Sequence analysis and expression of a cDNA clone encoding a 98-kDa allergen in Dermatophagoides farinae
The important dust mite allergens identified to date are of molecular weights ranging from 14 to 60 kDa. Our previous protein study indicated that the 98-kDa native paramyosin in Dermatophagoides farinae mite showed IgE reactivity with 82% of the mite-sensitive asthmatic patients suggesting that it...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Tsai, L.-C. [verfasserIn] Sun, Y.-C. [verfasserIn] Chao, P.-L. [verfasserIn] |
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| Format: |
E-Artikel |
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| Erschienen: |
Oxford BSL: Blackwell Science Ltd ; 1999 |
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| Umfang: |
Online-Ressource |
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| Reproduktion: |
2002 ; Blackwell Publishing Journal Backfiles 1879-2005 |
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| Übergeordnetes Werk: |
In: Clinical & experimental allergy - Oxford : Blackwell Science, 1989, 29(1999), 12, Seite 0 |
| Übergeordnetes Werk: |
volume:29 ; year:1999 ; number:12 ; pages:0 |
| Links: |
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| DOI / URN: |
10.1046/j.1365-2222.1999.00603.x |
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| Katalog-ID: |
NLEJ242619843 |
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| 100 | 1 | |a Tsai, L.-C. |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a Sequence analysis and expression of a cDNA clone encoding a 98-kDa allergen in Dermatophagoides farinae |
| 264 | 1 | |a Oxford BSL |b Blackwell Science Ltd |c 1999 | |
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| 520 | |a The important dust mite allergens identified to date are of molecular weights ranging from 14 to 60 kDa. Our previous protein study indicated that the 98-kDa native paramyosin in Dermatophagoides farinae mite showed IgE reactivity with 82% of the mite-sensitive asthmatic patients suggesting that it is a novel major mite allergen. This study described the isolation and characterization of the cDNA clone encoding the 98-kDa mite allergen.<section xml:id="abs1-2"><title type="main">MethodsA Dermatophagoides farinae cDNA library was constructed in lambda ZAPII vector and the library was immunoscreened with a monoclonal antibody 642. The cDNA insert was sub-cloned into M13 sequencing vector for single-stranded sequencing. The whole cDNA insert was expressed in pGEX-2T Escherichia coli expression system as a fusion protein with GST. The allergenicity of the recombinant peptides was tested by skin tests and IgE immunoassay. The IgE and IgG immunoassays were performed with sera from 20 mite-allergic patients.<section xml:id="abs1-3"><title type="main">ResultsThe cDNA clone Df642 was 2134 bp long, coding for a polypeptide of 711 amino acid residues. Protein sequence analysis and alignment confirmed that the deduced polypeptide is a mite paramyosin which is truncated slightly at the N- and C-terminuses. In vivo skin tests and in vitro IgE-binding study showed that 62% (13/21) and 50% (10/20) of the mite-sensitive asthmatic patients reacted positively with the recombinant Dermatophagoides farinae paramyosin, respectively.<section xml:id="abs1-4"><title type="main">ConclusionThe study indicated that 98-kDa mite paramyosin is an important allergen. | ||
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| 700 | 1 | |a Chao, P.-L. |e verfasserin |4 aut | |
| 700 | 1 | |a Ng, H.-P. |4 oth | |
| 700 | 1 | |a Hung, M.-W. |4 oth | |
| 700 | 1 | |a Hsieh, K.-H. |4 oth | |
| 700 | 1 | |a Liaw, S.-H. |4 oth | |
| 700 | 1 | |a Chua, K.-Y. |4 oth | |
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10.1046/j.1365-2222.1999.00603.x doi (DE-627)NLEJ242619843 DE-627 ger DE-627 rakwb Tsai, L.-C. verfasserin aut Sequence analysis and expression of a cDNA clone encoding a 98-kDa allergen in Dermatophagoides farinae Oxford BSL Blackwell Science Ltd 1999 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The important dust mite allergens identified to date are of molecular weights ranging from 14 to 60 kDa. Our previous protein study indicated that the 98-kDa native paramyosin in Dermatophagoides farinae mite showed IgE reactivity with 82% of the mite-sensitive asthmatic patients suggesting that it is a novel major mite allergen. This study described the isolation and characterization of the cDNA clone encoding the 98-kDa mite allergen.<section xml:id="abs1-2"><title type="main">MethodsA Dermatophagoides farinae cDNA library was constructed in lambda ZAPII vector and the library was immunoscreened with a monoclonal antibody 642. The cDNA insert was sub-cloned into M13 sequencing vector for single-stranded sequencing. The whole cDNA insert was expressed in pGEX-2T Escherichia coli expression system as a fusion protein with GST. The allergenicity of the recombinant peptides was tested by skin tests and IgE immunoassay. The IgE and IgG immunoassays were performed with sera from 20 mite-allergic patients.<section xml:id="abs1-3"><title type="main">ResultsThe cDNA clone Df642 was 2134 bp long, coding for a polypeptide of 711 amino acid residues. Protein sequence analysis and alignment confirmed that the deduced polypeptide is a mite paramyosin which is truncated slightly at the N- and C-terminuses. In vivo skin tests and in vitro IgE-binding study showed that 62% (13/21) and 50% (10/20) of the mite-sensitive asthmatic patients reacted positively with the recombinant Dermatophagoides farinae paramyosin, respectively.<section xml:id="abs1-4"><title type="main">ConclusionThe study indicated that 98-kDa mite paramyosin is an important allergen. 2002 Blackwell Publishing Journal Backfiles 1879-2005 |2002|||||||||| cDNA clone Sun, Y.-C. verfasserin aut Chao, P.-L. verfasserin aut Ng, H.-P. oth Hung, M.-W. oth Hsieh, K.-H. oth Liaw, S.-H. oth Chua, K.-Y. oth In Clinical & experimental allergy Oxford : Blackwell Science, 1989 29(1999), 12, Seite 0 Online-Ressource (DE-627)NLEJ243926391 (DE-600)2004469-0 1365-2222 nnns volume:29 year:1999 number:12 pages:0 http://dx.doi.org/10.1046/j.1365-2222.1999.00603.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 29 1999 12 0 |
| spelling |
10.1046/j.1365-2222.1999.00603.x doi (DE-627)NLEJ242619843 DE-627 ger DE-627 rakwb Tsai, L.-C. verfasserin aut Sequence analysis and expression of a cDNA clone encoding a 98-kDa allergen in Dermatophagoides farinae Oxford BSL Blackwell Science Ltd 1999 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The important dust mite allergens identified to date are of molecular weights ranging from 14 to 60 kDa. Our previous protein study indicated that the 98-kDa native paramyosin in Dermatophagoides farinae mite showed IgE reactivity with 82% of the mite-sensitive asthmatic patients suggesting that it is a novel major mite allergen. This study described the isolation and characterization of the cDNA clone encoding the 98-kDa mite allergen.<section xml:id="abs1-2"><title type="main">MethodsA Dermatophagoides farinae cDNA library was constructed in lambda ZAPII vector and the library was immunoscreened with a monoclonal antibody 642. The cDNA insert was sub-cloned into M13 sequencing vector for single-stranded sequencing. The whole cDNA insert was expressed in pGEX-2T Escherichia coli expression system as a fusion protein with GST. The allergenicity of the recombinant peptides was tested by skin tests and IgE immunoassay. The IgE and IgG immunoassays were performed with sera from 20 mite-allergic patients.<section xml:id="abs1-3"><title type="main">ResultsThe cDNA clone Df642 was 2134 bp long, coding for a polypeptide of 711 amino acid residues. Protein sequence analysis and alignment confirmed that the deduced polypeptide is a mite paramyosin which is truncated slightly at the N- and C-terminuses. In vivo skin tests and in vitro IgE-binding study showed that 62% (13/21) and 50% (10/20) of the mite-sensitive asthmatic patients reacted positively with the recombinant Dermatophagoides farinae paramyosin, respectively.<section xml:id="abs1-4"><title type="main">ConclusionThe study indicated that 98-kDa mite paramyosin is an important allergen. 2002 Blackwell Publishing Journal Backfiles 1879-2005 |2002|||||||||| cDNA clone Sun, Y.-C. verfasserin aut Chao, P.-L. verfasserin aut Ng, H.-P. oth Hung, M.-W. oth Hsieh, K.-H. oth Liaw, S.-H. oth Chua, K.-Y. oth In Clinical & experimental allergy Oxford : Blackwell Science, 1989 29(1999), 12, Seite 0 Online-Ressource (DE-627)NLEJ243926391 (DE-600)2004469-0 1365-2222 nnns volume:29 year:1999 number:12 pages:0 http://dx.doi.org/10.1046/j.1365-2222.1999.00603.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 29 1999 12 0 |
| allfields_unstemmed |
10.1046/j.1365-2222.1999.00603.x doi (DE-627)NLEJ242619843 DE-627 ger DE-627 rakwb Tsai, L.-C. verfasserin aut Sequence analysis and expression of a cDNA clone encoding a 98-kDa allergen in Dermatophagoides farinae Oxford BSL Blackwell Science Ltd 1999 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The important dust mite allergens identified to date are of molecular weights ranging from 14 to 60 kDa. Our previous protein study indicated that the 98-kDa native paramyosin in Dermatophagoides farinae mite showed IgE reactivity with 82% of the mite-sensitive asthmatic patients suggesting that it is a novel major mite allergen. This study described the isolation and characterization of the cDNA clone encoding the 98-kDa mite allergen.<section xml:id="abs1-2"><title type="main">MethodsA Dermatophagoides farinae cDNA library was constructed in lambda ZAPII vector and the library was immunoscreened with a monoclonal antibody 642. The cDNA insert was sub-cloned into M13 sequencing vector for single-stranded sequencing. The whole cDNA insert was expressed in pGEX-2T Escherichia coli expression system as a fusion protein with GST. The allergenicity of the recombinant peptides was tested by skin tests and IgE immunoassay. The IgE and IgG immunoassays were performed with sera from 20 mite-allergic patients.<section xml:id="abs1-3"><title type="main">ResultsThe cDNA clone Df642 was 2134 bp long, coding for a polypeptide of 711 amino acid residues. Protein sequence analysis and alignment confirmed that the deduced polypeptide is a mite paramyosin which is truncated slightly at the N- and C-terminuses. In vivo skin tests and in vitro IgE-binding study showed that 62% (13/21) and 50% (10/20) of the mite-sensitive asthmatic patients reacted positively with the recombinant Dermatophagoides farinae paramyosin, respectively.<section xml:id="abs1-4"><title type="main">ConclusionThe study indicated that 98-kDa mite paramyosin is an important allergen. 2002 Blackwell Publishing Journal Backfiles 1879-2005 |2002|||||||||| cDNA clone Sun, Y.-C. verfasserin aut Chao, P.-L. verfasserin aut Ng, H.-P. oth Hung, M.-W. oth Hsieh, K.-H. oth Liaw, S.-H. oth Chua, K.-Y. oth In Clinical & experimental allergy Oxford : Blackwell Science, 1989 29(1999), 12, Seite 0 Online-Ressource (DE-627)NLEJ243926391 (DE-600)2004469-0 1365-2222 nnns volume:29 year:1999 number:12 pages:0 http://dx.doi.org/10.1046/j.1365-2222.1999.00603.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 29 1999 12 0 |
| allfieldsGer |
10.1046/j.1365-2222.1999.00603.x doi (DE-627)NLEJ242619843 DE-627 ger DE-627 rakwb Tsai, L.-C. verfasserin aut Sequence analysis and expression of a cDNA clone encoding a 98-kDa allergen in Dermatophagoides farinae Oxford BSL Blackwell Science Ltd 1999 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The important dust mite allergens identified to date are of molecular weights ranging from 14 to 60 kDa. Our previous protein study indicated that the 98-kDa native paramyosin in Dermatophagoides farinae mite showed IgE reactivity with 82% of the mite-sensitive asthmatic patients suggesting that it is a novel major mite allergen. This study described the isolation and characterization of the cDNA clone encoding the 98-kDa mite allergen.<section xml:id="abs1-2"><title type="main">MethodsA Dermatophagoides farinae cDNA library was constructed in lambda ZAPII vector and the library was immunoscreened with a monoclonal antibody 642. The cDNA insert was sub-cloned into M13 sequencing vector for single-stranded sequencing. The whole cDNA insert was expressed in pGEX-2T Escherichia coli expression system as a fusion protein with GST. The allergenicity of the recombinant peptides was tested by skin tests and IgE immunoassay. The IgE and IgG immunoassays were performed with sera from 20 mite-allergic patients.<section xml:id="abs1-3"><title type="main">ResultsThe cDNA clone Df642 was 2134 bp long, coding for a polypeptide of 711 amino acid residues. Protein sequence analysis and alignment confirmed that the deduced polypeptide is a mite paramyosin which is truncated slightly at the N- and C-terminuses. In vivo skin tests and in vitro IgE-binding study showed that 62% (13/21) and 50% (10/20) of the mite-sensitive asthmatic patients reacted positively with the recombinant Dermatophagoides farinae paramyosin, respectively.<section xml:id="abs1-4"><title type="main">ConclusionThe study indicated that 98-kDa mite paramyosin is an important allergen. 2002 Blackwell Publishing Journal Backfiles 1879-2005 |2002|||||||||| cDNA clone Sun, Y.-C. verfasserin aut Chao, P.-L. verfasserin aut Ng, H.-P. oth Hung, M.-W. oth Hsieh, K.-H. oth Liaw, S.-H. oth Chua, K.-Y. oth In Clinical & experimental allergy Oxford : Blackwell Science, 1989 29(1999), 12, Seite 0 Online-Ressource (DE-627)NLEJ243926391 (DE-600)2004469-0 1365-2222 nnns volume:29 year:1999 number:12 pages:0 http://dx.doi.org/10.1046/j.1365-2222.1999.00603.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 29 1999 12 0 |
| allfieldsSound |
10.1046/j.1365-2222.1999.00603.x doi (DE-627)NLEJ242619843 DE-627 ger DE-627 rakwb Tsai, L.-C. verfasserin aut Sequence analysis and expression of a cDNA clone encoding a 98-kDa allergen in Dermatophagoides farinae Oxford BSL Blackwell Science Ltd 1999 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The important dust mite allergens identified to date are of molecular weights ranging from 14 to 60 kDa. Our previous protein study indicated that the 98-kDa native paramyosin in Dermatophagoides farinae mite showed IgE reactivity with 82% of the mite-sensitive asthmatic patients suggesting that it is a novel major mite allergen. This study described the isolation and characterization of the cDNA clone encoding the 98-kDa mite allergen.<section xml:id="abs1-2"><title type="main">MethodsA Dermatophagoides farinae cDNA library was constructed in lambda ZAPII vector and the library was immunoscreened with a monoclonal antibody 642. The cDNA insert was sub-cloned into M13 sequencing vector for single-stranded sequencing. The whole cDNA insert was expressed in pGEX-2T Escherichia coli expression system as a fusion protein with GST. The allergenicity of the recombinant peptides was tested by skin tests and IgE immunoassay. The IgE and IgG immunoassays were performed with sera from 20 mite-allergic patients.<section xml:id="abs1-3"><title type="main">ResultsThe cDNA clone Df642 was 2134 bp long, coding for a polypeptide of 711 amino acid residues. Protein sequence analysis and alignment confirmed that the deduced polypeptide is a mite paramyosin which is truncated slightly at the N- and C-terminuses. In vivo skin tests and in vitro IgE-binding study showed that 62% (13/21) and 50% (10/20) of the mite-sensitive asthmatic patients reacted positively with the recombinant Dermatophagoides farinae paramyosin, respectively.<section xml:id="abs1-4"><title type="main">ConclusionThe study indicated that 98-kDa mite paramyosin is an important allergen. 2002 Blackwell Publishing Journal Backfiles 1879-2005 |2002|||||||||| cDNA clone Sun, Y.-C. verfasserin aut Chao, P.-L. verfasserin aut Ng, H.-P. oth Hung, M.-W. oth Hsieh, K.-H. oth Liaw, S.-H. oth Chua, K.-Y. oth In Clinical & experimental allergy Oxford : Blackwell Science, 1989 29(1999), 12, Seite 0 Online-Ressource (DE-627)NLEJ243926391 (DE-600)2004469-0 1365-2222 nnns volume:29 year:1999 number:12 pages:0 http://dx.doi.org/10.1046/j.1365-2222.1999.00603.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 29 1999 12 0 |
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The IgE and IgG immunoassays were performed with sera from 20 mite-allergic patients.<section xml:id="abs1-3"><title type="main">ResultsThe cDNA clone Df642 was 2134 bp long, coding for a polypeptide of 711 amino acid residues. Protein sequence analysis and alignment confirmed that the deduced polypeptide is a mite paramyosin which is truncated slightly at the N- and C-terminuses. 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Sequence analysis and expression of a cDNA clone encoding a 98-kDa allergen in Dermatophagoides farinae |
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Sequence analysis and expression of a cDNA clone encoding a 98-kDa allergen in Dermatophagoides farinae |
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Tsai, L.-C. |
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Clinical & experimental allergy |
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Tsai, L.-C. Sun, Y.-C. Chao, P.-L. |
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Tsai, L.-C. |
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10.1046/j.1365-2222.1999.00603.x |
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sequence analysis and expression of a cdna clone encoding a 98-kda allergen in dermatophagoides farinae |
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Sequence analysis and expression of a cDNA clone encoding a 98-kDa allergen in Dermatophagoides farinae |
| abstract |
The important dust mite allergens identified to date are of molecular weights ranging from 14 to 60 kDa. Our previous protein study indicated that the 98-kDa native paramyosin in Dermatophagoides farinae mite showed IgE reactivity with 82% of the mite-sensitive asthmatic patients suggesting that it is a novel major mite allergen. This study described the isolation and characterization of the cDNA clone encoding the 98-kDa mite allergen.<section xml:id="abs1-2"><title type="main">MethodsA Dermatophagoides farinae cDNA library was constructed in lambda ZAPII vector and the library was immunoscreened with a monoclonal antibody 642. The cDNA insert was sub-cloned into M13 sequencing vector for single-stranded sequencing. The whole cDNA insert was expressed in pGEX-2T Escherichia coli expression system as a fusion protein with GST. The allergenicity of the recombinant peptides was tested by skin tests and IgE immunoassay. The IgE and IgG immunoassays were performed with sera from 20 mite-allergic patients.<section xml:id="abs1-3"><title type="main">ResultsThe cDNA clone Df642 was 2134 bp long, coding for a polypeptide of 711 amino acid residues. Protein sequence analysis and alignment confirmed that the deduced polypeptide is a mite paramyosin which is truncated slightly at the N- and C-terminuses. In vivo skin tests and in vitro IgE-binding study showed that 62% (13/21) and 50% (10/20) of the mite-sensitive asthmatic patients reacted positively with the recombinant Dermatophagoides farinae paramyosin, respectively.<section xml:id="abs1-4"><title type="main">ConclusionThe study indicated that 98-kDa mite paramyosin is an important allergen. |
| abstractGer |
The important dust mite allergens identified to date are of molecular weights ranging from 14 to 60 kDa. Our previous protein study indicated that the 98-kDa native paramyosin in Dermatophagoides farinae mite showed IgE reactivity with 82% of the mite-sensitive asthmatic patients suggesting that it is a novel major mite allergen. This study described the isolation and characterization of the cDNA clone encoding the 98-kDa mite allergen.<section xml:id="abs1-2"><title type="main">MethodsA Dermatophagoides farinae cDNA library was constructed in lambda ZAPII vector and the library was immunoscreened with a monoclonal antibody 642. The cDNA insert was sub-cloned into M13 sequencing vector for single-stranded sequencing. The whole cDNA insert was expressed in pGEX-2T Escherichia coli expression system as a fusion protein with GST. The allergenicity of the recombinant peptides was tested by skin tests and IgE immunoassay. The IgE and IgG immunoassays were performed with sera from 20 mite-allergic patients.<section xml:id="abs1-3"><title type="main">ResultsThe cDNA clone Df642 was 2134 bp long, coding for a polypeptide of 711 amino acid residues. Protein sequence analysis and alignment confirmed that the deduced polypeptide is a mite paramyosin which is truncated slightly at the N- and C-terminuses. In vivo skin tests and in vitro IgE-binding study showed that 62% (13/21) and 50% (10/20) of the mite-sensitive asthmatic patients reacted positively with the recombinant Dermatophagoides farinae paramyosin, respectively.<section xml:id="abs1-4"><title type="main">ConclusionThe study indicated that 98-kDa mite paramyosin is an important allergen. |
| abstract_unstemmed |
The important dust mite allergens identified to date are of molecular weights ranging from 14 to 60 kDa. Our previous protein study indicated that the 98-kDa native paramyosin in Dermatophagoides farinae mite showed IgE reactivity with 82% of the mite-sensitive asthmatic patients suggesting that it is a novel major mite allergen. This study described the isolation and characterization of the cDNA clone encoding the 98-kDa mite allergen.<section xml:id="abs1-2"><title type="main">MethodsA Dermatophagoides farinae cDNA library was constructed in lambda ZAPII vector and the library was immunoscreened with a monoclonal antibody 642. The cDNA insert was sub-cloned into M13 sequencing vector for single-stranded sequencing. The whole cDNA insert was expressed in pGEX-2T Escherichia coli expression system as a fusion protein with GST. The allergenicity of the recombinant peptides was tested by skin tests and IgE immunoassay. The IgE and IgG immunoassays were performed with sera from 20 mite-allergic patients.<section xml:id="abs1-3"><title type="main">ResultsThe cDNA clone Df642 was 2134 bp long, coding for a polypeptide of 711 amino acid residues. Protein sequence analysis and alignment confirmed that the deduced polypeptide is a mite paramyosin which is truncated slightly at the N- and C-terminuses. In vivo skin tests and in vitro IgE-binding study showed that 62% (13/21) and 50% (10/20) of the mite-sensitive asthmatic patients reacted positively with the recombinant Dermatophagoides farinae paramyosin, respectively.<section xml:id="abs1-4"><title type="main">ConclusionThe study indicated that 98-kDa mite paramyosin is an important allergen. |
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Sequence analysis and expression of a cDNA clone encoding a 98-kDa allergen in Dermatophagoides farinae |
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Sun, Y.-C. Chao, P.-L. Ng, H.-P. Hung, M.-W. Hsieh, K.-H. Liaw, S.-H. Chua, K.-Y. |
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Sun, Y.-C. Chao, P.-L. Ng, H.-P. Hung, M.-W. Hsieh, K.-H. Liaw, S.-H. Chua, K.-Y. |
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