IgE recognizing β-parvalbumins. It was shown that fish allergic individuals are at risk of allergic reaction when consuming meat from crocodiles. Additionally, several parvalbumins such as the β-parvalbumin from cod have been noted to oligomerize, which may have an impact on its allergenicity.

OBJECTIVES

Comparative studies of fish and reptilian parvalbumins will help to understand the molecular basis of the cross-reactivity and can improve generation of avoidance guidelines for parvalbumin-allergic patients. Biochemical, structural, and immunological studies will be performed in pursuit of this goal.

METHODS

Gad m 1.0201 (Atlantic cod), Cro p 1.0101 and Cro p 2.0101 (saltwater crocodile), human α-parvalbumin, and α-parvalbumins from Raja clavata and Callorhinchus millii were recombinantly produced in E. coli. The produced proteins were used for structural, stability and antibody binding studies. Differential scanning fluorimetry was used for assessment of thermal stability, X-ray crystallography and NMR were used for structural characterization, and ELISA and immunoblotting were used for antibody binding.

RESULTS

The studied parvalbumins displayed remarkable thermal stability, which is important from the perspective of food processing, and it was shown that calcium cations are necessary for protein stability. Five novel structures were determined via x-ray crystallography. They not only provided a detailed picture of the parvalbumins’ structures, but they also revealed the existence of a domain-swapped Gad m 1 dimer. Cross-reactivity between fish and reptilian parvalbumins was demonstrated.

CONCLUSIONS

Further analysis of the structural and biochemical properties of α- and β-parvalbumin will allow for better understanding of the allergic response to seafood parvalbumin as well as the protein’s capacity for oligomerization.
