Major allergen Phl p Vb in timothy grass is a novel pollen RNase
A cDNA coding for the major group V allergen Phl p Vb was isolated from a timothy grass pollen cDNA library by immunoscreening with a specific monoclonal antibody. It was discovered for the first time that the recombinant Phl p Vb pollen allergen after expression and purification has ribonuclease ac...
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| Veröffentlicht in: | FEBS letters 1995-04, Vol.363 (1), p.6-12 |
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| creator | Bufe, A. Schramm, G. Keown, M.B. Schlaak, M. Becker, W.-M. |
| description | A cDNA coding for the major group V allergen
Phl p Vb was isolated from a timothy grass pollen cDNA library by immunoscreening with a specific monoclonal antibody. It was discovered for the first time that the recombinant
Phl p Vb pollen allergen after expression and purification has ribonuclease activity. High homology of
Phl p Vb to other group V allergens in grass pollen indicates similar function. By RNase activity gel of natural pollen extract of timothy grass and consecutive Western blot analysis of the excised proteins, the RNase active bands were shown to be group V allergens. Additionally it was demonstrated that an homologous protein to
Phl p Vb in the mother plant could be induced by salicylic acid. This indicates that group Vb allergens may be involved in host-pathogen interactions because in pollen they are quickly exported RNases and in the mother plant they depend on a hormone which is related to expression of plant resistance genes. |
| doi_str_mv | 10.1016/0014-5793(95)00259-C |
| format | Article |
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Phl p Vb was isolated from a timothy grass pollen cDNA library by immunoscreening with a specific monoclonal antibody. It was discovered for the first time that the recombinant
Phl p Vb pollen allergen after expression and purification has ribonuclease activity. High homology of
Phl p Vb to other group V allergens in grass pollen indicates similar function. By RNase activity gel of natural pollen extract of timothy grass and consecutive Western blot analysis of the excised proteins, the RNase active bands were shown to be group V allergens. Additionally it was demonstrated that an homologous protein to
Phl p Vb in the mother plant could be induced by salicylic acid. This indicates that group Vb allergens may be involved in host-pathogen interactions because in pollen they are quickly exported RNases and in the mother plant they depend on a hormone which is related to expression of plant resistance genes.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/0014-5793(95)00259-C</identifier><identifier>PMID: 7729555</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Allergens ; Amino Acid Sequence ; Antibodies, Monoclonal ; Base Sequence ; Blotting, Western ; cDNA ; Chromatography, High Pressure Liquid ; DNA, Complementary - chemistry ; DNA, Complementary - isolation & purification ; Electrophoresis, Polyacrylamide Gel ; Major allergen ; Molecular Sequence Data ; Plant Proteins - chemistry ; Plant Proteins - genetics ; Plant Proteins - metabolism ; Pollen ; Recombinant Proteins - chemistry ; Recombinant Proteins - metabolism ; Ribonucleases - metabolism ; RNA, Messenger - metabolism ; RNase activity ; Salicylates - pharmacology ; Salicylic Acid ; Sequence Homology ; Timothy grass pollen</subject><ispartof>FEBS letters, 1995-04, Vol.363 (1), p.6-12</ispartof><rights>1995</rights><rights>FEBS Letters 363 (1995) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c420C-5cc1e56cbcda70279c8be9fa9d15bede70cef07ab2dab334672734f2b1d1a58b3</citedby><cites>FETCH-LOGICAL-c420C-5cc1e56cbcda70279c8be9fa9d15bede70cef07ab2dab334672734f2b1d1a58b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0014-5793(95)00259-C$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7729555$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bufe, A.</creatorcontrib><creatorcontrib>Schramm, G.</creatorcontrib><creatorcontrib>Keown, M.B.</creatorcontrib><creatorcontrib>Schlaak, M.</creatorcontrib><creatorcontrib>Becker, W.-M.</creatorcontrib><title>Major allergen Phl p Vb in timothy grass is a novel pollen RNase</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>A cDNA coding for the major group V allergen
Phl p Vb was isolated from a timothy grass pollen cDNA library by immunoscreening with a specific monoclonal antibody. It was discovered for the first time that the recombinant
Phl p Vb pollen allergen after expression and purification has ribonuclease activity. High homology of
Phl p Vb to other group V allergens in grass pollen indicates similar function. By RNase activity gel of natural pollen extract of timothy grass and consecutive Western blot analysis of the excised proteins, the RNase active bands were shown to be group V allergens. Additionally it was demonstrated that an homologous protein to
Phl p Vb in the mother plant could be induced by salicylic acid. This indicates that group Vb allergens may be involved in host-pathogen interactions because in pollen they are quickly exported RNases and in the mother plant they depend on a hormone which is related to expression of plant resistance genes.</description><subject>Allergens</subject><subject>Amino Acid Sequence</subject><subject>Antibodies, Monoclonal</subject><subject>Base Sequence</subject><subject>Blotting, Western</subject><subject>cDNA</subject><subject>Chromatography, High Pressure Liquid</subject><subject>DNA, Complementary - chemistry</subject><subject>DNA, Complementary - isolation & purification</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Major allergen</subject><subject>Molecular Sequence Data</subject><subject>Plant Proteins - chemistry</subject><subject>Plant Proteins - genetics</subject><subject>Plant Proteins - metabolism</subject><subject>Pollen</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - metabolism</subject><subject>Ribonucleases - metabolism</subject><subject>RNA, Messenger - metabolism</subject><subject>RNase activity</subject><subject>Salicylates - pharmacology</subject><subject>Salicylic Acid</subject><subject>Sequence Homology</subject><subject>Timothy grass pollen</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkE1LxDAQhoMouq7-A4WcRA_VpG02zUXU4qrgF6JeQ5JONdKPNemu7L83tYtH8TTMvO-8mTwI7VFyTAmdnBBC04hxkRwKdkRIzESUr6ERzXgSJekkW0ejX8sW2vb-g4Q-o2ITbXIeC8bYCJ3dqY_WYVVV4N6gwY_vFZ7hV41tgztbt937Er855T22HivctAsIhjbYG_x0rzzsoI1SVR52V3WMXqaXz_l1dPtwdZOf30YmjUkeMWMosInRplCcxFyYTIMolSgo01AAJwZKwpWOC6WTcD6PeZKWsaYFVSzTyRgdDLkz137OwXeytt5AVakG2rmX4UdJkqUsGNPBaFzrvYNSzpytlVtKSmQPTvZUZE9FCiZ_wMk8rO2v8ue6huJ3aUUq6NNB_7IVLP-VKaeXF3Ev9HPBfqb9Q6dDEARaCwtOemOhMVBYB6aTRWv_vvQb8DCPkQ</recordid><startdate>19950417</startdate><enddate>19950417</enddate><creator>Bufe, A.</creator><creator>Schramm, G.</creator><creator>Keown, M.B.</creator><creator>Schlaak, M.</creator><creator>Becker, W.-M.</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</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>19950417</creationdate><title>Major allergen Phl p Vb in timothy grass is a novel pollen RNase</title><author>Bufe, A. ; Schramm, G. ; Keown, M.B. ; Schlaak, M. ; Becker, W.-M.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c420C-5cc1e56cbcda70279c8be9fa9d15bede70cef07ab2dab334672734f2b1d1a58b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>Allergens</topic><topic>Amino Acid Sequence</topic><topic>Antibodies, Monoclonal</topic><topic>Base Sequence</topic><topic>Blotting, Western</topic><topic>cDNA</topic><topic>Chromatography, High Pressure Liquid</topic><topic>DNA, Complementary - chemistry</topic><topic>DNA, Complementary - isolation & purification</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Major allergen</topic><topic>Molecular Sequence Data</topic><topic>Plant Proteins - chemistry</topic><topic>Plant Proteins - genetics</topic><topic>Plant Proteins - metabolism</topic><topic>Pollen</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - metabolism</topic><topic>Ribonucleases - metabolism</topic><topic>RNA, Messenger - metabolism</topic><topic>RNase activity</topic><topic>Salicylates - pharmacology</topic><topic>Salicylic Acid</topic><topic>Sequence Homology</topic><topic>Timothy grass pollen</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bufe, A.</creatorcontrib><creatorcontrib>Schramm, G.</creatorcontrib><creatorcontrib>Keown, M.B.</creatorcontrib><creatorcontrib>Schlaak, M.</creatorcontrib><creatorcontrib>Becker, W.-M.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</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>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bufe, A.</au><au>Schramm, G.</au><au>Keown, M.B.</au><au>Schlaak, M.</au><au>Becker, W.-M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Major allergen Phl p Vb in timothy grass is a novel pollen RNase</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1995-04-17</date><risdate>1995</risdate><volume>363</volume><issue>1</issue><spage>6</spage><epage>12</epage><pages>6-12</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>A cDNA coding for the major group V allergen
Phl p Vb was isolated from a timothy grass pollen cDNA library by immunoscreening with a specific monoclonal antibody. It was discovered for the first time that the recombinant
Phl p Vb pollen allergen after expression and purification has ribonuclease activity. High homology of
Phl p Vb to other group V allergens in grass pollen indicates similar function. By RNase activity gel of natural pollen extract of timothy grass and consecutive Western blot analysis of the excised proteins, the RNase active bands were shown to be group V allergens. Additionally it was demonstrated that an homologous protein to
Phl p Vb in the mother plant could be induced by salicylic acid. This indicates that group Vb allergens may be involved in host-pathogen interactions because in pollen they are quickly exported RNases and in the mother plant they depend on a hormone which is related to expression of plant resistance genes.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>7729555</pmid><doi>10.1016/0014-5793(95)00259-C</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
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| ispartof | FEBS letters, 1995-04, Vol.363 (1), p.6-12 |
| issn | 0014-5793 1873-3468 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Allergens Amino Acid Sequence Antibodies, Monoclonal Base Sequence Blotting, Western cDNA Chromatography, High Pressure Liquid DNA, Complementary - chemistry DNA, Complementary - isolation & purification Electrophoresis, Polyacrylamide Gel Major allergen Molecular Sequence Data Plant Proteins - chemistry Plant Proteins - genetics Plant Proteins - metabolism Pollen Recombinant Proteins - chemistry Recombinant Proteins - metabolism Ribonucleases - metabolism RNA, Messenger - metabolism RNase activity Salicylates - pharmacology Salicylic Acid Sequence Homology Timothy grass pollen |
| title | Major allergen Phl p Vb in timothy grass is a novel pollen RNase |
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