Isolation and characterization of native Cry j 3 from Japanese cedar (Cryptomeria japonica) pollen.
Identifieur interne : 000367 ( Main/Exploration ); précédent : 000366; suivant : 000368Isolation and characterization of native Cry j 3 from Japanese cedar (Cryptomeria japonica) pollen.
Auteurs : T. Fujimura [Japon] ; N. Futamura ; T. Midoro-Horiuti ; A. Togawa ; R M Goldblum ; H. Yasueda ; A. Saito ; K. Shinohara ; K. Masuda ; K. Kurata ; M. SakaguchiSource :
- Allergy [ 0105-4538 ] ; 2007.
Descripteurs français
- KwdFr :
- Antigènes végétaux (immunologie), Antigènes végétaux (isolement et purification), Antigènes végétaux (métabolisme), Cryptomeria (composition chimique), Cryptomeria (génétique), Cryptomeria (immunologie), Données de séquences moléculaires (MeSH), Humains (MeSH), Hypersensibilité (immunologie), Hypersensibilité (métabolisme), Immunoglobuline E (biosynthèse), Immunoglobuline E (sang), Isoformes de protéines (immunologie), Isoformes de protéines (métabolisme), Liaison aux protéines (immunologie), Pollen (composition chimique), Pollen (immunologie), Sites de fixation des anticorps (MeSH), Séquence d'acides aminés (MeSH), Séquence nucléotidique (MeSH).
- MESH :
- biosynthèse : Immunoglobuline E.
- composition chimique : Cryptomeria, Pollen.
- génétique : Cryptomeria.
- immunologie : Antigènes végétaux, Cryptomeria, Hypersensibilité, Isoformes de protéines, Liaison aux protéines, Pollen.
- isolement et purification : Antigènes végétaux.
- métabolisme : Antigènes végétaux, Hypersensibilité, Isoformes de protéines.
- sang : Immunoglobuline E.
- Données de séquences moléculaires, Humains, Sites de fixation des anticorps, Séquence d'acides aminés, Séquence nucléotidique.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Antigens, Plant (immunology), Antigens, Plant (isolation & purification), Antigens, Plant (metabolism), Base Sequence (MeSH), Binding Sites, Antibody (MeSH), Cryptomeria (chemistry), Cryptomeria (genetics), Cryptomeria (immunology), Humans (MeSH), Hypersensitivity (immunology), Hypersensitivity (metabolism), Immunoglobulin E (biosynthesis), Immunoglobulin E (blood), Molecular Sequence Data (MeSH), Pollen (chemistry), Pollen (immunology), Protein Binding (immunology), Protein Isoforms (immunology), Protein Isoforms (metabolism).
- MESH :
- chemical , biosynthesis : Immunoglobulin E.
- chemical , blood : Immunoglobulin E.
- chemical , immunology : Antigens, Plant, Protein Isoforms.
- chemical , isolation & purification : Antigens, Plant.
- chemical , metabolism : Antigens, Plant, Protein Isoforms.
- chemistry : Cryptomeria, Pollen.
- genetics : Cryptomeria.
- immunology : Cryptomeria, Hypersensitivity, Pollen, Protein Binding.
- metabolism : Hypersensitivity.
- Amino Acid Sequence, Base Sequence, Binding Sites, Antibody, Humans, Molecular Sequence Data.
Abstract
BACKGROUND
Japanese cedar (Cryptomeria japonica) pollinosis is the most prevalent allergy in Japan. Recently, the Japanese cedar pollen allergen Cry j 3 was cloned as a homologue of Jun a 3, which is a major allergen from mountain cedar (Juniperus ashei) pollen. However, native Cry j 3 has not been isolated and there are no reports on its allergenic activity. The aims of this study were to isolate native Cry j 3 and assess its immunoglobulin E (IgE)-binding capacity in patients with Japanese cedar pollinosis.
METHODS
Native Cry j 3 was purified from Japanese cedar pollen by multidimensional chromatography. We assessed the IgE-binding capacity using sera from patients allergic to Japanese cedar pollen by immunoblot analysis and ELISA. Moreover, we assayed the capacity of Cry j 3 to induce histamine release from the patients' leukocytes. We cloned cDNA corresponding to purified Cry j 3 from a cDNA library of Japanese cedar pollen.
RESULTS
We isolated native Cry j 3 as a 27-kDa protein. The IgE-binding frequency of Cry j 3 from the sera of patients allergic to Japanese cedar pollen was estimated as 27% (27/100) by ELISA. Cry j 3 induced the release of histamine from leukocytes. We cloned the cDNA and named it Cry j 3.8. Cry j 3.8 cDNA encoded 225 amino acids and had significant homology with thaumatin-like proteins.
CONCLUSIONS
Cry j 3 is a causative allergen in Japanese cedar pollinosis and may play crucial roles in the cross-reactivity with oral allergy syndrome.
DOI: 10.1111/j.1398-9995.2007.01331.x
PubMed: 17441795
PubMed Central: PMC2587458
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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<term>Antigens, Plant (metabolism)</term>
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<front><div type="abstract" xml:lang="en"><p><b>BACKGROUND</b>
</p>
<p>Japanese cedar (Cryptomeria japonica) pollinosis is the most prevalent allergy in Japan. Recently, the Japanese cedar pollen allergen Cry j 3 was cloned as a homologue of Jun a 3, which is a major allergen from mountain cedar (Juniperus ashei) pollen. However, native Cry j 3 has not been isolated and there are no reports on its allergenic activity. The aims of this study were to isolate native Cry j 3 and assess its immunoglobulin E (IgE)-binding capacity in patients with Japanese cedar pollinosis.</p>
</div>
<div type="abstract" xml:lang="en"><p><b>METHODS</b>
</p>
<p>Native Cry j 3 was purified from Japanese cedar pollen by multidimensional chromatography. We assessed the IgE-binding capacity using sera from patients allergic to Japanese cedar pollen by immunoblot analysis and ELISA. Moreover, we assayed the capacity of Cry j 3 to induce histamine release from the patients' leukocytes. We cloned cDNA corresponding to purified Cry j 3 from a cDNA library of Japanese cedar pollen.</p>
</div>
<div type="abstract" xml:lang="en"><p><b>RESULTS</b>
</p>
<p>We isolated native Cry j 3 as a 27-kDa protein. The IgE-binding frequency of Cry j 3 from the sera of patients allergic to Japanese cedar pollen was estimated as 27% (27/100) by ELISA. Cry j 3 induced the release of histamine from leukocytes. We cloned the cDNA and named it Cry j 3.8. Cry j 3.8 cDNA encoded 225 amino acids and had significant homology with thaumatin-like proteins.</p>
</div>
<div type="abstract" xml:lang="en"><p><b>CONCLUSIONS</b>
</p>
<p>Cry j 3 is a causative allergen in Japanese cedar pollinosis and may play crucial roles in the cross-reactivity with oral allergy syndrome.</p>
</div>
</front>
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<Abstract><AbstractText Label="BACKGROUND" NlmCategory="BACKGROUND">Japanese cedar (Cryptomeria japonica) pollinosis is the most prevalent allergy in Japan. Recently, the Japanese cedar pollen allergen Cry j 3 was cloned as a homologue of Jun a 3, which is a major allergen from mountain cedar (Juniperus ashei) pollen. However, native Cry j 3 has not been isolated and there are no reports on its allergenic activity. The aims of this study were to isolate native Cry j 3 and assess its immunoglobulin E (IgE)-binding capacity in patients with Japanese cedar pollinosis.</AbstractText>
<AbstractText Label="METHODS" NlmCategory="METHODS">Native Cry j 3 was purified from Japanese cedar pollen by multidimensional chromatography. We assessed the IgE-binding capacity using sera from patients allergic to Japanese cedar pollen by immunoblot analysis and ELISA. Moreover, we assayed the capacity of Cry j 3 to induce histamine release from the patients' leukocytes. We cloned cDNA corresponding to purified Cry j 3 from a cDNA library of Japanese cedar pollen.</AbstractText>
<AbstractText Label="RESULTS" NlmCategory="RESULTS">We isolated native Cry j 3 as a 27-kDa protein. The IgE-binding frequency of Cry j 3 from the sera of patients allergic to Japanese cedar pollen was estimated as 27% (27/100) by ELISA. Cry j 3 induced the release of histamine from leukocytes. We cloned the cDNA and named it Cry j 3.8. Cry j 3.8 cDNA encoded 225 amino acids and had significant homology with thaumatin-like proteins.</AbstractText>
<AbstractText Label="CONCLUSIONS" NlmCategory="CONCLUSIONS">Cry j 3 is a causative allergen in Japanese cedar pollinosis and may play crucial roles in the cross-reactivity with oral allergy syndrome.</AbstractText>
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