Cross-Reactivity between Major IgE Epitopes of Family 5 Allergens from Dermatophagoides pteronyssinus and Blomia tropicalis.
Adult
Allergens
/ genetics
Animals
Antibody Specificity
Antigens, Dermatophagoides
/ genetics
Arthropod Proteins
/ genetics
Cross Reactions
/ immunology
Dermatophagoides pteronyssinus
/ genetics
Enzyme-Linked Immunosorbent Assay
Epitope Mapping
Epitopes
/ chemistry
Female
Humans
Hypersensitivity
/ blood
Immunoglobulin E
/ blood
Male
Middle Aged
Mutagenesis
Recombinant Proteins
Young Adult
Allergen
Cross-reactivity
House dust mite
Peptide epitope
Journal
International archives of allergy and immunology
ISSN: 1423-0097
Titre abrégé: Int Arch Allergy Immunol
Pays: Switzerland
ID NLM: 9211652
Informations de publication
Date de publication:
Historique:
received:
25
03
2018
accepted:
11
08
2018
pubmed:
1
11
2018
medline:
11
4
2019
entrez:
1
11
2018
Statut:
ppublish
Résumé
The aim of this work was to understand the molecular features that trigger the cross-reactivity observed between Der p 5 from Dermatophagoides pteronyssinus, Blo t 5 from Blomia tropicalis, and Der f 5 from D. farinae. We collected serum from 60 house dust mite (HDM)-allergic patients residing in the Dellys area of Boumerdès province in northern Algeria. The presence of specific IgE to Der p 5, Der f 5, and Blo t 5 was analyzed. We performed in silico analysis of the structure of the different allergens in order to identify epitopes that can elicit the cross-reactivity of the sera. Synthetic peptides corresponding to the linear epitope sequence of Der p 5, Der f 5, and Blo t 5 were used to evaluate its implication in the cross-reactivity between the allergens. We also modified the sequence of the conformational epitope of Der p 5 by site-directed mutagenesis to mimic Blo t 5. Several sera of patients allergic to HDM contained specific IgE antibodies to Der p 5 and Blo t 5. We demonstrated that the linear epitope of Der p 5 and Blo t 5 is not involved in the cross-reactivity of the sera. Furthermore, mutations introduced in the sequence of Der p 5 to mimic Blo t 5 could not modulate the cross-reactivity between them. The major linear IgE epitopes of Der p 5 and Blo t 5 are involved in species-specific recognition. Our results may be useful for the development of a hypoallergenic vaccine against HDM group 5 allergens.
Sections du résumé
BACKGROUND
BACKGROUND
The aim of this work was to understand the molecular features that trigger the cross-reactivity observed between Der p 5 from Dermatophagoides pteronyssinus, Blo t 5 from Blomia tropicalis, and Der f 5 from D. farinae.
METHODS
METHODS
We collected serum from 60 house dust mite (HDM)-allergic patients residing in the Dellys area of Boumerdès province in northern Algeria. The presence of specific IgE to Der p 5, Der f 5, and Blo t 5 was analyzed. We performed in silico analysis of the structure of the different allergens in order to identify epitopes that can elicit the cross-reactivity of the sera. Synthetic peptides corresponding to the linear epitope sequence of Der p 5, Der f 5, and Blo t 5 were used to evaluate its implication in the cross-reactivity between the allergens. We also modified the sequence of the conformational epitope of Der p 5 by site-directed mutagenesis to mimic Blo t 5.
RESULTS
RESULTS
Several sera of patients allergic to HDM contained specific IgE antibodies to Der p 5 and Blo t 5. We demonstrated that the linear epitope of Der p 5 and Blo t 5 is not involved in the cross-reactivity of the sera. Furthermore, mutations introduced in the sequence of Der p 5 to mimic Blo t 5 could not modulate the cross-reactivity between them.
CONCLUSIONS
CONCLUSIONS
The major linear IgE epitopes of Der p 5 and Blo t 5 are involved in species-specific recognition. Our results may be useful for the development of a hypoallergenic vaccine against HDM group 5 allergens.
Identifiants
pubmed: 30380546
pii: 000492871
doi: 10.1159/000492871
doi:
Substances chimiques
Allergens
0
Antigens, Dermatophagoides
0
Arthropod Proteins
0
Dermatophagoides pteronyssinus antigen p 5
0
Epitopes
0
Recombinant Proteins
0
Immunoglobulin E
37341-29-0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
10-18Informations de copyright
© 2018 S. Karger AG, Basel.