Intracellular processing and transport of Junin virus glycoproteins influences virion infectivity
The influence of glycoprotein processing, cleavage and transport on Junin virus (JV) infectivity was investigated using monensin combined with lectin binding assays. Yields of extracellular virus were more significantly reduced than cell-associated virus, indicating that monensin inhibited the trans...
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| Veröffentlicht in: | Virus research 1994-12, Vol.34 (3), p.317-326 |
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| container_title | Virus research |
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| creator | Damonte, Elsa B. Mersich, Susana E. Candurra, Nélida A. |
| description | The influence of glycoprotein processing, cleavage and transport on Junin virus (JV) infectivity was investigated using monensin combined with lectin binding assays. Yields of extracellular virus were more significantly reduced than cell-associated virus, indicating that monensin inhibited the transport of infectious virus to the extracellular space on a late stage of the replicative cycle. Shown by lectin reactivity and immunoprecipitation, the intracellular processing of JV glycoproteins involved first the maturation of GPC oligosaccharides to a complex form and then the precursor cleavage which might occur late in transit through or exit from the Golgi cisternae. Cleavage of GPC to yield the mature GP38 as well as cell surface immunofluorescence were blocked by monensin. Thus, GP38 production together with glycoprotein transport to the cell membrane seemed to be required for the release of infectious virus from JV-infected cells. |
| doi_str_mv | 10.1016/0168-1702(94)90131-7 |
| format | Article |
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Yields of extracellular virus were more significantly reduced than cell-associated virus, indicating that monensin inhibited the transport of infectious virus to the extracellular space on a late stage of the replicative cycle. Shown by lectin reactivity and immunoprecipitation, the intracellular processing of JV glycoproteins involved first the maturation of GPC oligosaccharides to a complex form and then the precursor cleavage which might occur late in transit through or exit from the Golgi cisternae. Cleavage of GPC to yield the mature GP38 as well as cell surface immunofluorescence were blocked by monensin. Thus, GP38 production together with glycoprotein transport to the cell membrane seemed to be required for the release of infectious virus from JV-infected cells.</description><subject>Animals</subject><subject>Arenavirus</subject><subject>Biological Transport - drug effects</subject><subject>Cercopithecus aethiops</subject><subject>Fluorescent Antibody Technique</subject><subject>Glycoprotein processing</subject><subject>Glycoprotein transport</subject><subject>Glycoproteins - metabolism</subject><subject>Junin virus</subject><subject>Junin virus - drug effects</subject><subject>Junin virus - pathogenicity</subject><subject>Junin virus - physiology</subject><subject>Lectins - pharmacology</subject><subject>Monensin</subject><subject>Monensin - pharmacology</subject><subject>Peptide Hydrolases</subject><subject>Protein Processing, Post-Translational - drug effects</subject><subject>Vero Cells</subject><subject>Viral Envelope Proteins</subject><subject>Viral Proteins - metabolism</subject><subject>Virus Replication - drug effects</subject><issn>0168-1702</issn><issn>1872-7492</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUtLAzEUhYMotVb_gcKsRBejeczksRFEfFJw033IZJISmSY1mSn035uxpUtdhAs559zkfheASwTvEET0Ph9eIgbxjahuBUQElewITBFnuGSVwMdgerCcgrOUviCElDA6ARPGa0oQmwL17vuotOm6oVOxWMegTUrOLwvl2yJLPq1D7Itgi4_BO19sXBxSsey2OmRzb5xPhfO2G4zPyVF2wY83Rvdu4_rtOTixqkvmYl9nYPHyvHh6K-efr-9Pj_NSE877shIVqVutGgwhtkbVhmhkG41wpWtoaygYq1VD2oZazLFBgnJhCRVQ6ZZbMgPXu7b5V9-DSb1cuTTOpbwJQ5KMMZIT-F8joqzmmWY2VjujjiGlaKxcR7dScSsRlOMG5IhXjnilqOTvBiTLsat9_6FZmfYQ2iPP-sNONxnGxpkok3YjvNbFzEy2wf39wA-pSpeH</recordid><startdate>19941201</startdate><enddate>19941201</enddate><creator>Damonte, Elsa B.</creator><creator>Mersich, Susana E.</creator><creator>Candurra, Nélida A.</creator><general>Elsevier B.V</general><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>7U9</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>19941201</creationdate><title>Intracellular processing and transport of Junin virus glycoproteins influences virion infectivity</title><author>Damonte, Elsa B. ; Mersich, Susana E. ; Candurra, Nélida A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c388t-49435dcab2002fea5e3c1fbc124c50f509775ab3db6f282e19689f3690acd8f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Animals</topic><topic>Arenavirus</topic><topic>Biological Transport - drug effects</topic><topic>Cercopithecus aethiops</topic><topic>Fluorescent Antibody Technique</topic><topic>Glycoprotein processing</topic><topic>Glycoprotein transport</topic><topic>Glycoproteins - metabolism</topic><topic>Junin virus</topic><topic>Junin virus - drug effects</topic><topic>Junin virus - pathogenicity</topic><topic>Junin virus - physiology</topic><topic>Lectins - pharmacology</topic><topic>Monensin</topic><topic>Monensin - pharmacology</topic><topic>Peptide Hydrolases</topic><topic>Protein Processing, Post-Translational - drug effects</topic><topic>Vero Cells</topic><topic>Viral Envelope Proteins</topic><topic>Viral Proteins - metabolism</topic><topic>Virus Replication - drug effects</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Damonte, Elsa B.</creatorcontrib><creatorcontrib>Mersich, Susana E.</creatorcontrib><creatorcontrib>Candurra, Nélida A.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Virology and AIDS Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Virus research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Damonte, Elsa B.</au><au>Mersich, Susana E.</au><au>Candurra, Nélida A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Intracellular processing and transport of Junin virus glycoproteins influences virion infectivity</atitle><jtitle>Virus research</jtitle><addtitle>Virus Res</addtitle><date>1994-12-01</date><risdate>1994</risdate><volume>34</volume><issue>3</issue><spage>317</spage><epage>326</epage><pages>317-326</pages><issn>0168-1702</issn><eissn>1872-7492</eissn><abstract>The influence of glycoprotein processing, cleavage and transport on Junin virus (JV) infectivity was investigated using monensin combined with lectin binding assays. Yields of extracellular virus were more significantly reduced than cell-associated virus, indicating that monensin inhibited the transport of infectious virus to the extracellular space on a late stage of the replicative cycle. Shown by lectin reactivity and immunoprecipitation, the intracellular processing of JV glycoproteins involved first the maturation of GPC oligosaccharides to a complex form and then the precursor cleavage which might occur late in transit through or exit from the Golgi cisternae. Cleavage of GPC to yield the mature GP38 as well as cell surface immunofluorescence were blocked by monensin. Thus, GP38 production together with glycoprotein transport to the cell membrane seemed to be required for the release of infectious virus from JV-infected cells.</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>7856317</pmid><doi>10.1016/0168-1702(94)90131-7</doi><tpages>10</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0168-1702 |
| ispartof | Virus research, 1994-12, Vol.34 (3), p.317-326 |
| issn | 0168-1702 1872-7492 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Animals Arenavirus Biological Transport - drug effects Cercopithecus aethiops Fluorescent Antibody Technique Glycoprotein processing Glycoprotein transport Glycoproteins - metabolism Junin virus Junin virus - drug effects Junin virus - pathogenicity Junin virus - physiology Lectins - pharmacology Monensin Monensin - pharmacology Peptide Hydrolases Protein Processing, Post-Translational - drug effects Vero Cells Viral Envelope Proteins Viral Proteins - metabolism Virus Replication - drug effects |
| title | Intracellular processing and transport of Junin virus glycoproteins influences virion infectivity |
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