Identification of Italian cypress (Cupressus sempervirens) pollen allergen Cup s 3 using homology and cross-reactivity

Akihisa Togawa, Raphael C. Panzani, Maritza A. Garza, Reiko Kishikawa, Randall M. Goldblum, Terumi Midoro-Horiuti

Research output: Contribution to journalArticle

20 Citations (Scopus)

Abstract

Background: The prevalence of seasonal allergic diseases of the upper airways is increasing in industrialized countries. The Cupressaceae are important causes of pollinosis, particularly in Europe. Objective: To determine whether the pollen from Cupressus sempervirens (Italian cypress) contains a pathogenesis-related group 5 (PR-5) protein, similar to that found in other allergenic Cupressaceae pollens. Methods: Messenger RNA was purified from Italian cypress pollen, and complementary DNA (cDNA) was synthesized. cDNAs for PR-5 proteins were amplified by polymerase chain reaction and extended by rapid amplification of cDNA ends methods. Recombinant Cup s 3 was expressed in Escherichia coli as a fusion protein. Inhibition enzyme-linked immunosorbent assays were used to test the allergenicity of Cup s 3. Results: Three cDNAs were cloned. These clones had approximately 95% identity to Jun a 3 and Cup a 3. Recombinant Cup s 3.0102 maltose-binding protein inhibited the IgE from most patients from binding to an extract of Italian cypress. The extent of inhibition suggested that antibodies to Cup s 3 were a prominent component of the IgE response to Italian cypress pollen. Conclusion: Cup s 3, an allergen of Italian cypress pollen, was identified based on cross-reactivity and homology with other pollen PR-5 proteins, despite an apparently low level of protein expression. Variations in the content of Cup s 3 in the pollen from different regions or trees should be considered in the choice of extracts for diagnosis and specific immunotherapy for Italian cypress pollen hypersensitivity.

Original languageEnglish (US)
Pages (from-to)336-342
Number of pages7
JournalAnnals of Allergy, Asthma and Immunology
Volume97
Issue number3
StatePublished - Sep 2006

Fingerprint

Cupressus
Pollen
Allergens
Cupressaceae
Complementary DNA
Proteins
Immunoglobulin E
Maltose-Binding Proteins
Seasonal Allergic Rhinitis
Developed Countries
Immunotherapy
Hypersensitivity
Clone Cells
Enzyme-Linked Immunosorbent Assay
Escherichia coli
Polymerase Chain Reaction
Messenger RNA

ASJC Scopus subject areas

  • Immunology and Allergy

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Identification of Italian cypress (Cupressus sempervirens) pollen allergen Cup s 3 using homology and cross-reactivity. / Togawa, Akihisa; Panzani, Raphael C.; Garza, Maritza A.; Kishikawa, Reiko; Goldblum, Randall M.; Midoro-Horiuti, Terumi.

In: Annals of Allergy, Asthma and Immunology, Vol. 97, No. 3, 09.2006, p. 336-342.

Research output: Contribution to journalArticle

Togawa, Akihisa ; Panzani, Raphael C. ; Garza, Maritza A. ; Kishikawa, Reiko ; Goldblum, Randall M. ; Midoro-Horiuti, Terumi. / Identification of Italian cypress (Cupressus sempervirens) pollen allergen Cup s 3 using homology and cross-reactivity. In: Annals of Allergy, Asthma and Immunology. 2006 ; Vol. 97, No. 3. pp. 336-342.
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abstract = "Background: The prevalence of seasonal allergic diseases of the upper airways is increasing in industrialized countries. The Cupressaceae are important causes of pollinosis, particularly in Europe. Objective: To determine whether the pollen from Cupressus sempervirens (Italian cypress) contains a pathogenesis-related group 5 (PR-5) protein, similar to that found in other allergenic Cupressaceae pollens. Methods: Messenger RNA was purified from Italian cypress pollen, and complementary DNA (cDNA) was synthesized. cDNAs for PR-5 proteins were amplified by polymerase chain reaction and extended by rapid amplification of cDNA ends methods. Recombinant Cup s 3 was expressed in Escherichia coli as a fusion protein. Inhibition enzyme-linked immunosorbent assays were used to test the allergenicity of Cup s 3. Results: Three cDNAs were cloned. These clones had approximately 95{\%} identity to Jun a 3 and Cup a 3. Recombinant Cup s 3.0102 maltose-binding protein inhibited the IgE from most patients from binding to an extract of Italian cypress. The extent of inhibition suggested that antibodies to Cup s 3 were a prominent component of the IgE response to Italian cypress pollen. Conclusion: Cup s 3, an allergen of Italian cypress pollen, was identified based on cross-reactivity and homology with other pollen PR-5 proteins, despite an apparently low level of protein expression. Variations in the content of Cup s 3 in the pollen from different regions or trees should be considered in the choice of extracts for diagnosis and specific immunotherapy for Italian cypress pollen hypersensitivity.",
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