Loading…

Interaction between the tobacco mosaic virus movement protein and host cell pectin methylesterases is required for viral cell-to-cell movement

Virus‐encoded movement protein (MP) mediates cell‐to‐cell spread of tobacco mosaic virus (TMV) through plant intercellular connections, the plasmodesmata. The molecular pathway by which TMV MP interacts with the host cell is largely unknown. To understand this process better, a cell wall‐associated...

Full description

Saved in:
Bibliographic Details
Published in:The EMBO journal 2000-03, Vol.19 (5), p.913-920
Main Authors: Chen, Min-Huei, Sheng, Jinsong, Hind, Geoffrey, Handa, Avtar K., Citovsky, Vitaly
Format: Article
Language:English
Subjects:
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by cdi_FETCH-LOGICAL-c6354-e190b04ed8cf6f5d7768c9e6c14813ba4dd25a5e9f92036726289cc56c64cd503
cites cdi_FETCH-LOGICAL-c6354-e190b04ed8cf6f5d7768c9e6c14813ba4dd25a5e9f92036726289cc56c64cd503
container_end_page 920
container_issue 5
container_start_page 913
container_title The EMBO journal
container_volume 19
creator Chen, Min-Huei
Sheng, Jinsong
Hind, Geoffrey
Handa, Avtar K.
Citovsky, Vitaly
description Virus‐encoded movement protein (MP) mediates cell‐to‐cell spread of tobacco mosaic virus (TMV) through plant intercellular connections, the plasmodesmata. The molecular pathway by which TMV MP interacts with the host cell is largely unknown. To understand this process better, a cell wall‐associated protein that specifically binds the viral MP was purified from tobacco leaf cell walls and identified as pectin methylesterase (PME). In addition to TMV MP, PME is recognized by MPs of turnip vein clearing virus (TVCV) and cauliflower mosaic virus (CaMV). The use of amino acid deletion mutants of TMV MP showed that its domain was necessary and sufficient for association with PME. Deletion of the PME‐binding region resulted in inactivation of TMV cell‐to‐cell movement.
doi_str_mv 10.1093/emboj/19.5.913
format article
fullrecord <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_305631</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>373526841</sourcerecordid><originalsourceid>FETCH-LOGICAL-c6354-e190b04ed8cf6f5d7768c9e6c14813ba4dd25a5e9f92036726289cc56c64cd503</originalsourceid><addsrcrecordid>eNqFkcFv0zAUxiMEYmNw5YgsDtzS2nFsxwcOdBplaMAFBDfLcV5Wl8Tu7KSj_wR_M24zpoKEOFlP_n7f-56-LHtO8IxgSefQ1349J3LGZpLQB9kpKTnOCyzYw-wUF5zkJankSfYkxjXGmFWCPM5OCOaykpSeZj8v3QBBm8F6h2oYbgEcGlaABl9rYzzqfdTWoK0NY0zDFnpwA9oEP4B1SLsGrXwckIGuQxtIPg71MKx2HcS9cYSIbEQBbkYboEGtD3sv3R2IfPD5gfxt_DR71OouwrO79yz78vbi8_m7_OrT8vL8zVVuOGVlDkTiGpfQVKblLWuE4JWRwA0pK0JrXTZNwTQD2coCUy4KXlTSGMYNL03DMD3LXk--m7HuoTFpdcqkNsH2OuyU11b9-ePsSl37raKYcUoS_-qOD_5mTKeq3sb9JdqBH6MiglFGJUvCl38J134MLt2miGQFF7wsk2g2iUzwMQZo74MQrPY1q0PNiVBMpZoT8OI4_pF86jUJxCS4tR3s_mOnLj4s3gsmiwLvs8wnMibIXUM4CvyvMPlE2NT4j_tdOnxXXFDB1NePSyW-LZZFWS2UpL8AsGXYqA</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>195267644</pqid></control><display><type>article</type><title>Interaction between the tobacco mosaic virus movement protein and host cell pectin methylesterases is required for viral cell-to-cell movement</title><source>PubMed Central</source><creator>Chen, Min-Huei ; Sheng, Jinsong ; Hind, Geoffrey ; Handa, Avtar K. ; Citovsky, Vitaly</creator><creatorcontrib>Chen, Min-Huei ; Sheng, Jinsong ; Hind, Geoffrey ; Handa, Avtar K. ; Citovsky, Vitaly</creatorcontrib><description>Virus‐encoded movement protein (MP) mediates cell‐to‐cell spread of tobacco mosaic virus (TMV) through plant intercellular connections, the plasmodesmata. The molecular pathway by which TMV MP interacts with the host cell is largely unknown. To understand this process better, a cell wall‐associated protein that specifically binds the viral MP was purified from tobacco leaf cell walls and identified as pectin methylesterase (PME). In addition to TMV MP, PME is recognized by MPs of turnip vein clearing virus (TVCV) and cauliflower mosaic virus (CaMV). The use of amino acid deletion mutants of TMV MP showed that its domain was necessary and sufficient for association with PME. Deletion of the PME‐binding region resulted in inactivation of TMV cell‐to‐cell movement.</description><identifier>ISSN: 0261-4189</identifier><identifier>EISSN: 1460-2075</identifier><identifier>DOI: 10.1093/emboj/19.5.913</identifier><identifier>PMID: 10698933</identifier><identifier>CODEN: EMJODG</identifier><language>eng</language><publisher>Chichester, UK: John Wiley &amp; Sons, Ltd</publisher><subject>Amino Acid Sequence ; Amino acids ; Binding Sites ; Carboxylic Ester Hydrolases - metabolism ; Cauliflower mosaic virus ; Inactivation ; Molecular Sequence Data ; movement protein ; movement proteins ; MP protein ; Nicotiana - metabolism ; Nicotiana - virology ; Nicotiana tabacum ; pectin methylesterase ; pectin methylesterases ; Plant Viral Movement Proteins ; plant viruses ; Plants, Toxic ; plasmodesmata ; Protein Binding ; Sequence Alignment ; Tobacco ; Tobacco mosaic virus ; Tobacco Mosaic Virus - physiology ; Turnip vein-clearing virus ; Viral Proteins - metabolism ; Virus Replication</subject><ispartof>The EMBO journal, 2000-03, Vol.19 (5), p.913-920</ispartof><rights>European Molecular Biology Organization 2000</rights><rights>Copyright © 2000 European Molecular Biology Organization</rights><rights>Copyright Oxford University Press(England) Mar 01, 2000</rights><rights>Copyright © 2000 European Molecular Biology Organization 2000</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c6354-e190b04ed8cf6f5d7768c9e6c14813ba4dd25a5e9f92036726289cc56c64cd503</citedby><cites>FETCH-LOGICAL-c6354-e190b04ed8cf6f5d7768c9e6c14813ba4dd25a5e9f92036726289cc56c64cd503</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC305631/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC305631/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,724,777,781,882,27905,27906,53772,53774</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10698933$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Chen, Min-Huei</creatorcontrib><creatorcontrib>Sheng, Jinsong</creatorcontrib><creatorcontrib>Hind, Geoffrey</creatorcontrib><creatorcontrib>Handa, Avtar K.</creatorcontrib><creatorcontrib>Citovsky, Vitaly</creatorcontrib><title>Interaction between the tobacco mosaic virus movement protein and host cell pectin methylesterases is required for viral cell-to-cell movement</title><title>The EMBO journal</title><addtitle>EMBO J</addtitle><addtitle>EMBO J</addtitle><description>Virus‐encoded movement protein (MP) mediates cell‐to‐cell spread of tobacco mosaic virus (TMV) through plant intercellular connections, the plasmodesmata. The molecular pathway by which TMV MP interacts with the host cell is largely unknown. To understand this process better, a cell wall‐associated protein that specifically binds the viral MP was purified from tobacco leaf cell walls and identified as pectin methylesterase (PME). In addition to TMV MP, PME is recognized by MPs of turnip vein clearing virus (TVCV) and cauliflower mosaic virus (CaMV). The use of amino acid deletion mutants of TMV MP showed that its domain was necessary and sufficient for association with PME. Deletion of the PME‐binding region resulted in inactivation of TMV cell‐to‐cell movement.</description><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Binding Sites</subject><subject>Carboxylic Ester Hydrolases - metabolism</subject><subject>Cauliflower mosaic virus</subject><subject>Inactivation</subject><subject>Molecular Sequence Data</subject><subject>movement protein</subject><subject>movement proteins</subject><subject>MP protein</subject><subject>Nicotiana - metabolism</subject><subject>Nicotiana - virology</subject><subject>Nicotiana tabacum</subject><subject>pectin methylesterase</subject><subject>pectin methylesterases</subject><subject>Plant Viral Movement Proteins</subject><subject>plant viruses</subject><subject>Plants, Toxic</subject><subject>plasmodesmata</subject><subject>Protein Binding</subject><subject>Sequence Alignment</subject><subject>Tobacco</subject><subject>Tobacco mosaic virus</subject><subject>Tobacco Mosaic Virus - physiology</subject><subject>Turnip vein-clearing virus</subject><subject>Viral Proteins - metabolism</subject><subject>Virus Replication</subject><issn>0261-4189</issn><issn>1460-2075</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><recordid>eNqFkcFv0zAUxiMEYmNw5YgsDtzS2nFsxwcOdBplaMAFBDfLcV5Wl8Tu7KSj_wR_M24zpoKEOFlP_n7f-56-LHtO8IxgSefQ1349J3LGZpLQB9kpKTnOCyzYw-wUF5zkJankSfYkxjXGmFWCPM5OCOaykpSeZj8v3QBBm8F6h2oYbgEcGlaABl9rYzzqfdTWoK0NY0zDFnpwA9oEP4B1SLsGrXwckIGuQxtIPg71MKx2HcS9cYSIbEQBbkYboEGtD3sv3R2IfPD5gfxt_DR71OouwrO79yz78vbi8_m7_OrT8vL8zVVuOGVlDkTiGpfQVKblLWuE4JWRwA0pK0JrXTZNwTQD2coCUy4KXlTSGMYNL03DMD3LXk--m7HuoTFpdcqkNsH2OuyU11b9-ePsSl37raKYcUoS_-qOD_5mTKeq3sb9JdqBH6MiglFGJUvCl38J134MLt2miGQFF7wsk2g2iUzwMQZo74MQrPY1q0PNiVBMpZoT8OI4_pF86jUJxCS4tR3s_mOnLj4s3gsmiwLvs8wnMibIXUM4CvyvMPlE2NT4j_tdOnxXXFDB1NePSyW-LZZFWS2UpL8AsGXYqA</recordid><startdate>20000301</startdate><enddate>20000301</enddate><creator>Chen, Min-Huei</creator><creator>Sheng, Jinsong</creator><creator>Hind, Geoffrey</creator><creator>Handa, Avtar K.</creator><creator>Citovsky, Vitaly</creator><general>John Wiley &amp; Sons, Ltd</general><general>Nature Publishing Group UK</general><general>Blackwell Publishing Ltd</general><general>Oxford University Press</general><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>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>BKSAR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M7N</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PCBAR</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>5PM</scope></search><sort><creationdate>20000301</creationdate><title>Interaction between the tobacco mosaic virus movement protein and host cell pectin methylesterases is required for viral cell-to-cell movement</title><author>Chen, Min-Huei ; Sheng, Jinsong ; Hind, Geoffrey ; Handa, Avtar K. ; Citovsky, Vitaly</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c6354-e190b04ed8cf6f5d7768c9e6c14813ba4dd25a5e9f92036726289cc56c64cd503</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>Binding Sites</topic><topic>Carboxylic Ester Hydrolases - metabolism</topic><topic>Cauliflower mosaic virus</topic><topic>Inactivation</topic><topic>Molecular Sequence Data</topic><topic>movement protein</topic><topic>movement proteins</topic><topic>MP protein</topic><topic>Nicotiana - metabolism</topic><topic>Nicotiana - virology</topic><topic>Nicotiana tabacum</topic><topic>pectin methylesterase</topic><topic>pectin methylesterases</topic><topic>Plant Viral Movement Proteins</topic><topic>plant viruses</topic><topic>Plants, Toxic</topic><topic>plasmodesmata</topic><topic>Protein Binding</topic><topic>Sequence Alignment</topic><topic>Tobacco</topic><topic>Tobacco mosaic virus</topic><topic>Tobacco Mosaic Virus - physiology</topic><topic>Turnip vein-clearing virus</topic><topic>Viral Proteins - metabolism</topic><topic>Virus Replication</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Chen, Min-Huei</creatorcontrib><creatorcontrib>Sheng, Jinsong</creatorcontrib><creatorcontrib>Hind, Geoffrey</creatorcontrib><creatorcontrib>Handa, Avtar K.</creatorcontrib><creatorcontrib>Citovsky, Vitaly</creatorcontrib><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>ProQuest Central (Corporate)</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium &amp; Calcified Tissue Abstracts</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health &amp; Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Earth, Atmospheric &amp; Aquatic Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health &amp; Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health &amp; Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Research Library (Corporate)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Earth, Atmospheric &amp; Aquatic Science Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>Genetics Abstracts</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The EMBO journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Chen, Min-Huei</au><au>Sheng, Jinsong</au><au>Hind, Geoffrey</au><au>Handa, Avtar K.</au><au>Citovsky, Vitaly</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Interaction between the tobacco mosaic virus movement protein and host cell pectin methylesterases is required for viral cell-to-cell movement</atitle><jtitle>The EMBO journal</jtitle><stitle>EMBO J</stitle><addtitle>EMBO J</addtitle><date>2000-03-01</date><risdate>2000</risdate><volume>19</volume><issue>5</issue><spage>913</spage><epage>920</epage><pages>913-920</pages><issn>0261-4189</issn><eissn>1460-2075</eissn><coden>EMJODG</coden><abstract>Virus‐encoded movement protein (MP) mediates cell‐to‐cell spread of tobacco mosaic virus (TMV) through plant intercellular connections, the plasmodesmata. The molecular pathway by which TMV MP interacts with the host cell is largely unknown. To understand this process better, a cell wall‐associated protein that specifically binds the viral MP was purified from tobacco leaf cell walls and identified as pectin methylesterase (PME). In addition to TMV MP, PME is recognized by MPs of turnip vein clearing virus (TVCV) and cauliflower mosaic virus (CaMV). The use of amino acid deletion mutants of TMV MP showed that its domain was necessary and sufficient for association with PME. Deletion of the PME‐binding region resulted in inactivation of TMV cell‐to‐cell movement.</abstract><cop>Chichester, UK</cop><pub>John Wiley &amp; Sons, Ltd</pub><pmid>10698933</pmid><doi>10.1093/emboj/19.5.913</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 0261-4189
ispartof The EMBO journal, 2000-03, Vol.19 (5), p.913-920
issn 0261-4189
1460-2075
language eng
recordid cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_305631
source PubMed Central
subjects Amino Acid Sequence
Amino acids
Binding Sites
Carboxylic Ester Hydrolases - metabolism
Cauliflower mosaic virus
Inactivation
Molecular Sequence Data
movement protein
movement proteins
MP protein
Nicotiana - metabolism
Nicotiana - virology
Nicotiana tabacum
pectin methylesterase
pectin methylesterases
Plant Viral Movement Proteins
plant viruses
Plants, Toxic
plasmodesmata
Protein Binding
Sequence Alignment
Tobacco
Tobacco mosaic virus
Tobacco Mosaic Virus - physiology
Turnip vein-clearing virus
Viral Proteins - metabolism
Virus Replication
title Interaction between the tobacco mosaic virus movement protein and host cell pectin methylesterases is required for viral cell-to-cell movement
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-18T20%3A43%3A51IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Interaction%20between%20the%20tobacco%20mosaic%20virus%20movement%20protein%20and%20host%20cell%20pectin%20methylesterases%20is%20required%20for%20viral%20cell-to-cell%20movement&rft.jtitle=The%20EMBO%20journal&rft.au=Chen,%20Min-Huei&rft.date=2000-03-01&rft.volume=19&rft.issue=5&rft.spage=913&rft.epage=920&rft.pages=913-920&rft.issn=0261-4189&rft.eissn=1460-2075&rft.coden=EMJODG&rft_id=info:doi/10.1093/emboj/19.5.913&rft_dat=%3Cproquest_pubme%3E373526841%3C/proquest_pubme%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c6354-e190b04ed8cf6f5d7768c9e6c14813ba4dd25a5e9f92036726289cc56c64cd503%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=195267644&rft_id=info:pmid/10698933&rfr_iscdi=true