Characterization of a major allergen (cod)

K, Aas; Elsayed, S.

doi:10.1016/0021-8707(69)90025-2

Cited by 64 publications

(16 citation statements)

References 25 publications

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“…While the IgE binding epitopes from the major allergens of cow milk (30), codfish (31), hazel (32), soy (33), and shrimp (34) have all been elucidated there have been few, if any, characteristics found in common with these binding sites. Our work on the IgE binding epitopes of Ara h1 also indicates that there is no common amino acid sequence motif found in all epitopes (10).…”

Section: Discussionmentioning

confidence: 99%

Biochemical and Structural Analysis of the IgE Binding Sites on Ara h1, an Abundant and Highly Allergenic Peanut Protein

Shin¹,

Compadre²,

Maleki³

et al. 1998

Journal of Biological Chemistry

237

201

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Allergy to peanut is a significant IgE-mediated health problem because of the high prevalence, potential severity, and chronicity of the reaction. Ara h1, an abundant peanut protein, is recognized by serum IgE from >90% of peanut-sensitive individuals. It has been shown to belong to the vicilin family of seed storage proteins and to contain 23 linear IgE binding epitopes. In this communication, we have determined the critical amino acids within each of the IgE binding epitopes of Ara h1 that are important for immunoglobulin binding. Surprisingly, substitution of a single amino acid within each of the epitopes led to loss of IgE binding. In addition, hydrophobic residues appeared to be most critical for IgE binding. The position of each of the IgE binding epitopes on a homology-based molecular model of Ara h1 showed that they were clustered into two main regions, despite their more even distribution in the primary sequence. Finally, we have shown that Ara h1 forms a stable trimer by the use of a reproducible fluorescence assay. This information will be important in studies designed to reduce the risk of peanut-induced anaphylaxis by lowering the IgE binding capacity of the allergen.

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Section: Discussionmentioning

confidence: 99%

Biochemical and Structural Analysis of the IgE Binding Sites on Ara h1, an Abundant and Highly Allergenic Peanut Protein

Shin¹,

Compadre²,

Maleki³

et al. 1998

Journal of Biological Chemistry

237

201

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show abstract

“…Resistance to boiling and to enzymes of the gastrointestinal tract may, in fact, be a predisposing factor that these proteins can act as potent sensitizing agents for Ͼ95% of fish allergic patients (6,(21)(22)(23)(24). It was further shown that patients who mount IgE Abs against one parvalbumin will cross-react with the homologous proteins from other fish species (24), which demonstrates the importance of parvalbumins as cross-reactive fish allergens and explains why allergic individuals exhibit clinical symptoms upon contact with various fish species.…”

mentioning

confidence: 99%

Recombinant Carp Parvalbumin, the Major Cross-Reactive Fish Allergen: A Tool for Diagnosis and Therapy of Fish Allergy

Swoboda¹,

Bugajska-Schretter²,

Verdino

et al. 2002

The Journal of Immunology

218

168

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IgE-mediated reactions to fish allergens represent one of the most frequent causes of food allergy. We have constructed an expression cDNA library from carp (Cyprinus carpio) muscle in phage λgt11 and used serum IgE from a fish allergic patient to isolate 33 cDNA clones that coded for two parvalbumin isoforms (Cyp c 1.01 and Cyp c 1.02) with comparable IgE binding capacities. Both isoforms represented calcium-binding proteins that belonged to the β-lineage of parvalbumins. The Cyp c 1.01 cDNA was overexpressed in Escherichia coli, and rCyp c 1.01 was purified to homogeneity. Circular dichroism analysis and mass spectroscopy showed that rCyp c 1.01 represented a folded protein with mainly α-helical secondary structure and a molecular mass of 11,416 Da, respectively. rCyp c 1.01 reacted with IgE from all fish-allergic patients tested (n = 60), induced specific and dose-dependent basophil histamine release, and contained most of the IgE epitopes (70%) present in natural allergen extracts from cod, tuna, and salmon. Therefore, it may be used to identify patients suffering from IgE-mediated fish allergy. The therapeutic potential of rCyp c 1.01 is indicated by our findings that rabbit Abs raised against rCyp c 1.01 inhibited the binding of IgE (n = 25) in fish-allergic patients to rCyp c 1.01 between 35 and 97% (84% mean inhibition) and that depletion of calcium strongly reduced IgE recognition of rCyp c 1.01. The latter results suggest that it will be possible to develop strategies for immunotherapy for fish allergy that are based on calcium-free hypoallergenic rCyp c 1.01 derivatives.

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“…The major fish allergens, in common with many other food allergens, have been reported to be stable proteins that resist the effects of heating, although allergenicity to certain proteins in tuna and salmon [20] and in pomfret and hilsa [21] was reported to be reduced by heat processing. Resistance to digestive hydrolysis is also attributed to typical food allergens, and early studies found that Gad c 1 was relatively digestion resistant [22]. However, recent reports show that parvalbumin is rapidly degraded under simulated gastric conditions, but that the extent of hydrolysis, and thus allergenic potency, is influenced by marginal alterations in pH [23].…”

Section: Introductionmentioning

confidence: 99%

Effects of Industrial Processing on the Immunogenicity of Commonly Ingested Fish Species

Sletten¹,

Do²,

Lindvik³

et al. 2009

Int Arch Allergy Immunol

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Background: Food-processing techniques may induce changes in fish protein immunogenicity. Allergens from >100 fish species have been identified, but little is known on the effects of processing on fish protein immunogenicity. Methods: IgE binding of sera of patients allergic to fresh and processed (smoked, salted/sugar-cured, canned, lye-treated and fermented) cod, haddock, salmon, trout, tuna, mackerel and herring and of hydrolysates based on salmon and whiting was investigated using immunoblot and inhibition ELISA. Results: Parvalbumin oligomers were identified using monoclonal and polyclonal antibodies. IgE binding was seen in most sera at 12–14 kDa (parvalbumin), and at 17–60 kDa for all fish except tuna. Changes in IgE binding appeared to reflect altered parvalbumin monomers and oligomers. Smoked haddock, salmon and mackerel had increased IgE binding and novel bands at 30 kDa. Chemically processed cod, salmon, trout and pickled herring had reduced or abolished IgE binding. The serum of 1 subject, however, had increased IgE binding to these products and also inhibition of binding by both fish hydrolysates to their constituent fish species. Conclusion: Process-induced changes in fish protein immunogenicity were more dependent on process rather than species, although individual responses varied. Changes in the allergenicity of a product may depend on the net effect of processing on parvalbumin oligomerization patterns, which may also vary in different species. Chemical processes generally caused loss in IgE-binding activity, though sensitization may occur to modified or degraded rather than intact peptides as shown by increased binding by chemically processed fish and hydrolysates in 1 subject. The clinical significance of these findings remains to be established.

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Characterization of a major allergen (cod)

Cited by 64 publications

References 25 publications

Biochemical and Structural Analysis of the IgE Binding Sites on Ara h1, an Abundant and Highly Allergenic Peanut Protein

Biochemical and Structural Analysis of the IgE Binding Sites on Ara h1, an Abundant and Highly Allergenic Peanut Protein

Recombinant Carp Parvalbumin, the Major Cross-Reactive Fish Allergen: A Tool for Diagnosis and Therapy of Fish Allergy

Effects of Industrial Processing on the Immunogenicity of Commonly Ingested Fish Species

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