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Purification and structural stability of the peach allergens Pru p 1 and Pru p 3
Pru p 1 (a Bet v 1 homologue) and Pru p 3 (a nonspecific lipid transfer protein; nsLTP) are major allergenic proteins in peach fruit, but differ in their abundance and stability. Pru p 1 has low abundance and is highly labile and was purified after expression as a recombinant protein in Escherichia...
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| Published in: | Molecular nutrition & food research 2008-11, Vol.52 (S2), p.S220-S229 |
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| container_title | Molecular nutrition & food research |
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| creator | Gaier, Sonja Marsh, Justin Oberhuber, Christina Rigby, Neil M Lovegrove, Alison Alessandri, Stefano Briza, Peter Radauer, Christian Zuidmeer, Laurian van Ree, Ronald Hemmer, Wolfgang Sancho, Ana I Mills, Clare Hoffmann-Sommergruber, Karin Shewry, Peter R |
| description | Pru p 1 (a Bet v 1 homologue) and Pru p 3 (a nonspecific lipid transfer protein; nsLTP) are major allergenic proteins in peach fruit, but differ in their abundance and stability. Pru p 1 has low abundance and is highly labile and was purified after expression as a recombinant protein in Escherichia coli. Pru p 3 is highly abundant in peach peel and was purified by conventional methods. The identities of the proteins were confirmed by sequence analysis and their masses determined by MS analysis. The purified proteins reacted with antisera against related allergens from other species: Pru p 1 with antiserum to Bet v 1 and Pru p 3 with antiserum to Mal d 3 (from apple). The presence of secondary and tertiary structure was demonstrated by circular dichroism (CD) and high field NMR spectroscopy. CD spectroscopy also showed that the two proteins differed in their stability at pH 3 and in their ability to refold after heating to 95°C. Thus, Pru p 1 was unfolded at pH 3 even at 25°C but was able to refold after heating to 95°C at pH 7.5. In contrast, Pru p 3 was unable to refold after heating under neutral conditions but readily refolded after heating at pH 3. |
| doi_str_mv | 10.1002/mnfr.200700274 |
| format | article |
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Pru p 1 has low abundance and is highly labile and was purified after expression as a recombinant protein in Escherichia coli. Pru p 3 is highly abundant in peach peel and was purified by conventional methods. The identities of the proteins were confirmed by sequence analysis and their masses determined by MS analysis. The purified proteins reacted with antisera against related allergens from other species: Pru p 1 with antiserum to Bet v 1 and Pru p 3 with antiserum to Mal d 3 (from apple). The presence of secondary and tertiary structure was demonstrated by circular dichroism (CD) and high field NMR spectroscopy. CD spectroscopy also showed that the two proteins differed in their stability at pH 3 and in their ability to refold after heating to 95°C. Thus, Pru p 1 was unfolded at pH 3 even at 25°C but was able to refold after heating to 95°C at pH 7.5. In contrast, Pru p 3 was unable to refold after heating under neutral conditions but readily refolded after heating at pH 3.</description><identifier>ISSN: 1613-4125</identifier><identifier>EISSN: 1613-4133</identifier><identifier>EISSN: 1521-3803</identifier><identifier>DOI: 10.1002/mnfr.200700274</identifier><identifier>PMID: 18384093</identifier><language>eng</language><publisher>Weinheim: Wiley-VCH Verlag</publisher><subject>Allergens - chemistry ; Allergens - immunology ; Allergens - isolation & purification ; Antigens, Plant ; Bet v 1 homologue ; Circular Dichroism ; Escherichia coli ; Food allergy ; Humans ; Hydrogen-Ion Concentration ; Lipid transfer protein ; Magnetic Resonance Spectroscopy ; Malus ; Peach ; Plant Proteins ; Protein Structure, Secondary ; Pru p 3 ; Prunus ; Recombinant Proteins - chemistry ; Recombinant Proteins - isolation & purification</subject><ispartof>Molecular nutrition & food research, 2008-11, Vol.52 (S2), p.S220-S229</ispartof><rights>Copyright © 2008 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5024-753720bc769c2695a062f0c6e08824450c049741f63200a13cc65b8b7f5e63e13</citedby><cites>FETCH-LOGICAL-c5024-753720bc769c2695a062f0c6e08824450c049741f63200a13cc65b8b7f5e63e13</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18384093$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Gaier, Sonja</creatorcontrib><creatorcontrib>Marsh, Justin</creatorcontrib><creatorcontrib>Oberhuber, Christina</creatorcontrib><creatorcontrib>Rigby, Neil M</creatorcontrib><creatorcontrib>Lovegrove, Alison</creatorcontrib><creatorcontrib>Alessandri, Stefano</creatorcontrib><creatorcontrib>Briza, Peter</creatorcontrib><creatorcontrib>Radauer, Christian</creatorcontrib><creatorcontrib>Zuidmeer, Laurian</creatorcontrib><creatorcontrib>van Ree, Ronald</creatorcontrib><creatorcontrib>Hemmer, Wolfgang</creatorcontrib><creatorcontrib>Sancho, Ana I</creatorcontrib><creatorcontrib>Mills, Clare</creatorcontrib><creatorcontrib>Hoffmann-Sommergruber, Karin</creatorcontrib><creatorcontrib>Shewry, Peter R</creatorcontrib><title>Purification and structural stability of the peach allergens Pru p 1 and Pru p 3</title><title>Molecular nutrition & food research</title><addtitle>Mol. Nutr. Food Res</addtitle><description>Pru p 1 (a Bet v 1 homologue) and Pru p 3 (a nonspecific lipid transfer protein; nsLTP) are major allergenic proteins in peach fruit, but differ in their abundance and stability. Pru p 1 has low abundance and is highly labile and was purified after expression as a recombinant protein in Escherichia coli. Pru p 3 is highly abundant in peach peel and was purified by conventional methods. The identities of the proteins were confirmed by sequence analysis and their masses determined by MS analysis. The purified proteins reacted with antisera against related allergens from other species: Pru p 1 with antiserum to Bet v 1 and Pru p 3 with antiserum to Mal d 3 (from apple). The presence of secondary and tertiary structure was demonstrated by circular dichroism (CD) and high field NMR spectroscopy. CD spectroscopy also showed that the two proteins differed in their stability at pH 3 and in their ability to refold after heating to 95°C. Thus, Pru p 1 was unfolded at pH 3 even at 25°C but was able to refold after heating to 95°C at pH 7.5. In contrast, Pru p 3 was unable to refold after heating under neutral conditions but readily refolded after heating at pH 3.</description><subject>Allergens - chemistry</subject><subject>Allergens - immunology</subject><subject>Allergens - isolation & purification</subject><subject>Antigens, Plant</subject><subject>Bet v 1 homologue</subject><subject>Circular Dichroism</subject><subject>Escherichia coli</subject><subject>Food allergy</subject><subject>Humans</subject><subject>Hydrogen-Ion Concentration</subject><subject>Lipid transfer protein</subject><subject>Magnetic Resonance Spectroscopy</subject><subject>Malus</subject><subject>Peach</subject><subject>Plant Proteins</subject><subject>Protein Structure, Secondary</subject><subject>Pru p 3</subject><subject>Prunus</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - isolation & purification</subject><issn>1613-4125</issn><issn>1613-4133</issn><issn>1521-3803</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><recordid>eNqFkE1P3DAURS1EBZSyZdl61V2mz37-SJYFFVqJTkcdEEvLMTa4ZJLBTtTOv29oRkN3rHwtnXuldwg5ZTBjAPzTqg1pxgH0-NFijxwxxbAQDHF_l7k8JG9z_gWAjAs8IIesxFJAhUdksRhSDNHZPnYtte0dzX0aXD8k24zR1rGJ_YZ2gfYPnq69dQ_UNo1P977NdJEGuqbsX2_K-I68CbbJ_mT7HpObiy_X51-Lqx-X384_XxVOAheFlqg51E6rynFVSQuKB3DKQ1lyISQ4EJUWLCgcr7MMnVOyLmsdpFfoGR6Tj9PuOnVPg8-9WcXsfNPY1ndDNqoqUTLGXwU5KCGFwBGcTaBLXc7JB7NOcWXTxjAwz7LNs2yzkz0W3m-Xh3rl717wrd0RqCbgd2z85pU5831-8fP_8WLqxtz7P7uuTY9GadTS3M4vzfx6eTuXyzOzHPkPEx9sZ-x9itncLDkwBCaVVBrwL7yHoU4</recordid><startdate>200811</startdate><enddate>200811</enddate><creator>Gaier, Sonja</creator><creator>Marsh, Justin</creator><creator>Oberhuber, Christina</creator><creator>Rigby, Neil M</creator><creator>Lovegrove, Alison</creator><creator>Alessandri, Stefano</creator><creator>Briza, Peter</creator><creator>Radauer, Christian</creator><creator>Zuidmeer, Laurian</creator><creator>van Ree, Ronald</creator><creator>Hemmer, Wolfgang</creator><creator>Sancho, Ana I</creator><creator>Mills, Clare</creator><creator>Hoffmann-Sommergruber, Karin</creator><creator>Shewry, Peter R</creator><general>Wiley-VCH Verlag</general><general>WILEY-VCH Verlag</general><general>WILEY‐VCH Verlag</general><scope>FBQ</scope><scope>BSCLL</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>7QL</scope><scope>7T5</scope><scope>C1K</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>200811</creationdate><title>Purification and structural stability of the peach allergens Pru p 1 and Pru p 3</title><author>Gaier, Sonja ; Marsh, Justin ; Oberhuber, Christina ; Rigby, Neil M ; Lovegrove, Alison ; Alessandri, Stefano ; Briza, Peter ; Radauer, Christian ; Zuidmeer, Laurian ; van Ree, Ronald ; Hemmer, Wolfgang ; Sancho, Ana I ; Mills, Clare ; Hoffmann-Sommergruber, Karin ; Shewry, Peter R</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5024-753720bc769c2695a062f0c6e08824450c049741f63200a13cc65b8b7f5e63e13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Allergens - chemistry</topic><topic>Allergens - immunology</topic><topic>Allergens - isolation & purification</topic><topic>Antigens, Plant</topic><topic>Bet v 1 homologue</topic><topic>Circular Dichroism</topic><topic>Escherichia coli</topic><topic>Food allergy</topic><topic>Humans</topic><topic>Hydrogen-Ion Concentration</topic><topic>Lipid transfer protein</topic><topic>Magnetic Resonance Spectroscopy</topic><topic>Malus</topic><topic>Peach</topic><topic>Plant Proteins</topic><topic>Protein Structure, Secondary</topic><topic>Pru p 3</topic><topic>Prunus</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - isolation & purification</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Gaier, Sonja</creatorcontrib><creatorcontrib>Marsh, Justin</creatorcontrib><creatorcontrib>Oberhuber, Christina</creatorcontrib><creatorcontrib>Rigby, Neil M</creatorcontrib><creatorcontrib>Lovegrove, Alison</creatorcontrib><creatorcontrib>Alessandri, Stefano</creatorcontrib><creatorcontrib>Briza, Peter</creatorcontrib><creatorcontrib>Radauer, Christian</creatorcontrib><creatorcontrib>Zuidmeer, Laurian</creatorcontrib><creatorcontrib>van Ree, Ronald</creatorcontrib><creatorcontrib>Hemmer, Wolfgang</creatorcontrib><creatorcontrib>Sancho, Ana I</creatorcontrib><creatorcontrib>Mills, Clare</creatorcontrib><creatorcontrib>Hoffmann-Sommergruber, Karin</creatorcontrib><creatorcontrib>Shewry, Peter R</creatorcontrib><collection>AGRIS</collection><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Immunology Abstracts</collection><collection>Environmental Sciences and Pollution Management</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Molecular nutrition & food research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gaier, Sonja</au><au>Marsh, Justin</au><au>Oberhuber, Christina</au><au>Rigby, Neil M</au><au>Lovegrove, Alison</au><au>Alessandri, Stefano</au><au>Briza, Peter</au><au>Radauer, Christian</au><au>Zuidmeer, Laurian</au><au>van Ree, Ronald</au><au>Hemmer, Wolfgang</au><au>Sancho, Ana I</au><au>Mills, Clare</au><au>Hoffmann-Sommergruber, Karin</au><au>Shewry, Peter R</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and structural stability of the peach allergens Pru p 1 and Pru p 3</atitle><jtitle>Molecular nutrition & food research</jtitle><addtitle>Mol. Nutr. Food Res</addtitle><date>2008-11</date><risdate>2008</risdate><volume>52</volume><issue>S2</issue><spage>S220</spage><epage>S229</epage><pages>S220-S229</pages><issn>1613-4125</issn><eissn>1613-4133</eissn><eissn>1521-3803</eissn><abstract>Pru p 1 (a Bet v 1 homologue) and Pru p 3 (a nonspecific lipid transfer protein; nsLTP) are major allergenic proteins in peach fruit, but differ in their abundance and stability. Pru p 1 has low abundance and is highly labile and was purified after expression as a recombinant protein in Escherichia coli. Pru p 3 is highly abundant in peach peel and was purified by conventional methods. The identities of the proteins were confirmed by sequence analysis and their masses determined by MS analysis. The purified proteins reacted with antisera against related allergens from other species: Pru p 1 with antiserum to Bet v 1 and Pru p 3 with antiserum to Mal d 3 (from apple). The presence of secondary and tertiary structure was demonstrated by circular dichroism (CD) and high field NMR spectroscopy. CD spectroscopy also showed that the two proteins differed in their stability at pH 3 and in their ability to refold after heating to 95°C. Thus, Pru p 1 was unfolded at pH 3 even at 25°C but was able to refold after heating to 95°C at pH 7.5. In contrast, Pru p 3 was unable to refold after heating under neutral conditions but readily refolded after heating at pH 3.</abstract><cop>Weinheim</cop><pub>Wiley-VCH Verlag</pub><pmid>18384093</pmid><doi>10.1002/mnfr.200700274</doi><tpages>10</tpages></addata></record> |
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| ispartof | Molecular nutrition & food research, 2008-11, Vol.52 (S2), p.S220-S229 |
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| source | Wiley-Blackwell Read & Publish Collection |
| subjects | Allergens - chemistry Allergens - immunology Allergens - isolation & purification Antigens, Plant Bet v 1 homologue Circular Dichroism Escherichia coli Food allergy Humans Hydrogen-Ion Concentration Lipid transfer protein Magnetic Resonance Spectroscopy Malus Peach Plant Proteins Protein Structure, Secondary Pru p 3 Prunus Recombinant Proteins - chemistry Recombinant Proteins - isolation & purification |
| title | Purification and structural stability of the peach allergens Pru p 1 and Pru p 3 |
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