A pollen-specific polygalacturonase from lily is related to major grass pollen allergens
A pollen-specific gene from lily ( Lilium longiflorum Thunb. cv. Snow Queen), designated LLP-PG, was characterized. Southern blots of lily genomic DNA indicated that LLP-PG is a member of a small gene family. A thorough sequence analysis revealed that the LLP-PG gene is interrupted by two introns an...
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| creator | Chiang, J.-Y. Balic, N. Hsu, S.-W. Yang, C.-Y. Ko, C.-W. Hsu, Y.-F. Swoboda, I. Wang, C.-S. |
| description | A pollen-specific gene from lily (
Lilium longiflorum Thunb. cv. Snow Queen), designated
LLP-PG, was characterized. Southern blots of lily genomic DNA indicated that
LLP-PG is a member of a small gene family. A thorough sequence analysis revealed that the
LLP-PG gene is interrupted by two introns and encodes a protein of 413 amino acids, with a calculated molecular mass of 44 kDa, and a p
I of 8.1. Evaluation of the hydropathy profile showed that the protein has a hydrophobic segment at the N-terminus, indicating the presence of a putative signal peptide. A sequence similarity search showed a significant homology of the encoded protein to pollen polygalacturonases (PGs) from various plant species and to an important group (group 13) of grass pollen allergens. The
LLP-PG transcript is pollen-specific and it accumulates only at the latest stage during pollen development, in the mature pollen. In contrast to other "late genes"
LLP-PG transcript can neither be induced by abscisic acid (ABA) nor by dehydration. Immunoblot analyses of pollen protein extracts from lily, timothy grass and tobacco with IgG antibodies directed against LLP-PG and against the timothy grass pollen allergen, Phl p 13, indicated that lily LLP-PG shares surface-exposed epitopes with pollen PGs from monocotyledonous and dicotyledonous plants. Enzyme-linked immunosorbent assay (ELISA) analyses and inhibition ELISA assays with patients' IgE demonstrated a very low IgE reactivity of lily rLLP-PG and a lack of cross-reactivity between rLLP-PG and the timothy grass pollen allergen, rPhl p 13. These data demonstrated that despite the significant sequence homology and the conserved surface-exposed epitopes LLP-PG represents a low-allergenic member of pollen PGs. |
| doi_str_mv | 10.1016/j.plaphy.2006.10.005 |
| format | Article |
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Lilium longiflorum Thunb. cv. Snow Queen), designated
LLP-PG, was characterized. Southern blots of lily genomic DNA indicated that
LLP-PG is a member of a small gene family. A thorough sequence analysis revealed that the
LLP-PG gene is interrupted by two introns and encodes a protein of 413 amino acids, with a calculated molecular mass of 44 kDa, and a p
I of 8.1. Evaluation of the hydropathy profile showed that the protein has a hydrophobic segment at the N-terminus, indicating the presence of a putative signal peptide. A sequence similarity search showed a significant homology of the encoded protein to pollen polygalacturonases (PGs) from various plant species and to an important group (group 13) of grass pollen allergens. The
LLP-PG transcript is pollen-specific and it accumulates only at the latest stage during pollen development, in the mature pollen. In contrast to other "late genes"
LLP-PG transcript can neither be induced by abscisic acid (ABA) nor by dehydration. Immunoblot analyses of pollen protein extracts from lily, timothy grass and tobacco with IgG antibodies directed against LLP-PG and against the timothy grass pollen allergen, Phl p 13, indicated that lily LLP-PG shares surface-exposed epitopes with pollen PGs from monocotyledonous and dicotyledonous plants. Enzyme-linked immunosorbent assay (ELISA) analyses and inhibition ELISA assays with patients' IgE demonstrated a very low IgE reactivity of lily rLLP-PG and a lack of cross-reactivity between rLLP-PG and the timothy grass pollen allergen, rPhl p 13. These data demonstrated that despite the significant sequence homology and the conserved surface-exposed epitopes LLP-PG represents a low-allergenic member of pollen PGs.</description><identifier>ISSN: 0981-9428</identifier><identifier>EISSN: 1873-2690</identifier><identifier>DOI: 10.1016/j.plaphy.2006.10.005</identifier><identifier>PMID: 17097294</identifier><identifier>CODEN: PPBIEX</identifier><language>eng</language><publisher>Paris: Elsevier Masson SAS</publisher><subject>Agronomy. Soil science and plant productions ; Allergen ; Allergens - biosynthesis ; Allergens - genetics ; Allergens - immunology ; Base Sequence ; Biological and medical sciences ; Cross Reactions - immunology ; Economic plant physiology ; Epitopes - biosynthesis ; Epitopes - genetics ; Epitopes - immunology ; Flowering, floral biology, reproduction patterns ; Fundamental and applied biological sciences. Psychology ; Gene expression ; Gene Expression Regulation, Plant - physiology ; Growth and development ; Humans ; Hypersensitivity - enzymology ; Hypersensitivity - immunology ; IgE cross-reactivity ; Immunoglobulin E - immunology ; Immunoglobulin G - immunology ; Lilium - enzymology ; Lilium - genetics ; Lilium - immunology ; Lilium longiflorum ; Molecular Sequence Data ; Nicotiana - enzymology ; Nicotiana - genetics ; Nicotiana - immunology ; Phleum - enzymology ; Phleum - genetics ; Phleum - immunology ; Plant Proteins - biosynthesis ; Plant Proteins - genetics ; Plant Proteins - immunology ; Pollen - enzymology ; Pollen - genetics ; Pollen - immunology ; Pollen-specific ; Polygalacturonase ; Polygalacturonase - biosynthesis ; Polygalacturonase - genetics ; Polygalacturonase - immunology ; Recombinant Proteins - biosynthesis ; Recombinant Proteins - genetics ; Recombinant Proteins - immunology ; Sequence Homology</subject><ispartof>Plant physiology and biochemistry, 2006-11, Vol.44 (11), p.743-751</ispartof><rights>2006 Elsevier Masson SAS</rights><rights>2007 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c390t-4ef970060f92a6800f3c7a412b88565ec54aeaac31ed333fe02c3443e2b841d93</citedby><cites>FETCH-LOGICAL-c390t-4ef970060f92a6800f3c7a412b88565ec54aeaac31ed333fe02c3443e2b841d93</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.plaphy.2006.10.005$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>315,782,786,3552,27931,27932,46002</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=18382037$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17097294$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Chiang, J.-Y.</creatorcontrib><creatorcontrib>Balic, N.</creatorcontrib><creatorcontrib>Hsu, S.-W.</creatorcontrib><creatorcontrib>Yang, C.-Y.</creatorcontrib><creatorcontrib>Ko, C.-W.</creatorcontrib><creatorcontrib>Hsu, Y.-F.</creatorcontrib><creatorcontrib>Swoboda, I.</creatorcontrib><creatorcontrib>Wang, C.-S.</creatorcontrib><title>A pollen-specific polygalacturonase from lily is related to major grass pollen allergens</title><title>Plant physiology and biochemistry</title><addtitle>Plant Physiol Biochem</addtitle><description>A pollen-specific gene from lily (
Lilium longiflorum Thunb. cv. Snow Queen), designated
LLP-PG, was characterized. Southern blots of lily genomic DNA indicated that
LLP-PG is a member of a small gene family. A thorough sequence analysis revealed that the
LLP-PG gene is interrupted by two introns and encodes a protein of 413 amino acids, with a calculated molecular mass of 44 kDa, and a p
I of 8.1. Evaluation of the hydropathy profile showed that the protein has a hydrophobic segment at the N-terminus, indicating the presence of a putative signal peptide. A sequence similarity search showed a significant homology of the encoded protein to pollen polygalacturonases (PGs) from various plant species and to an important group (group 13) of grass pollen allergens. The
LLP-PG transcript is pollen-specific and it accumulates only at the latest stage during pollen development, in the mature pollen. In contrast to other "late genes"
LLP-PG transcript can neither be induced by abscisic acid (ABA) nor by dehydration. Immunoblot analyses of pollen protein extracts from lily, timothy grass and tobacco with IgG antibodies directed against LLP-PG and against the timothy grass pollen allergen, Phl p 13, indicated that lily LLP-PG shares surface-exposed epitopes with pollen PGs from monocotyledonous and dicotyledonous plants. Enzyme-linked immunosorbent assay (ELISA) analyses and inhibition ELISA assays with patients' IgE demonstrated a very low IgE reactivity of lily rLLP-PG and a lack of cross-reactivity between rLLP-PG and the timothy grass pollen allergen, rPhl p 13. These data demonstrated that despite the significant sequence homology and the conserved surface-exposed epitopes LLP-PG represents a low-allergenic member of pollen PGs.</description><subject>Agronomy. Soil science and plant productions</subject><subject>Allergen</subject><subject>Allergens - biosynthesis</subject><subject>Allergens - genetics</subject><subject>Allergens - immunology</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Cross Reactions - immunology</subject><subject>Economic plant physiology</subject><subject>Epitopes - biosynthesis</subject><subject>Epitopes - genetics</subject><subject>Epitopes - immunology</subject><subject>Flowering, floral biology, reproduction patterns</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene expression</subject><subject>Gene Expression Regulation, Plant - physiology</subject><subject>Growth and development</subject><subject>Humans</subject><subject>Hypersensitivity - enzymology</subject><subject>Hypersensitivity - immunology</subject><subject>IgE cross-reactivity</subject><subject>Immunoglobulin E - immunology</subject><subject>Immunoglobulin G - immunology</subject><subject>Lilium - enzymology</subject><subject>Lilium - genetics</subject><subject>Lilium - immunology</subject><subject>Lilium longiflorum</subject><subject>Molecular Sequence Data</subject><subject>Nicotiana - enzymology</subject><subject>Nicotiana - genetics</subject><subject>Nicotiana - immunology</subject><subject>Phleum - enzymology</subject><subject>Phleum - genetics</subject><subject>Phleum - immunology</subject><subject>Plant Proteins - biosynthesis</subject><subject>Plant Proteins - genetics</subject><subject>Plant Proteins - immunology</subject><subject>Pollen - enzymology</subject><subject>Pollen - genetics</subject><subject>Pollen - immunology</subject><subject>Pollen-specific</subject><subject>Polygalacturonase</subject><subject>Polygalacturonase - biosynthesis</subject><subject>Polygalacturonase - genetics</subject><subject>Polygalacturonase - immunology</subject><subject>Recombinant Proteins - biosynthesis</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - immunology</subject><subject>Sequence Homology</subject><issn>0981-9428</issn><issn>1873-2690</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kM2KFDEQx4Mo7rj6BiJ90VuPlY_pTi7CsvgFC1704CnUpitjhnSnTXoW5m18Fp_MDNOwNy8pUvzqT9WPsdccthx49_6wnSPOv05bAdDV1hZg94RtuO5lKzoDT9kGjOatUUJfsRelHABAqF4-Z1e8B9MLozbs500zpxhpastMLvjgzv_THiO65ZjThIUan9PYxBBPTShNpogLDc2S_v4Z8ZBys89YyhrTYH3znqbykj3zGAu9Wus1-_Hp4_fbL-3dt89fb2_uWicNLK0ib_p6AXgjsNMAXroeFRf3Wu-6HbmdQkJ0ktMgpfQEwkmlJFVA8cHIa_bukjvn9PtIZbFjKI5ixInSsdhOi67rpaiguoAup1IyeTvnMGI-WQ72rNQe7EWpPSs9d6vSOvZmzT_ejzQ8Dq0OK_B2BbA4jD7j5EJ55LTUAmRfuQ8XjqqNh0DZFhdocjSETG6xQwr_3-QfOjuYIA</recordid><startdate>20061101</startdate><enddate>20061101</enddate><creator>Chiang, J.-Y.</creator><creator>Balic, N.</creator><creator>Hsu, S.-W.</creator><creator>Yang, C.-Y.</creator><creator>Ko, C.-W.</creator><creator>Hsu, Y.-F.</creator><creator>Swoboda, I.</creator><creator>Wang, C.-S.</creator><general>Elsevier Masson SAS</general><general>Elsevier</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20061101</creationdate><title>A pollen-specific polygalacturonase from lily is related to major grass pollen allergens</title><author>Chiang, J.-Y. ; Balic, N. ; Hsu, S.-W. ; Yang, C.-Y. ; Ko, C.-W. ; Hsu, Y.-F. ; Swoboda, I. ; Wang, C.-S.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c390t-4ef970060f92a6800f3c7a412b88565ec54aeaac31ed333fe02c3443e2b841d93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Agronomy. Soil science and plant productions</topic><topic>Allergen</topic><topic>Allergens - biosynthesis</topic><topic>Allergens - genetics</topic><topic>Allergens - immunology</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Cross Reactions - immunology</topic><topic>Economic plant physiology</topic><topic>Epitopes - biosynthesis</topic><topic>Epitopes - genetics</topic><topic>Epitopes - immunology</topic><topic>Flowering, floral biology, reproduction patterns</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene expression</topic><topic>Gene Expression Regulation, Plant - physiology</topic><topic>Growth and development</topic><topic>Humans</topic><topic>Hypersensitivity - enzymology</topic><topic>Hypersensitivity - immunology</topic><topic>IgE cross-reactivity</topic><topic>Immunoglobulin E - immunology</topic><topic>Immunoglobulin G - immunology</topic><topic>Lilium - enzymology</topic><topic>Lilium - genetics</topic><topic>Lilium - immunology</topic><topic>Lilium longiflorum</topic><topic>Molecular Sequence Data</topic><topic>Nicotiana - enzymology</topic><topic>Nicotiana - genetics</topic><topic>Nicotiana - immunology</topic><topic>Phleum - enzymology</topic><topic>Phleum - genetics</topic><topic>Phleum - immunology</topic><topic>Plant Proteins - biosynthesis</topic><topic>Plant Proteins - genetics</topic><topic>Plant Proteins - immunology</topic><topic>Pollen - enzymology</topic><topic>Pollen - genetics</topic><topic>Pollen - immunology</topic><topic>Pollen-specific</topic><topic>Polygalacturonase</topic><topic>Polygalacturonase - biosynthesis</topic><topic>Polygalacturonase - genetics</topic><topic>Polygalacturonase - immunology</topic><topic>Recombinant Proteins - biosynthesis</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - immunology</topic><topic>Sequence Homology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Chiang, J.-Y.</creatorcontrib><creatorcontrib>Balic, N.</creatorcontrib><creatorcontrib>Hsu, S.-W.</creatorcontrib><creatorcontrib>Yang, C.-Y.</creatorcontrib><creatorcontrib>Ko, C.-W.</creatorcontrib><creatorcontrib>Hsu, Y.-F.</creatorcontrib><creatorcontrib>Swoboda, I.</creatorcontrib><creatorcontrib>Wang, C.-S.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Plant physiology and biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Chiang, J.-Y.</au><au>Balic, N.</au><au>Hsu, S.-W.</au><au>Yang, C.-Y.</au><au>Ko, C.-W.</au><au>Hsu, Y.-F.</au><au>Swoboda, I.</au><au>Wang, C.-S.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A pollen-specific polygalacturonase from lily is related to major grass pollen allergens</atitle><jtitle>Plant physiology and biochemistry</jtitle><addtitle>Plant Physiol Biochem</addtitle><date>2006-11-01</date><risdate>2006</risdate><volume>44</volume><issue>11</issue><spage>743</spage><epage>751</epage><pages>743-751</pages><issn>0981-9428</issn><eissn>1873-2690</eissn><coden>PPBIEX</coden><abstract>A pollen-specific gene from lily (
Lilium longiflorum Thunb. cv. Snow Queen), designated
LLP-PG, was characterized. Southern blots of lily genomic DNA indicated that
LLP-PG is a member of a small gene family. A thorough sequence analysis revealed that the
LLP-PG gene is interrupted by two introns and encodes a protein of 413 amino acids, with a calculated molecular mass of 44 kDa, and a p
I of 8.1. Evaluation of the hydropathy profile showed that the protein has a hydrophobic segment at the N-terminus, indicating the presence of a putative signal peptide. A sequence similarity search showed a significant homology of the encoded protein to pollen polygalacturonases (PGs) from various plant species and to an important group (group 13) of grass pollen allergens. The
LLP-PG transcript is pollen-specific and it accumulates only at the latest stage during pollen development, in the mature pollen. In contrast to other "late genes"
LLP-PG transcript can neither be induced by abscisic acid (ABA) nor by dehydration. Immunoblot analyses of pollen protein extracts from lily, timothy grass and tobacco with IgG antibodies directed against LLP-PG and against the timothy grass pollen allergen, Phl p 13, indicated that lily LLP-PG shares surface-exposed epitopes with pollen PGs from monocotyledonous and dicotyledonous plants. Enzyme-linked immunosorbent assay (ELISA) analyses and inhibition ELISA assays with patients' IgE demonstrated a very low IgE reactivity of lily rLLP-PG and a lack of cross-reactivity between rLLP-PG and the timothy grass pollen allergen, rPhl p 13. These data demonstrated that despite the significant sequence homology and the conserved surface-exposed epitopes LLP-PG represents a low-allergenic member of pollen PGs.</abstract><cop>Paris</cop><pub>Elsevier Masson SAS</pub><pmid>17097294</pmid><doi>10.1016/j.plaphy.2006.10.005</doi><tpages>9</tpages></addata></record> |
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| ispartof | Plant physiology and biochemistry, 2006-11, Vol.44 (11), p.743-751 |
| issn | 0981-9428 1873-2690 |
| language | eng |
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| subjects | Agronomy. Soil science and plant productions Allergen Allergens - biosynthesis Allergens - genetics Allergens - immunology Base Sequence Biological and medical sciences Cross Reactions - immunology Economic plant physiology Epitopes - biosynthesis Epitopes - genetics Epitopes - immunology Flowering, floral biology, reproduction patterns Fundamental and applied biological sciences. Psychology Gene expression Gene Expression Regulation, Plant - physiology Growth and development Humans Hypersensitivity - enzymology Hypersensitivity - immunology IgE cross-reactivity Immunoglobulin E - immunology Immunoglobulin G - immunology Lilium - enzymology Lilium - genetics Lilium - immunology Lilium longiflorum Molecular Sequence Data Nicotiana - enzymology Nicotiana - genetics Nicotiana - immunology Phleum - enzymology Phleum - genetics Phleum - immunology Plant Proteins - biosynthesis Plant Proteins - genetics Plant Proteins - immunology Pollen - enzymology Pollen - genetics Pollen - immunology Pollen-specific Polygalacturonase Polygalacturonase - biosynthesis Polygalacturonase - genetics Polygalacturonase - immunology Recombinant Proteins - biosynthesis Recombinant Proteins - genetics Recombinant Proteins - immunology Sequence Homology |
| title | A pollen-specific polygalacturonase from lily is related to major grass pollen allergens |
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