Linear epitopes of bony fish β-parvalbumins
(2024) In Frontiers in Immunology 15.- Abstract
Introduction: Fish β-parvalbumins are common targets of allergy-causing immunity. The nature of antibody responses to such allergens determines the biological outcome following exposure to fish. Specific epitopes on these allergens recognised by antibodies are incompletely characterised. Methods: High-content peptide microarrays offer a solution to the identification of linear epitopes recognised by antibodies. We characterized IgG and IgG4 recognition of linear epitopes of fish β-parvalbumins defined in the WHO/IUIS allergen database as such responses hold the potential to counter an allergic reaction to these allergens. Peripheral blood samples, collected over three years, of 15 atopic but not fish-allergic subjects were investigated... (More)
Introduction: Fish β-parvalbumins are common targets of allergy-causing immunity. The nature of antibody responses to such allergens determines the biological outcome following exposure to fish. Specific epitopes on these allergens recognised by antibodies are incompletely characterised. Methods: High-content peptide microarrays offer a solution to the identification of linear epitopes recognised by antibodies. We characterized IgG and IgG4 recognition of linear epitopes of fish β-parvalbumins defined in the WHO/IUIS allergen database as such responses hold the potential to counter an allergic reaction to these allergens. Peripheral blood samples, collected over three years, of 15 atopic but not fish-allergic subjects were investigated using a microarray platform that carried every possible 16-mer peptide of known isoforms and isoallergens of these and other allergens. Results: Interindividual differences in epitope recognition patterns were observed. In contrast, reactivity patterns in a given individual were by comparison more stable during the 3 years-course of the study. Nevertheless, evidence of the induction of novel specificities over time was identified across multiple regions of the allergens. Particularly reactive epitopes were identified in the D helix of Cyp c 1 and in the C-terminus of Gad c 1 and Gad m 1.02. Residues important for the recognition of certain linear epitopes were identified. Patterns of differential recognition of isoallergens were observed in some subjects. Conclusions: Altogether, comprehensive analysis of antibody recognition of linear epitopes of multiple allergens enables characterisation of the nature of the antibody responses targeting this important set of food allergens.
(Less)
- author
- Franciskovic, Eric
LU
; Thörnqvist, Linnea
LU
; Greiff, Lennart
LU
; Gasset, Maria
and Ohlin, Mats
LU
- organization
- publishing date
- 2024
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- allergen, epitope, fish, microarray, parvalbumin, peptide microarray
- in
- Frontiers in Immunology
- volume
- 15
- article number
- 1293793
- publisher
- Frontiers Media S. A.
- external identifiers
-
- pmid:38504976
- scopus:85188085080
- ISSN
- 1664-3224
- DOI
- 10.3389/fimmu.2024.1293793
- language
- English
- LU publication?
- yes
- id
- a457e462-6777-4314-85c7-676d33206493
- date added to LUP
- 2024-04-10 10:57:44
- date last changed
- 2024-08-14 23:51:31
@article{a457e462-6777-4314-85c7-676d33206493, abstract = {{<p>Introduction: Fish β-parvalbumins are common targets of allergy-causing immunity. The nature of antibody responses to such allergens determines the biological outcome following exposure to fish. Specific epitopes on these allergens recognised by antibodies are incompletely characterised. Methods: High-content peptide microarrays offer a solution to the identification of linear epitopes recognised by antibodies. We characterized IgG and IgG4 recognition of linear epitopes of fish β-parvalbumins defined in the WHO/IUIS allergen database as such responses hold the potential to counter an allergic reaction to these allergens. Peripheral blood samples, collected over three years, of 15 atopic but not fish-allergic subjects were investigated using a microarray platform that carried every possible 16-mer peptide of known isoforms and isoallergens of these and other allergens. Results: Interindividual differences in epitope recognition patterns were observed. In contrast, reactivity patterns in a given individual were by comparison more stable during the 3 years-course of the study. Nevertheless, evidence of the induction of novel specificities over time was identified across multiple regions of the allergens. Particularly reactive epitopes were identified in the D helix of Cyp c 1 and in the C-terminus of Gad c 1 and Gad m 1.02. Residues important for the recognition of certain linear epitopes were identified. Patterns of differential recognition of isoallergens were observed in some subjects. Conclusions: Altogether, comprehensive analysis of antibody recognition of linear epitopes of multiple allergens enables characterisation of the nature of the antibody responses targeting this important set of food allergens.</p>}}, author = {{Franciskovic, Eric and Thörnqvist, Linnea and Greiff, Lennart and Gasset, Maria and Ohlin, Mats}}, issn = {{1664-3224}}, keywords = {{allergen; epitope; fish; microarray; parvalbumin; peptide microarray}}, language = {{eng}}, publisher = {{Frontiers Media S. A.}}, series = {{Frontiers in Immunology}}, title = {{Linear epitopes of bony fish β-parvalbumins}}, url = {{http://dx.doi.org/10.3389/fimmu.2024.1293793}}, doi = {{10.3389/fimmu.2024.1293793}}, volume = {{15}}, year = {{2024}}, }