The thermal stability and decapsidation mechanism of tymoviruses: A differential calorimetric study
The thermal stability of virions present in purified suspensions of three tymoviruses, turnip yellow mosaic virus (TYMV), belladonna mottle virus (VelMV) and eggplant mosaic virus (EMV) was investigated by microcalorimetry. Virions are less stable than natural empty shells at 4.5 ⩽ pH ⩽ 8.5. Polyval...
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| Veröffentlicht in: | Biochimie 1993, Vol.75 (8), p.667-674 |
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| container_title | Biochimie |
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| creator | Mutombo, K. Michels, B. Ott, H. Cerf, R. Witz, J. |
| description | The thermal stability of virions present in purified suspensions of three tymoviruses, turnip yellow mosaic virus (TYMV), belladonna mottle virus (VelMV) and eggplant mosaic virus (EMV) was investigated by microcalorimetry. Virions are less stable than natural empty shells at 4.5 ⩽ pH ⩽ 8.5. Polyvalent cations present in TYMV stabilize the virions at pH ⩽ 5.0 only. Virions decapsidate in three steps: i) the release of the viral RNA, probably through a hole in the capsid; ii) the dissociation of the artificial empty shells thus formed; and iii) the denaturation of the dissociated components. An exothermic process accompanies the first step. Structural implications are discussed. |
| doi_str_mv | 10.1016/0300-9084(93)90097-C |
| format | Article |
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Virions are less stable than natural empty shells at 4.5 ⩽ pH ⩽ 8.5. Polyvalent cations present in TYMV stabilize the virions at pH ⩽ 5.0 only. Virions decapsidate in three steps: i) the release of the viral RNA, probably through a hole in the capsid; ii) the dissociation of the artificial empty shells thus formed; and iii) the denaturation of the dissociated components. An exothermic process accompanies the first step. Structural implications are discussed.</description><identifier>ISSN: 0300-9084</identifier><identifier>EISSN: 1638-6183</identifier><identifier>DOI: 10.1016/0300-9084(93)90097-C</identifier><identifier>PMID: 8286439</identifier><language>eng</language><publisher>France: Elsevier Masson SAS</publisher><subject>ARN ; CALORIMETRIA ; CALORIMETRIE ; CALORIMETRY ; Calorimetry, Differential Scanning ; Capsid - chemistry ; Capsid - metabolism ; decapsidation ; Hot Temperature ; Hydrogen-Ion Concentration ; microcalorimetry ; Microscopy, Electron ; Plants ; PROPIEDADES TERMICAS ; PROPRIETE THERMIQUE ; RNA ; RNA, Viral - chemistry ; THERMAL PROPERTIES ; turnip yellow mosaic virus ; TYMOVIRUS ; Tymovirus - chemistry ; Tymovirus - metabolism ; Tymovirus - ultrastructure ; TYMOVIRUSES ; Virion - chemistry</subject><ispartof>Biochimie, 1993, Vol.75 (8), p.667-674</ispartof><rights>1993</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c376t-bec2424fce7d9bd79ac4029ae499f873d3fa30d0b098fe0e56c4f6e467a9d12f3</citedby><cites>FETCH-LOGICAL-c376t-bec2424fce7d9bd79ac4029ae499f873d3fa30d0b098fe0e56c4f6e467a9d12f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0300-9084(93)90097-C$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,4024,27923,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8286439$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Mutombo, K.</creatorcontrib><creatorcontrib>Michels, B.</creatorcontrib><creatorcontrib>Ott, H.</creatorcontrib><creatorcontrib>Cerf, R.</creatorcontrib><creatorcontrib>Witz, J.</creatorcontrib><title>The thermal stability and decapsidation mechanism of tymoviruses: A differential calorimetric study</title><title>Biochimie</title><addtitle>Biochimie</addtitle><description>The thermal stability of virions present in purified suspensions of three tymoviruses, turnip yellow mosaic virus (TYMV), belladonna mottle virus (VelMV) and eggplant mosaic virus (EMV) was investigated by microcalorimetry. Virions are less stable than natural empty shells at 4.5 ⩽ pH ⩽ 8.5. Polyvalent cations present in TYMV stabilize the virions at pH ⩽ 5.0 only. Virions decapsidate in three steps: i) the release of the viral RNA, probably through a hole in the capsid; ii) the dissociation of the artificial empty shells thus formed; and iii) the denaturation of the dissociated components. An exothermic process accompanies the first step. Structural implications are discussed.</description><subject>ARN</subject><subject>CALORIMETRIA</subject><subject>CALORIMETRIE</subject><subject>CALORIMETRY</subject><subject>Calorimetry, Differential Scanning</subject><subject>Capsid - chemistry</subject><subject>Capsid - metabolism</subject><subject>decapsidation</subject><subject>Hot Temperature</subject><subject>Hydrogen-Ion Concentration</subject><subject>microcalorimetry</subject><subject>Microscopy, Electron</subject><subject>Plants</subject><subject>PROPIEDADES TERMICAS</subject><subject>PROPRIETE THERMIQUE</subject><subject>RNA</subject><subject>RNA, Viral - chemistry</subject><subject>THERMAL PROPERTIES</subject><subject>turnip yellow mosaic virus</subject><subject>TYMOVIRUS</subject><subject>Tymovirus - chemistry</subject><subject>Tymovirus - metabolism</subject><subject>Tymovirus - ultrastructure</subject><subject>TYMOVIRUSES</subject><subject>Virion - chemistry</subject><issn>0300-9084</issn><issn>1638-6183</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE9rFDEYxoModW39AqKQk9jDtO9MssnEg1CWVgsFQeo5ZJI3bmRmsiaZwn57s-7So6f38Px5H36EvG_hqoVWXAMDaBT0_JNilwpAyWbzgqxawfpGtD17SVbPltfkTc6_AWANnTojZ33XC87UitjHLdKyxTSZkeZihjCGsqdmdtShNbscnCkhznRCuzVzyBONnpb9FJ9CWjLmz_SGuuA9JpxLqCXWjDGFCUsKtjYubn9BXnkzZnx7uufk593t4-Zb8_D96_3m5qGxTIrSDGg73nFvUTo1OKmM5XWtQa6U7yVzzBsGDgZQvUfAtbDcC-RCGuXazrNz8vHYu0vxz4K56Clki-NoZoxL1lK0QnIpq5EfjTbFnBN6vauLTdrrFvSBrT6A0wdwWjH9j63e1NiHU_8yTOieQyeYVX931L2J2vxKIeu7H2oNnPfrKn45ilgJPAVMOtuAs0UXEtqiXQz___4X8LSTGg</recordid><startdate>1993</startdate><enddate>1993</enddate><creator>Mutombo, K.</creator><creator>Michels, B.</creator><creator>Ott, H.</creator><creator>Cerf, R.</creator><creator>Witz, J.</creator><general>Elsevier Masson SAS</general><scope>FBQ</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>1993</creationdate><title>The thermal stability and decapsidation mechanism of tymoviruses: A differential calorimetric study</title><author>Mutombo, K. ; Michels, B. ; Ott, H. ; Cerf, R. ; Witz, J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c376t-bec2424fce7d9bd79ac4029ae499f873d3fa30d0b098fe0e56c4f6e467a9d12f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>ARN</topic><topic>CALORIMETRIA</topic><topic>CALORIMETRIE</topic><topic>CALORIMETRY</topic><topic>Calorimetry, Differential Scanning</topic><topic>Capsid - chemistry</topic><topic>Capsid - metabolism</topic><topic>decapsidation</topic><topic>Hot Temperature</topic><topic>Hydrogen-Ion Concentration</topic><topic>microcalorimetry</topic><topic>Microscopy, Electron</topic><topic>Plants</topic><topic>PROPIEDADES TERMICAS</topic><topic>PROPRIETE THERMIQUE</topic><topic>RNA</topic><topic>RNA, Viral - chemistry</topic><topic>THERMAL PROPERTIES</topic><topic>turnip yellow mosaic virus</topic><topic>TYMOVIRUS</topic><topic>Tymovirus - chemistry</topic><topic>Tymovirus - metabolism</topic><topic>Tymovirus - ultrastructure</topic><topic>TYMOVIRUSES</topic><topic>Virion - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Mutombo, K.</creatorcontrib><creatorcontrib>Michels, B.</creatorcontrib><creatorcontrib>Ott, H.</creatorcontrib><creatorcontrib>Cerf, R.</creatorcontrib><creatorcontrib>Witz, J.</creatorcontrib><collection>AGRIS</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>Biochimie</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Mutombo, K.</au><au>Michels, B.</au><au>Ott, H.</au><au>Cerf, R.</au><au>Witz, J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The thermal stability and decapsidation mechanism of tymoviruses: A differential calorimetric study</atitle><jtitle>Biochimie</jtitle><addtitle>Biochimie</addtitle><date>1993</date><risdate>1993</risdate><volume>75</volume><issue>8</issue><spage>667</spage><epage>674</epage><pages>667-674</pages><issn>0300-9084</issn><eissn>1638-6183</eissn><abstract>The thermal stability of virions present in purified suspensions of three tymoviruses, turnip yellow mosaic virus (TYMV), belladonna mottle virus (VelMV) and eggplant mosaic virus (EMV) was investigated by microcalorimetry. Virions are less stable than natural empty shells at 4.5 ⩽ pH ⩽ 8.5. Polyvalent cations present in TYMV stabilize the virions at pH ⩽ 5.0 only. Virions decapsidate in three steps: i) the release of the viral RNA, probably through a hole in the capsid; ii) the dissociation of the artificial empty shells thus formed; and iii) the denaturation of the dissociated components. An exothermic process accompanies the first step. Structural implications are discussed.</abstract><cop>France</cop><pub>Elsevier Masson SAS</pub><pmid>8286439</pmid><doi>10.1016/0300-9084(93)90097-C</doi><tpages>8</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0300-9084 |
| ispartof | Biochimie, 1993, Vol.75 (8), p.667-674 |
| issn | 0300-9084 1638-6183 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_76167477 |
| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | ARN CALORIMETRIA CALORIMETRIE CALORIMETRY Calorimetry, Differential Scanning Capsid - chemistry Capsid - metabolism decapsidation Hot Temperature Hydrogen-Ion Concentration microcalorimetry Microscopy, Electron Plants PROPIEDADES TERMICAS PROPRIETE THERMIQUE RNA RNA, Viral - chemistry THERMAL PROPERTIES turnip yellow mosaic virus TYMOVIRUS Tymovirus - chemistry Tymovirus - metabolism Tymovirus - ultrastructure TYMOVIRUSES Virion - chemistry |
| title | The thermal stability and decapsidation mechanism of tymoviruses: A differential calorimetric study |
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