Postbinding fusion function contributed by a chimeric murine leukemia virus envelope protein
We previously obtained a chimeric Friend murine leukemia virus (FMLV) envelope protein (Env) in which the whole receptor-binding domain (RBD) was replaced with a surface domain of human CD4. Here, we examined if the postbinding fusion function of the CD4-Env chimera still remains to be intact. While...
Gespeichert in:
Veröffentlicht in: | Archives of virology 2001-01, Vol.146 (5), p.953-961 |
---|---|
Hauptverfasser: | , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 961 |
---|---|
container_issue | 5 |
container_start_page | 953 |
container_title | Archives of virology |
container_volume | 146 |
creator | NAKAMURA, H TAKEDA, A MATANO, T |
description | We previously obtained a chimeric Friend murine leukemia virus (FMLV) envelope protein (Env) in which the whole receptor-binding domain (RBD) was replaced with a surface domain of human CD4. Here, we examined if the postbinding fusion function of the CD4-Env chimera still remains to be intact. While a pseudotype MLV bearing CD4-Env showed no infectivity, NIH 3T3 cells could be infected with a pseudotype MLV bearing both CD4-Env and a mutant FMLV Env defective in postbinding fusion function. The pseudotype MLV showed no infectivity on HeLa cells but on the FMLV receptor (mCAT1)-expressing HeLa cells. In NIH 3T3 cells, the R-peptide-deleted CD4-Env could not induce syncytia by itself but did so in co-operation with the fusion-deficient Env. Syncytia induced by the coexpression were not observed in HeLa cells but in the mCAT1-expressing HeLa cells. These results indicate that the CD4-Env could contribute postbinding fusion function in the membrane fusion process triggered by FMLV RBD-mCAT1 interaction. |
doi_str_mv | 10.1007/s007050170127 |
format | Article |
fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_71020216</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>71020216</sourcerecordid><originalsourceid>FETCH-LOGICAL-c378t-eb182e8ce6f09227f67b8cd864f1a50c3e297d0dbaf7362dbb4d0345aab620043</originalsourceid><addsrcrecordid>eNqF0U1LHTEUBuBQWur1Y-lWAsXupj35mCSzLKK1INSF7oQhyZyxsTOZ22Qi-O8b8YLYTTc5ITy8h_AScszgCwPQX3M9oAWmgXH9jmyYFLwxujPvyQYEyMYoMHtkP-cHgPog2o9kjzEpDQi-IXfXS15diEOI93QsOSyxjujX54tf4pqCKysO1D1RS_2vMGMKns4lhYh0wvIb52DpY0glU4yPOC1bpNu0rBjiIfkw2inj0W4ekNuL85uzy-bq5_cfZ9-uGi-0WRt0zHA0HtUIHed6VNoZPxglR2Zb8AJ5pwcYnB21UHxwTg4gZGutUxxAigPy-SW37v1TMK_9HLLHabIRl5J7zYADZ-q_kGnTMaV4hZ_-gQ9LSbF-oq9ZUsuWtW1VzYvyack54dhvU5hteqqof26nf9NO9Se71OJmHF71ro4KTnfAZm-nMdnoQ351kine1cV_AQd0lw8</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1024745155</pqid></control><display><type>article</type><title>Postbinding fusion function contributed by a chimeric murine leukemia virus envelope protein</title><source>MEDLINE</source><source>SpringerLink Journals</source><creator>NAKAMURA, H ; TAKEDA, A ; MATANO, T</creator><creatorcontrib>NAKAMURA, H ; TAKEDA, A ; MATANO, T</creatorcontrib><description>We previously obtained a chimeric Friend murine leukemia virus (FMLV) envelope protein (Env) in which the whole receptor-binding domain (RBD) was replaced with a surface domain of human CD4. Here, we examined if the postbinding fusion function of the CD4-Env chimera still remains to be intact. While a pseudotype MLV bearing CD4-Env showed no infectivity, NIH 3T3 cells could be infected with a pseudotype MLV bearing both CD4-Env and a mutant FMLV Env defective in postbinding fusion function. The pseudotype MLV showed no infectivity on HeLa cells but on the FMLV receptor (mCAT1)-expressing HeLa cells. In NIH 3T3 cells, the R-peptide-deleted CD4-Env could not induce syncytia by itself but did so in co-operation with the fusion-deficient Env. Syncytia induced by the coexpression were not observed in HeLa cells but in the mCAT1-expressing HeLa cells. These results indicate that the CD4-Env could contribute postbinding fusion function in the membrane fusion process triggered by FMLV RBD-mCAT1 interaction.</description><identifier>ISSN: 0304-8608</identifier><identifier>EISSN: 1432-8798</identifier><identifier>DOI: 10.1007/s007050170127</identifier><identifier>PMID: 11448032</identifier><language>eng</language><publisher>Wien: Springer</publisher><subject>3T3 Cells - virology ; Animal viral diseases ; Animals ; Binding Sites ; Biological and medical sciences ; CD4 Antigens - genetics ; Cytopathogenic Effect, Viral - genetics ; Friend murine leukemia virus ; Friend murine leukemia virus - genetics ; Friend murine leukemia virus - pathogenicity ; Friend murine leukemia virus - physiology ; Fundamental and applied biological sciences. Psychology ; Gene Products, env - physiology ; Genes, env ; Giant Cells - virology ; HeLa Cells - virology ; Humans ; Infectious diseases ; Medical sciences ; Membrane Fusion - genetics ; Membrane Fusion - physiology ; Membrane Glycoproteins - metabolism ; Mice ; Microbiology ; NIH-3T3 cells ; Point Mutation ; Protein Structure, Tertiary ; Receptors, Virus - metabolism ; Recombinant Fusion Proteins - genetics ; Recombinant Fusion Proteins - physiology ; Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains ; Viral diseases ; Virology ; Virulence ; Virus Cultivation</subject><ispartof>Archives of virology, 2001-01, Vol.146 (5), p.953-961</ispartof><rights>2002 INIST-CNRS</rights><rights>Springer-Verlag/Wien 2001</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c378t-eb182e8ce6f09227f67b8cd864f1a50c3e297d0dbaf7362dbb4d0345aab620043</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=14162955$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11448032$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>NAKAMURA, H</creatorcontrib><creatorcontrib>TAKEDA, A</creatorcontrib><creatorcontrib>MATANO, T</creatorcontrib><title>Postbinding fusion function contributed by a chimeric murine leukemia virus envelope protein</title><title>Archives of virology</title><addtitle>Arch Virol</addtitle><description>We previously obtained a chimeric Friend murine leukemia virus (FMLV) envelope protein (Env) in which the whole receptor-binding domain (RBD) was replaced with a surface domain of human CD4. Here, we examined if the postbinding fusion function of the CD4-Env chimera still remains to be intact. While a pseudotype MLV bearing CD4-Env showed no infectivity, NIH 3T3 cells could be infected with a pseudotype MLV bearing both CD4-Env and a mutant FMLV Env defective in postbinding fusion function. The pseudotype MLV showed no infectivity on HeLa cells but on the FMLV receptor (mCAT1)-expressing HeLa cells. In NIH 3T3 cells, the R-peptide-deleted CD4-Env could not induce syncytia by itself but did so in co-operation with the fusion-deficient Env. Syncytia induced by the coexpression were not observed in HeLa cells but in the mCAT1-expressing HeLa cells. These results indicate that the CD4-Env could contribute postbinding fusion function in the membrane fusion process triggered by FMLV RBD-mCAT1 interaction.</description><subject>3T3 Cells - virology</subject><subject>Animal viral diseases</subject><subject>Animals</subject><subject>Binding Sites</subject><subject>Biological and medical sciences</subject><subject>CD4 Antigens - genetics</subject><subject>Cytopathogenic Effect, Viral - genetics</subject><subject>Friend murine leukemia virus</subject><subject>Friend murine leukemia virus - genetics</subject><subject>Friend murine leukemia virus - pathogenicity</subject><subject>Friend murine leukemia virus - physiology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Products, env - physiology</subject><subject>Genes, env</subject><subject>Giant Cells - virology</subject><subject>HeLa Cells - virology</subject><subject>Humans</subject><subject>Infectious diseases</subject><subject>Medical sciences</subject><subject>Membrane Fusion - genetics</subject><subject>Membrane Fusion - physiology</subject><subject>Membrane Glycoproteins - metabolism</subject><subject>Mice</subject><subject>Microbiology</subject><subject>NIH-3T3 cells</subject><subject>Point Mutation</subject><subject>Protein Structure, Tertiary</subject><subject>Receptors, Virus - metabolism</subject><subject>Recombinant Fusion Proteins - genetics</subject><subject>Recombinant Fusion Proteins - physiology</subject><subject>Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains</subject><subject>Viral diseases</subject><subject>Virology</subject><subject>Virulence</subject><subject>Virus Cultivation</subject><issn>0304-8608</issn><issn>1432-8798</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNqF0U1LHTEUBuBQWur1Y-lWAsXupj35mCSzLKK1INSF7oQhyZyxsTOZ22Qi-O8b8YLYTTc5ITy8h_AScszgCwPQX3M9oAWmgXH9jmyYFLwxujPvyQYEyMYoMHtkP-cHgPog2o9kjzEpDQi-IXfXS15diEOI93QsOSyxjujX54tf4pqCKysO1D1RS_2vMGMKns4lhYh0wvIb52DpY0glU4yPOC1bpNu0rBjiIfkw2inj0W4ekNuL85uzy-bq5_cfZ9-uGi-0WRt0zHA0HtUIHed6VNoZPxglR2Zb8AJ5pwcYnB21UHxwTg4gZGutUxxAigPy-SW37v1TMK_9HLLHabIRl5J7zYADZ-q_kGnTMaV4hZ_-gQ9LSbF-oq9ZUsuWtW1VzYvyack54dhvU5hteqqof26nf9NO9Se71OJmHF71ro4KTnfAZm-nMdnoQ351kine1cV_AQd0lw8</recordid><startdate>20010101</startdate><enddate>20010101</enddate><creator>NAKAMURA, H</creator><creator>TAKEDA, A</creator><creator>MATANO, T</creator><general>Springer</general><general>Springer Nature B.V</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>3V.</scope><scope>7TK</scope><scope>7TM</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>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>P64</scope><scope>PHGZM</scope><scope>PHGZT</scope><scope>PJZUB</scope><scope>PKEHL</scope><scope>PPXIY</scope><scope>PQEST</scope><scope>PQGLB</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20010101</creationdate><title>Postbinding fusion function contributed by a chimeric murine leukemia virus envelope protein</title><author>NAKAMURA, H ; TAKEDA, A ; MATANO, T</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c378t-eb182e8ce6f09227f67b8cd864f1a50c3e297d0dbaf7362dbb4d0345aab620043</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>3T3 Cells - virology</topic><topic>Animal viral diseases</topic><topic>Animals</topic><topic>Binding Sites</topic><topic>Biological and medical sciences</topic><topic>CD4 Antigens - genetics</topic><topic>Cytopathogenic Effect, Viral - genetics</topic><topic>Friend murine leukemia virus</topic><topic>Friend murine leukemia virus - genetics</topic><topic>Friend murine leukemia virus - pathogenicity</topic><topic>Friend murine leukemia virus - physiology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene Products, env - physiology</topic><topic>Genes, env</topic><topic>Giant Cells - virology</topic><topic>HeLa Cells - virology</topic><topic>Humans</topic><topic>Infectious diseases</topic><topic>Medical sciences</topic><topic>Membrane Fusion - genetics</topic><topic>Membrane Fusion - physiology</topic><topic>Membrane Glycoproteins - metabolism</topic><topic>Mice</topic><topic>Microbiology</topic><topic>NIH-3T3 cells</topic><topic>Point Mutation</topic><topic>Protein Structure, Tertiary</topic><topic>Receptors, Virus - metabolism</topic><topic>Recombinant Fusion Proteins - genetics</topic><topic>Recombinant Fusion Proteins - physiology</topic><topic>Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains</topic><topic>Viral diseases</topic><topic>Virology</topic><topic>Virulence</topic><topic>Virus Cultivation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>NAKAMURA, H</creatorcontrib><creatorcontrib>TAKEDA, A</creatorcontrib><creatorcontrib>MATANO, T</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>ProQuest Central (Corporate)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & 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>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection (ProQuest)</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>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest Central (New)</collection><collection>ProQuest One Academic (New)</collection><collection>ProQuest Health & Medical Research Collection</collection><collection>ProQuest One Academic Middle East (New)</collection><collection>ProQuest One Health & Nursing</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Applied & Life Sciences</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Archives of virology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>NAKAMURA, H</au><au>TAKEDA, A</au><au>MATANO, T</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Postbinding fusion function contributed by a chimeric murine leukemia virus envelope protein</atitle><jtitle>Archives of virology</jtitle><addtitle>Arch Virol</addtitle><date>2001-01-01</date><risdate>2001</risdate><volume>146</volume><issue>5</issue><spage>953</spage><epage>961</epage><pages>953-961</pages><issn>0304-8608</issn><eissn>1432-8798</eissn><abstract>We previously obtained a chimeric Friend murine leukemia virus (FMLV) envelope protein (Env) in which the whole receptor-binding domain (RBD) was replaced with a surface domain of human CD4. Here, we examined if the postbinding fusion function of the CD4-Env chimera still remains to be intact. While a pseudotype MLV bearing CD4-Env showed no infectivity, NIH 3T3 cells could be infected with a pseudotype MLV bearing both CD4-Env and a mutant FMLV Env defective in postbinding fusion function. The pseudotype MLV showed no infectivity on HeLa cells but on the FMLV receptor (mCAT1)-expressing HeLa cells. In NIH 3T3 cells, the R-peptide-deleted CD4-Env could not induce syncytia by itself but did so in co-operation with the fusion-deficient Env. Syncytia induced by the coexpression were not observed in HeLa cells but in the mCAT1-expressing HeLa cells. These results indicate that the CD4-Env could contribute postbinding fusion function in the membrane fusion process triggered by FMLV RBD-mCAT1 interaction.</abstract><cop>Wien</cop><cop>New York, NY</cop><pub>Springer</pub><pmid>11448032</pmid><doi>10.1007/s007050170127</doi><tpages>9</tpages></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0304-8608 |
ispartof | Archives of virology, 2001-01, Vol.146 (5), p.953-961 |
issn | 0304-8608 1432-8798 |
language | eng |
recordid | cdi_proquest_miscellaneous_71020216 |
source | MEDLINE; SpringerLink Journals |
subjects | 3T3 Cells - virology Animal viral diseases Animals Binding Sites Biological and medical sciences CD4 Antigens - genetics Cytopathogenic Effect, Viral - genetics Friend murine leukemia virus Friend murine leukemia virus - genetics Friend murine leukemia virus - pathogenicity Friend murine leukemia virus - physiology Fundamental and applied biological sciences. Psychology Gene Products, env - physiology Genes, env Giant Cells - virology HeLa Cells - virology Humans Infectious diseases Medical sciences Membrane Fusion - genetics Membrane Fusion - physiology Membrane Glycoproteins - metabolism Mice Microbiology NIH-3T3 cells Point Mutation Protein Structure, Tertiary Receptors, Virus - metabolism Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - physiology Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains Viral diseases Virology Virulence Virus Cultivation |
title | Postbinding fusion function contributed by a chimeric murine leukemia virus envelope protein |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-19T00%3A29%3A18IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Postbinding%20fusion%20function%20contributed%20by%20a%20chimeric%20murine%20leukemia%20virus%20envelope%20protein&rft.jtitle=Archives%20of%20virology&rft.au=NAKAMURA,%20H&rft.date=2001-01-01&rft.volume=146&rft.issue=5&rft.spage=953&rft.epage=961&rft.pages=953-961&rft.issn=0304-8608&rft.eissn=1432-8798&rft_id=info:doi/10.1007/s007050170127&rft_dat=%3Cproquest_cross%3E71020216%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1024745155&rft_id=info:pmid/11448032&rfr_iscdi=true |