The chitinase allergens Der p 15 and Der p 18 from Dermatophagoides pteronyssinus

Susan O'Neill, T Heinrich, Belinda Hales, L Hazell, Deborah Holt, K FISCHER, Wayne Thomas

    Research output: Contribution to journalArticleResearchpeer-review

    Abstract

    Background: House dust mites Dermatophagoides pteronyssinus and Dermatophagoides farinae cause allergic disease in humans as well as in dogs. In geographical regions where the two mite species coexist, they both elicit specific immunoglobulin (Ig E) responses in humans whereas dogs preferentially react to D. farinae extracts. In dogs the main IgE binding is directed to the D. farinae chitinase allergens Der f 15 and Der f 18 and not to the groups 1 and 2 allergens as found for humans. Although the IgE response of humans to Der f 18 has been investigated there is no report on Der f 15-specific IgE in humans. Objective: This study aimed to characterize the chitinase allergens Der p 15 and Der p 18 of D. pteronyssinus and to find out whether they are important allergens for humans. Methods: cDNA was cloned by a polymerase chain reaction strategy from D. pteronyssinus libraries using primers based on conserved chitinase sequences. IgE binding to the recombinant polypeptides was measured by immunosorbent assay. Mice were immunized with the polypeptides and cross-reactivity examined. Results: Two variants of Der p 15 were isolated, encoding mature proteins of 58.8 and 61.4 kDa. The amino acid sequences had 90% identity to Der f 15. The cDNA for Der p 18 encoded a mature protein of 49.2 kDa with 88% sequence identity to Der f 18. Der p 15-specific IgE was detected in 70% and Der p 18-specific IgE in 63% of a panel of 27 human allergic sera. Conclusions: The D. pteronyssinus chitinases Der p 15 and Der p 18 show a high frequency of binding to IgE in allergic human sera. They are therefore potentially important allergens for humans as well as dogs. � 2006 The Authors.
    Original languageEnglish
    Pages (from-to)831-839
    Number of pages9
    JournalClinical and Experimental Allergy
    Volume36
    Issue number6
    Publication statusPublished - 2006

    Fingerprint

    Dermatophagoides pteronyssinus
    Chitinases
    Allergens
    Immunoglobulin E
    Dermatophagoides farinae
    Dogs
    Complementary DNA
    Dermatophagoides Antigens
    Pyroglyphidae
    Immunosorbents
    Peptides
    Conserved Sequence
    Mites
    Serum
    Libraries
    Amino Acid Sequence
    Proteins
    Polymerase Chain Reaction

    Cite this

    O'Neill, S., Heinrich, T., Hales, B., Hazell, L., Holt, D., FISCHER, K., & Thomas, W. (2006). The chitinase allergens Der p 15 and Der p 18 from Dermatophagoides pteronyssinus. Clinical and Experimental Allergy, 36(6), 831-839.
    O'Neill, Susan ; Heinrich, T ; Hales, Belinda ; Hazell, L ; Holt, Deborah ; FISCHER, K ; Thomas, Wayne. / The chitinase allergens Der p 15 and Der p 18 from Dermatophagoides pteronyssinus. In: Clinical and Experimental Allergy. 2006 ; Vol. 36, No. 6. pp. 831-839.
    @article{4abfbb41f3dc431cba2606b292624449,
    title = "The chitinase allergens Der p 15 and Der p 18 from Dermatophagoides pteronyssinus",
    abstract = "Background: House dust mites Dermatophagoides pteronyssinus and Dermatophagoides farinae cause allergic disease in humans as well as in dogs. In geographical regions where the two mite species coexist, they both elicit specific immunoglobulin (Ig E) responses in humans whereas dogs preferentially react to D. farinae extracts. In dogs the main IgE binding is directed to the D. farinae chitinase allergens Der f 15 and Der f 18 and not to the groups 1 and 2 allergens as found for humans. Although the IgE response of humans to Der f 18 has been investigated there is no report on Der f 15-specific IgE in humans. Objective: This study aimed to characterize the chitinase allergens Der p 15 and Der p 18 of D. pteronyssinus and to find out whether they are important allergens for humans. Methods: cDNA was cloned by a polymerase chain reaction strategy from D. pteronyssinus libraries using primers based on conserved chitinase sequences. IgE binding to the recombinant polypeptides was measured by immunosorbent assay. Mice were immunized with the polypeptides and cross-reactivity examined. Results: Two variants of Der p 15 were isolated, encoding mature proteins of 58.8 and 61.4 kDa. The amino acid sequences had 90{\%} identity to Der f 15. The cDNA for Der p 18 encoded a mature protein of 49.2 kDa with 88{\%} sequence identity to Der f 18. Der p 15-specific IgE was detected in 70{\%} and Der p 18-specific IgE in 63{\%} of a panel of 27 human allergic sera. Conclusions: The D. pteronyssinus chitinases Der p 15 and Der p 18 show a high frequency of binding to IgE in allergic human sera. They are therefore potentially important allergens for humans as well as dogs. � 2006 The Authors.",
    keywords = "chitinase, complementary DNA, Der p 15 allergen, Der p 18 allergen, house dust allergen, immunoglobulin E, polypeptide, recombinant protein, unclassified drug, allergy, amino acid sequence, article, clinical article, controlled study, cross reaction, Dermatophagoides farinae, Dermatophagoides pteronyssinus, dog, enzyme linked immunosorbent assay, human, immune response, molecular cloning, nonhuman, nucleotide sequence, polymerase chain reaction, priority journal, protein binding, protein isolation, sequence homology, Amino Acid Sequence, Animals, Antigens, Dermatophagoides, Base Sequence, Case-Control Studies, Chitinase, Cloning, Molecular, Cross Reactions, DNA, Complementary, Gene Library, Humans, Hypersensitivity, Immunoglobulin E, Mice, Mice, Inbred C57BL, Molecular Sequence Data, Recombinant Proteins, Sequence Alignment, Sequence Analysis, DNA",
    author = "Susan O'Neill and T Heinrich and Belinda Hales and L Hazell and Deborah Holt and K FISCHER and Wayne Thomas",
    year = "2006",
    language = "English",
    volume = "36",
    pages = "831--839",
    journal = "Clinical and Experimental Allergy",
    issn = "0954-7894",
    publisher = "Wiley-Blackwell",
    number = "6",

    }

    O'Neill, S, Heinrich, T, Hales, B, Hazell, L, Holt, D, FISCHER, K & Thomas, W 2006, 'The chitinase allergens Der p 15 and Der p 18 from Dermatophagoides pteronyssinus', Clinical and Experimental Allergy, vol. 36, no. 6, pp. 831-839.

    The chitinase allergens Der p 15 and Der p 18 from Dermatophagoides pteronyssinus. / O'Neill, Susan; Heinrich, T; Hales, Belinda; Hazell, L; Holt, Deborah; FISCHER, K; Thomas, Wayne.

    In: Clinical and Experimental Allergy, Vol. 36, No. 6, 2006, p. 831-839.

    Research output: Contribution to journalArticleResearchpeer-review

    TY - JOUR

    T1 - The chitinase allergens Der p 15 and Der p 18 from Dermatophagoides pteronyssinus

    AU - O'Neill, Susan

    AU - Heinrich, T

    AU - Hales, Belinda

    AU - Hazell, L

    AU - Holt, Deborah

    AU - FISCHER, K

    AU - Thomas, Wayne

    PY - 2006

    Y1 - 2006

    N2 - Background: House dust mites Dermatophagoides pteronyssinus and Dermatophagoides farinae cause allergic disease in humans as well as in dogs. In geographical regions where the two mite species coexist, they both elicit specific immunoglobulin (Ig E) responses in humans whereas dogs preferentially react to D. farinae extracts. In dogs the main IgE binding is directed to the D. farinae chitinase allergens Der f 15 and Der f 18 and not to the groups 1 and 2 allergens as found for humans. Although the IgE response of humans to Der f 18 has been investigated there is no report on Der f 15-specific IgE in humans. Objective: This study aimed to characterize the chitinase allergens Der p 15 and Der p 18 of D. pteronyssinus and to find out whether they are important allergens for humans. Methods: cDNA was cloned by a polymerase chain reaction strategy from D. pteronyssinus libraries using primers based on conserved chitinase sequences. IgE binding to the recombinant polypeptides was measured by immunosorbent assay. Mice were immunized with the polypeptides and cross-reactivity examined. Results: Two variants of Der p 15 were isolated, encoding mature proteins of 58.8 and 61.4 kDa. The amino acid sequences had 90% identity to Der f 15. The cDNA for Der p 18 encoded a mature protein of 49.2 kDa with 88% sequence identity to Der f 18. Der p 15-specific IgE was detected in 70% and Der p 18-specific IgE in 63% of a panel of 27 human allergic sera. Conclusions: The D. pteronyssinus chitinases Der p 15 and Der p 18 show a high frequency of binding to IgE in allergic human sera. They are therefore potentially important allergens for humans as well as dogs. � 2006 The Authors.

    AB - Background: House dust mites Dermatophagoides pteronyssinus and Dermatophagoides farinae cause allergic disease in humans as well as in dogs. In geographical regions where the two mite species coexist, they both elicit specific immunoglobulin (Ig E) responses in humans whereas dogs preferentially react to D. farinae extracts. In dogs the main IgE binding is directed to the D. farinae chitinase allergens Der f 15 and Der f 18 and not to the groups 1 and 2 allergens as found for humans. Although the IgE response of humans to Der f 18 has been investigated there is no report on Der f 15-specific IgE in humans. Objective: This study aimed to characterize the chitinase allergens Der p 15 and Der p 18 of D. pteronyssinus and to find out whether they are important allergens for humans. Methods: cDNA was cloned by a polymerase chain reaction strategy from D. pteronyssinus libraries using primers based on conserved chitinase sequences. IgE binding to the recombinant polypeptides was measured by immunosorbent assay. Mice were immunized with the polypeptides and cross-reactivity examined. Results: Two variants of Der p 15 were isolated, encoding mature proteins of 58.8 and 61.4 kDa. The amino acid sequences had 90% identity to Der f 15. The cDNA for Der p 18 encoded a mature protein of 49.2 kDa with 88% sequence identity to Der f 18. Der p 15-specific IgE was detected in 70% and Der p 18-specific IgE in 63% of a panel of 27 human allergic sera. Conclusions: The D. pteronyssinus chitinases Der p 15 and Der p 18 show a high frequency of binding to IgE in allergic human sera. They are therefore potentially important allergens for humans as well as dogs. � 2006 The Authors.

    KW - chitinase

    KW - complementary DNA

    KW - Der p 15 allergen

    KW - Der p 18 allergen

    KW - house dust allergen

    KW - immunoglobulin E

    KW - polypeptide

    KW - recombinant protein

    KW - unclassified drug

    KW - allergy

    KW - amino acid sequence

    KW - article

    KW - clinical article

    KW - controlled study

    KW - cross reaction

    KW - Dermatophagoides farinae

    KW - Dermatophagoides pteronyssinus

    KW - dog

    KW - enzyme linked immunosorbent assay

    KW - human

    KW - immune response

    KW - molecular cloning

    KW - nonhuman

    KW - nucleotide sequence

    KW - polymerase chain reaction

    KW - priority journal

    KW - protein binding

    KW - protein isolation

    KW - sequence homology

    KW - Amino Acid Sequence

    KW - Animals

    KW - Antigens, Dermatophagoides

    KW - Base Sequence

    KW - Case-Control Studies

    KW - Chitinase

    KW - Cloning, Molecular

    KW - Cross Reactions

    KW - DNA, Complementary

    KW - Gene Library

    KW - Humans

    KW - Hypersensitivity

    KW - Immunoglobulin E

    KW - Mice

    KW - Mice, Inbred C57BL

    KW - Molecular Sequence Data

    KW - Recombinant Proteins

    KW - Sequence Alignment

    KW - Sequence Analysis, DNA

    M3 - Article

    VL - 36

    SP - 831

    EP - 839

    JO - Clinical and Experimental Allergy

    JF - Clinical and Experimental Allergy

    SN - 0954-7894

    IS - 6

    ER -

    O'Neill S, Heinrich T, Hales B, Hazell L, Holt D, FISCHER K et al. The chitinase allergens Der p 15 and Der p 18 from Dermatophagoides pteronyssinus. Clinical and Experimental Allergy. 2006;36(6):831-839.