Sequence microheterogeneity of parvalbumin, the major fish allergen

Lapteva, Yulia S.; Uversky, Vladimir N.; Permyakov, Sergei E.

doi:10.1016/j.bbapap.2013.04.025

Cited by 9 publications

(9 citation statements)

References 56 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Commercially available polyclonal and monoclonal parvalbumin-specific antibodies are considered as useful tools for detecting parvalbumins in fish extracts and fish-containing products [ 30 , 31 ]. Polyclonal antibodies directed against parvalbumins from cod or barramundi appeared to be suitable for the detection of parvalbumins [ 16 , 17 , 32 , 33 ]…”

Section: Discussionmentioning

confidence: 99%

“…Many studies showed that this cross-reactivity was based on a predominant sensitization to epitopes on parvalbumins located on the highly conserved EF-hand motifs [ 9 , 13 – 15 ]. However, although sequence identities between parvalbumins from the same and different fish species show a high extent of variation, [ 16 , 17 ] recognition patterns of parvalbumin-specific IgE were not associated with the levels of their amino acid identities [ 15 ].…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

A Cross-Reactive Human Single-Chain Antibody for Detection of Major Fish Allergens, Parvalbumins, and Identification of a Major IgE-Binding Epitope

et al. 2015

View full text Add to dashboard Cite

Fish allergy is associated with moderate to severe IgE-mediated reactions to the calcium binding parvalbumins present in fish muscle. Allergy to multiple fish species is caused by parvalbumin-specific cross-reactive IgE recognizing conserved epitopes. In this study, we aimed to produce cross-reactive single chain variable fragment (scFv) antibodies for the detection of parvalbumins in fish extracts and the identification of IgE epitopes. Parvalbumin-specific phage clones were isolated from the human ETH-2 phage display library by three rounds of biopanning either against cod parvalbumin or by sequential biopanning against cod (Gad m 1), carp (Cyp c 1) and rainbow trout (Onc m 1) parvalbumins. While biopanning against Gad m 1 resulted in the selection of clones specific exclusively for Gad m 1, the second approach resulted in the selection of clones cross-reacting with all three parvalbumins. Two clones, scFv-gco9 recognizing all three parvalbumins, and scFv-goo8 recognizing only Gad m 1 were expressed in the E. coli non-suppressor strain HB2151 and purified from the periplasm. scFv-gco9 showed highly selective binding to parvalbumins in processed fish products such as breaded cod sticks, fried carp and smoked trout in Western blots. In addition, the scFv-gco9-AP produced as alkaline phosphatase fusion protein, allowed a single-step detection of the parvalbumins. In competitive ELISA, scFv-gco9 was able to inhibit binding of IgE from fish allergic patients’ sera to all three β-parvalbumins by up to 80%, whereas inhibition by scFv-goo8 was up to 20%. 1H/15N HSQC NMR analysis of the rGad m 1:scFv-gco9 complex showed participation of amino acid residues conserved among these three parvalbumins explaining their cross-reactivity on a molecular level. In this study, we have demonstrated an approach for the selection of cross-reactive parvalbumin-specific antibodies that can be used for allergen detection and for mapping of conserved epitopes.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

A Cross-Reactive Human Single-Chain Antibody for Detection of Major Fish Allergens, Parvalbumins, and Identification of a Major IgE-Binding Epitope

et al. 2015

View full text Add to dashboard Cite

show abstract

“…These isoforms seem to play a physiological role in the fish muscle adaptation to developmental and environmental changes. In the same fish, parvalbumins differing by sequence microheterogeneity (sequence identity >90%) have been reported (99). It is conceivable that these highly identical isoforms might be of variable allergenicity.…”

Section: Allergenicity Of Parvalbuminsmentioning

confidence: 97%

“…Recent classification by structural, biochemical, and phylogenetic analysis assigned alpha-parvalbumins into a common cluster together with higher vertebrate, including human proteins while beta-subtypes form a separate, only remotely related cluster of parvalbumins which might explain the variable allergenicity of both lineages (99, 100). …”

Section: Allergenicity Of Parvalbuminsmentioning

confidence: 99%

Fish Allergens at a Glance: Variable Allergenicity of Parvalbumins, the Major Fish Allergens

Swoboda²,

et al. 2014

View full text Add to dashboard Cite

Fish is a common trigger of severe, food-allergic reactions. Only a limited number of proteins induce specific IgE-mediated immune reactions. The major fish allergens are the parvalbumins. They are members of the calcium-binding EF-hand protein family characterized by a conserved protein structure. They represent highly cross-reactive allergens for patients with specific IgE to conserved epitopes. These patients might experience clinical reactions with various fish species. On the other hand, some individuals have IgE antibodies directed against unique, species-specific parvalbumin epitopes, and these patients show clinical symptoms only with certain fish species. Furthermore, different parvalbumin isoforms and isoallergens are present in the same fish and might display variable allergenicity. This was shown for salmon homologs, where only a single parvalbumin (beta-1) isoform was identified as allergen in specific patients. In addition to the parvalbumins, several other fish proteins, enolases, aldolases, and fish gelatin, seem to be important allergens. New clinical and molecular insights advanced the knowledge and understanding of fish allergy in the last years. These findings were useful for the advancement of the IgE-based diagnosis and also for the management of fish allergies consisting of advice and treatment of fish-allergic patients.

show abstract

“…Isoallergens per definition show at least 67 % sequence identity, whereas isoforms with pairwise sequence identity above 90 % are referred to as 'microheterogeneous isoforms' (Chapman et al, 2007). Since even microheterogeneous isoforms of some allergens may induce very different responses by human T and B cells (Wagner et al, 2008) and microheterogeneous isoforms are common in parvalbumin (Lapteva et al, 2013), allergic immune responses may be elicited by a wide repertoire of molecular forms of the same allergen (Lapteva et al, 2013). Certain species of fish (e.g.…”

Section: Fish Muscle and Skinmentioning

confidence: 99%

Scientific Opinion on the evaluation of allergenic foods and food ingredients for labelling purposes

Products¹

2014

EFS2

117

View full text Add to dashboard Cite

Following a request from the Food Safety Authority of Ireland, the EFSA Panel on Dietetic Products, Nutrition and Allergies (NDA Panel) was asked to deliver a scientific opinion on the evaluation of allergenic foods and food ingredients for labelling purposes. In view of the request, the NDA Panel decided to update its previous opinions relative to food ingredients or substances with known allergenic potential listed in Annex IIIa of 2003/89/EC, as amended. These include cereals containing gluten, milk and dairy products, eggs, nuts, peanuts, soy, fish, crustaceans, molluscs, celery, lupin, sesame, mustard and sulphites. The opinion relates to immunoglobulin (Ig)E-and non-IgE-mediated food allergy, to coeliac disease and to adverse reactions to sulphites in food, and it does not address non-immune-mediated adverse reactions to food. It includes information on the prevalence of food allergy in unselected populations, proteins identified as food allergens, cross-reactivities, the effects of food processing on the allergenicity of foods and ingredients, methods for the detection of allergens and allergenic foods, doses observed to trigger adverse reactions in sensitive individuals and risk assessment methodologies that have been used to derive individual and population thresholds for selected allergenic foods. The present opinion relates to immunoglobulin (Ig)E-and non-IgE-mediated food allergy, to coeliac disease and to adverse reactions to sulphites in food, and it does not address non-immune-mediated adverse reactions to food. For each food ingredient or substance listed in Annex IIIa, it includes information on the prevalence of food allergy in unselected populations, on proteins identified as food allergens, on cross-reactivities, on the effects of food processing on the allergenicity of foods and ingredients, on methods for the detection of allergens and allergenic foods, and on doses observed to trigger adverse reactions in sensitive individuals.Immune-mediated adverse reactions to foods manifest with clinical signs and symptoms of variable severity and duration, which may affect different organs and systems. Anaphylactic reactions to food are IgE mediated and may occur at any age. Non-IgE-mediated food allergy includes a wide range of diseases, including protein-induced enterocolitis and eosinophilic oesophagitis.A careful family and clinical history are the basis for diagnosis of food allergy. Food diaries, skin prick tests (SPTs), allergen-specific IgE measurements, food elimination diets and food challenges are part of the standard protocol for the diagnosis of food allergy. A positive SPT indicates sensitisation to the tested food, but it is not diagnostic of food allergy. Allergen-specific serum IgE antibodies similarly denote sensitisation to a particular food, but they are not diagnostic without a clinical history or food challenge. The use of atopy patch tests for the diagnosis of food allergy is controversial. Other available tests have no current role in the diagnosis of food allergy. Diag...

show abstract

Sequence microheterogeneity of parvalbumin, the major fish allergen

Cited by 9 publications

References 56 publications

A Cross-Reactive Human Single-Chain Antibody for Detection of Major Fish Allergens, Parvalbumins, and Identification of a Major IgE-Binding Epitope

A Cross-Reactive Human Single-Chain Antibody for Detection of Major Fish Allergens, Parvalbumins, and Identification of a Major IgE-Binding Epitope

Fish Allergens at a Glance: Variable Allergenicity of Parvalbumins, the Major Fish Allergens

Scientific Opinion on the evaluation of allergenic foods and food ingredients for labelling purposes

Contact Info

Product

Resources

About