Purification, characterization and molecular cloning of Cha o 1, a major allergen of Chamaecyparis obtusa (Japanese cypress) pollen

Suzuki, Motohiko; Komiyama, Naoki; Itoh, Makoto; Itoh, Hideomi; Sone, Toshio; Kino, Kohsuke; Takagi, Ippei; Ohta, Nobuo

doi:10.1016/0161-5890(95)00147-6

Cited by 60 publications

(55 citation statements)

References 35 publications

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“…The propensity for cedar allergens to induce IgE antibody responses and mediate allergic reactions is indicated by the finding that approximately half of those who suffer from mountain cedar pollinosis do not have reactions to any other allergens. The pollen of related species are responsible for severe, seasonal allergic diseases in Japan (Cryptomeria japonica (2,3) and Chamaecyparis obtusa (4)) and Europe (Cupressus arizonica (5) and Cupressus sempervirens (6)). Furthermore, the pollen from Juniperus ashei is cross-reactive with those from other cedars and cypresses (1), suggesting that homologues of the mountain cedar allergen participate in the vigorous allergic responses in diverse geographic regions and human populations.…”

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confidence: 99%

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Crystal Structure of Jun a 1, the Major Cedar Pollen Allergen from Juniperus ashei, Reveals a Parallel β-Helical Core

Czerwinski

Midoro-Horiuti

White

et al. 2005

Journal of Biological Chemistry

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Pollen from cedar and cypress trees is a major cause of seasonal hypersensitivity in humans in several regions of the Northern Hemisphere. We report the first crystal structure of a cedar allergen, Jun a 1, from the pollen of the mountain cedar Juniperus ashei (Cupressaceae). The core of the structure consists primarily of a parallel ␤-helix, which is nearly identical to that found in the pectin/pectate lyases from several plant pathogenic microorganisms. Four IgE epitopes mapped to the surface of the protein are accessible to the solvent. The conserved vWiDH sequence is covered by the first 30 residues of the N terminus. The potential reactive arginine, analogous to the pectin/pectate lyase reaction site, is accessible to the solvent, but the substrate binding groove is blocked by a histidine-aspartate salt bridge, a glutamine, and an ␣-helix, all of which are unique to Jun a 1. These observations suggest that steric hindrance in Jun a 1 precludes enzyme activity. The overall results suggest that it is the structure of Jun a 1 that makes it a potent allergen.

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confidence: 99%

“…3 Solvent accessibility calculations were performed using WhatIF (31). 4 Secondary structure alignments were calculated by the method of Krissinel and Henrick (32,33). 5 …”

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confidence: 99%

Crystal Structure of Jun a 1, the Major Cedar Pollen Allergen from Juniperus ashei, Reveals a Parallel β-Helical Core

Czerwinski

Midoro-Horiuti

White

et al. 2005

Journal of Biological Chemistry

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“…Recognition of this epitope by patient IgE was shown to require glycosylation. However, since none of the five known allergenic homologues of Cry j 1 share this glycosylation site (Midoro-Horiuti et al, 2001;Aceituno et al, 2000;Suzuki et al, 1996;Sone et al, 1994), this epitope cannot be shared with the other known cedar allergens (Midoro-Horiuti et al, 1992;Schwietz et al, 2000). The presence of additional IgE epitopes on Cry j 1 was demonstrated by the finding that three unique groups of anti-Cry j 1 mAbs inhibited the binding to Cry j 1 of IgE from the sera of patients with Japanese cedar hypersensitivity (Sakaguchi et al, 1997).…”

Section: Discussionmentioning

confidence: 99%

“…Group 1 allergens, which are structurally similar to bacterial pectate and pectin lyases (Czerwinski et al, 2005), have been isolated from pollens of mountain cedar (Jun a 1, Juniperus ashei, Cupressaceae; Midoro-Horiuti et al, 1999), eastern red cedar (Jun v 1, Juniperus virginiana, Cupressaceae;Midoro-Horiuti et al, 2001), Italian cypress (Cup s 1, Cupressus sempervirens, Cupressaceae; Arilla et al, 2004), Japanese cypress (Cha o 1, Chamaecyparis obtusa, Cupressaceae; Suzuki et al, 1996) and Japanese cedar (Cry j 1, Cryptomeria japonica, Taxodiaceae; Yasueda et al, 1983). A substantial proportion of the IgE anti-cedar pollen antibodies from patients with mountain cedar allergy react with Cry j 1 (Midoro-Horiuti et al, 1999;Taniai et al, 1993).…”

Section: Introductionmentioning

confidence: 99%

Structural basis for epitope sharing between group 1 allergens of cedar pollen

Midoro-Horiuti

Schein

Mathura

et al. 2006

Molecular Immunology

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The group 1 allergens are a major cause of cedar pollen hypersensitivity in several geographic areas. Allergens from several taxa have been shown to cross-react. The goal of these studies was to compare the structural features of the shared and unique epitopes of the group 1 allergen from mountain cedar (Jun a 1) and Japanese cedar (Cry j 1). An array of overlapping peptides from the sequence of Jun a 1 and a panel of monoclonal anti-Cry j 1 antibodies were used to identify the IgE epitopes recognized by cedar-sensitive patients from Texas and Japan. IgE from Japanese patients reacted with peptides representing one of the two linear epitopes within the highly conserved β-helical core structure and both epitopes within less ordered loops and turns near the N-and C-termini of Jun a 1. A threedimensional (3D) model of the Cry j 1, based on the crystal structure of Jun a 1, indicated a similar surface exposure for the four described epitopes of Jun a 1 and the homologous regions of Cry j 1. The monoclonal antibodies identified another shared epitope, which is most likely conformational and a unique Cry j 1 epitope that may be the previously recognized glycopeptide IgE epitope. Defining the structural basis for shared and unique epitopes will help to identify critical features of IgE epitopes that can be used to develop mimotopes or identify allergen homologues for vaccine development.

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“…Japanese cypress pollen is another major allergic pollen in Japan, and Cha o 1 is a major allergen contained in the cypress pollens. Although it is known that Cha o 1 is Nglycosylated, 4) the detailed chemical structures of the N-glycan moiety remain to be determined. Hence, in this study, we analyzed the structures of N-glycans linked to the Japanese cypress pollen allergen Cha o 1 to determine whether plant specific antigenic oligosaccharide or Lewis a epitope occurs in the allergen.…”

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Glycoform Analysis of Japanese Cypress Pollen Allergen, Cha o 1: A Comparison of the Glycoforms of Cedar and Cypress Pollen Allergens

Kimura

Kuroki²,

Maeda

et al. 2008

Bioscience, Biotechnology, and Biochemistry

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Purification, characterization and molecular cloning of Cha o 1, a major allergen of Chamaecyparis obtusa (Japanese cypress) pollen

Cited by 60 publications

References 35 publications

Crystal Structure of Jun a 1, the Major Cedar Pollen Allergen from Juniperus ashei, Reveals a Parallel β-Helical Core

Crystal Structure of Jun a 1, the Major Cedar Pollen Allergen from Juniperus ashei, Reveals a Parallel β-Helical Core

Structural basis for epitope sharing between group 1 allergens of cedar pollen

Glycoform Analysis of Japanese Cypress Pollen Allergen, Cha o 1: A Comparison of the Glycoforms of Cedar and Cypress Pollen Allergens

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