Heparin-like glycosaminoglycans prevent the infection of measles virus in SLAM-negative cell lines
The wide tissue tropism of the measles virus (MV) suggests that it involves ubiquitously expressed molecules. We have constructed a recombinant MV expressing the enhanced green fluorescent protein (EGFP) (rMV-EGFP) and demonstrated that the rMV-EGFP infected several cell types (HEK-293, HepG2, Hep3B...
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| Veröffentlicht in: | Antiviral research 2008-12, Vol.80 (3), p.370-376 |
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| creator | Terao-Muto, Yuri Yoneda, Misako Seki, Takahiro Watanabe, Akira Tsukiyama-Kohara, Kyoko Fujita, Kentaro Kai, Chieko |
| description | The wide tissue tropism of the measles virus (MV) suggests that it involves ubiquitously expressed molecules. We have constructed a recombinant MV expressing the enhanced green fluorescent protein (EGFP) (rMV-EGFP) and demonstrated that the rMV-EGFP infected several cell types (HEK-293, HepG2, Hep3B, Huh7, and WRL68 cells) that do not express the human signalling lymphocyte activation molecule (SLAM), which is known as a cellular receptor for morbilliviruses. MV infection of HEK-293 and HepG2 cells was not inhibited in an infectivity–inhibition assay using an anti-SLAM monoclonal antibody, indicating that MV could infect cells without using SLAM. Soluble heparin (HP) inhibited the rMV-EGFP infectivity in SLAM-negative cell lines in a dose-dependent manner. Direct interaction between purified virions and HP was detected in a surface plasmon resonance assay. We also demonstrated that the hemagglutinin (H) protein, but not the fusion (F) protein is responsible for the interaction between the virions and HP. Taken together, our results suggest that HP-like glycosaminoglycans bind to the H protein of MV and play a key role in the infection of SLAM-negative cells. |
| doi_str_mv | 10.1016/j.antiviral.2008.08.006 |
| format | Article |
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We have constructed a recombinant MV expressing the enhanced green fluorescent protein (EGFP) (rMV-EGFP) and demonstrated that the rMV-EGFP infected several cell types (HEK-293, HepG2, Hep3B, Huh7, and WRL68 cells) that do not express the human signalling lymphocyte activation molecule (SLAM), which is known as a cellular receptor for morbilliviruses. MV infection of HEK-293 and HepG2 cells was not inhibited in an infectivity–inhibition assay using an anti-SLAM monoclonal antibody, indicating that MV could infect cells without using SLAM. Soluble heparin (HP) inhibited the rMV-EGFP infectivity in SLAM-negative cell lines in a dose-dependent manner. Direct interaction between purified virions and HP was detected in a surface plasmon resonance assay. We also demonstrated that the hemagglutinin (H) protein, but not the fusion (F) protein is responsible for the interaction between the virions and HP. Taken together, our results suggest that HP-like glycosaminoglycans bind to the H protein of MV and play a key role in the infection of SLAM-negative cells.</description><identifier>ISSN: 0166-3542</identifier><identifier>EISSN: 1872-9096</identifier><identifier>DOI: 10.1016/j.antiviral.2008.08.006</identifier><identifier>PMID: 18812191</identifier><identifier>CODEN: ARSRDR</identifier><language>eng</language><publisher>Kidlington: Elsevier B.V</publisher><subject>Antibiotics. Antiinfectious agents. Antiparasitic agents ; Antigens, CD - metabolism ; Antiviral agents ; Biological and medical sciences ; Cell Line ; Glycosaminoglycans - metabolism ; Green Fluorescent Proteins - genetics ; Green Fluorescent Proteins - metabolism ; Hemagglutinin ; Hemagglutinins, Viral - genetics ; Hemagglutinins, Viral - metabolism ; Heparan sulphate ; Heparin - metabolism ; Humans ; Measles - metabolism ; Measles - prevention & control ; Measles - virology ; Measles virus ; Measles virus - genetics ; Measles virus - physiology ; Medical sciences ; Pharmacology. Drug treatments ; Protein Binding ; Receptors, Cell Surface - metabolism ; Receptors, Virus - metabolism ; Recombinant Fusion Proteins - genetics ; Recombinant Fusion Proteins - metabolism ; Signaling Lymphocytic Activation Molecule Family Member 1 ; SLAM-negative cells ; Viral Fusion Proteins - genetics ; Viral Fusion Proteins - metabolism ; Virus Internalization</subject><ispartof>Antiviral research, 2008-12, Vol.80 (3), p.370-376</ispartof><rights>2008 Elsevier B.V.</rights><rights>2009 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c430t-a29b1db46c8d29094251b2af4e3f17630bd717ddfd7c4ea69f805e0aa6ae4a9f3</citedby><cites>FETCH-LOGICAL-c430t-a29b1db46c8d29094251b2af4e3f17630bd717ddfd7c4ea69f805e0aa6ae4a9f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0166354208003872$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=20952716$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18812191$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Terao-Muto, Yuri</creatorcontrib><creatorcontrib>Yoneda, Misako</creatorcontrib><creatorcontrib>Seki, Takahiro</creatorcontrib><creatorcontrib>Watanabe, Akira</creatorcontrib><creatorcontrib>Tsukiyama-Kohara, Kyoko</creatorcontrib><creatorcontrib>Fujita, Kentaro</creatorcontrib><creatorcontrib>Kai, Chieko</creatorcontrib><title>Heparin-like glycosaminoglycans prevent the infection of measles virus in SLAM-negative cell lines</title><title>Antiviral research</title><addtitle>Antiviral Res</addtitle><description>The wide tissue tropism of the measles virus (MV) suggests that it involves ubiquitously expressed molecules. We have constructed a recombinant MV expressing the enhanced green fluorescent protein (EGFP) (rMV-EGFP) and demonstrated that the rMV-EGFP infected several cell types (HEK-293, HepG2, Hep3B, Huh7, and WRL68 cells) that do not express the human signalling lymphocyte activation molecule (SLAM), which is known as a cellular receptor for morbilliviruses. MV infection of HEK-293 and HepG2 cells was not inhibited in an infectivity–inhibition assay using an anti-SLAM monoclonal antibody, indicating that MV could infect cells without using SLAM. Soluble heparin (HP) inhibited the rMV-EGFP infectivity in SLAM-negative cell lines in a dose-dependent manner. Direct interaction between purified virions and HP was detected in a surface plasmon resonance assay. We also demonstrated that the hemagglutinin (H) protein, but not the fusion (F) protein is responsible for the interaction between the virions and HP. Taken together, our results suggest that HP-like glycosaminoglycans bind to the H protein of MV and play a key role in the infection of SLAM-negative cells.</description><subject>Antibiotics. Antiinfectious agents. Antiparasitic agents</subject><subject>Antigens, CD - metabolism</subject><subject>Antiviral agents</subject><subject>Biological and medical sciences</subject><subject>Cell Line</subject><subject>Glycosaminoglycans - metabolism</subject><subject>Green Fluorescent Proteins - genetics</subject><subject>Green Fluorescent Proteins - metabolism</subject><subject>Hemagglutinin</subject><subject>Hemagglutinins, Viral - genetics</subject><subject>Hemagglutinins, Viral - metabolism</subject><subject>Heparan sulphate</subject><subject>Heparin - metabolism</subject><subject>Humans</subject><subject>Measles - metabolism</subject><subject>Measles - prevention & control</subject><subject>Measles - virology</subject><subject>Measles virus</subject><subject>Measles virus - genetics</subject><subject>Measles virus - physiology</subject><subject>Medical sciences</subject><subject>Pharmacology. Drug treatments</subject><subject>Protein Binding</subject><subject>Receptors, Cell Surface - metabolism</subject><subject>Receptors, Virus - metabolism</subject><subject>Recombinant Fusion Proteins - genetics</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>Signaling Lymphocytic Activation Molecule Family Member 1</subject><subject>SLAM-negative cells</subject><subject>Viral Fusion Proteins - genetics</subject><subject>Viral Fusion Proteins - metabolism</subject><subject>Virus Internalization</subject><issn>0166-3542</issn><issn>1872-9096</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkcFu1DAQhi0EokvhFcAXestiO4kdH1cVtJW24tBytib2uHhJnMXOrtS3x9GuyrHSSDOSv5n5PT8hXzhbc8blt90a4hyOIcGwFox16yWYfENWvFOi0kzLt2RVSFnVbSMuyIecd6wQSnfvyQXvOi645ivS3-IeUojVEP4gfRqe7ZRhDHFaSoiZ7hMeMc50_o00RI92DlOkk6cjQh4w0yLikMsTfdhu7quIT1CEIbU4DHQIEfNH8s7DkPHTOV-SXz--P17fVtufN3fXm21lm5rNFQjdc9c30nZOlA80ouW9AN9g7bmSNeud4so575RtEKT2HWuRAUjABrSvL8nVae4-TX8PmGczhrzIgIjTIRupO650y18FuW4V6xpZQHUCbZpyTujNPoUR0rPhzCw-mJ158cEsPpgl2NL5-bzi0I_o_vedD1-Ar2cAsoXBJ4g25BdOMN0KxZdBmxOH5XLHgMlkGzBadCEVL4ybwqti_gEuTKx9</recordid><startdate>20081201</startdate><enddate>20081201</enddate><creator>Terao-Muto, Yuri</creator><creator>Yoneda, Misako</creator><creator>Seki, Takahiro</creator><creator>Watanabe, Akira</creator><creator>Tsukiyama-Kohara, Kyoko</creator><creator>Fujita, Kentaro</creator><creator>Kai, Chieko</creator><general>Elsevier B.V</general><general>Elsevier</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>7T7</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>20081201</creationdate><title>Heparin-like glycosaminoglycans prevent the infection of measles virus in SLAM-negative cell lines</title><author>Terao-Muto, Yuri ; Yoneda, Misako ; Seki, Takahiro ; Watanabe, Akira ; Tsukiyama-Kohara, Kyoko ; Fujita, Kentaro ; Kai, Chieko</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c430t-a29b1db46c8d29094251b2af4e3f17630bd717ddfd7c4ea69f805e0aa6ae4a9f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Antibiotics. Antiinfectious agents. Antiparasitic agents</topic><topic>Antigens, CD - metabolism</topic><topic>Antiviral agents</topic><topic>Biological and medical sciences</topic><topic>Cell Line</topic><topic>Glycosaminoglycans - metabolism</topic><topic>Green Fluorescent Proteins - genetics</topic><topic>Green Fluorescent Proteins - metabolism</topic><topic>Hemagglutinin</topic><topic>Hemagglutinins, Viral - genetics</topic><topic>Hemagglutinins, Viral - metabolism</topic><topic>Heparan sulphate</topic><topic>Heparin - metabolism</topic><topic>Humans</topic><topic>Measles - metabolism</topic><topic>Measles - prevention & control</topic><topic>Measles - virology</topic><topic>Measles virus</topic><topic>Measles virus - genetics</topic><topic>Measles virus - physiology</topic><topic>Medical sciences</topic><topic>Pharmacology. Drug treatments</topic><topic>Protein Binding</topic><topic>Receptors, Cell Surface - metabolism</topic><topic>Receptors, Virus - metabolism</topic><topic>Recombinant Fusion Proteins - genetics</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>Signaling Lymphocytic Activation Molecule Family Member 1</topic><topic>SLAM-negative cells</topic><topic>Viral Fusion Proteins - genetics</topic><topic>Viral Fusion Proteins - metabolism</topic><topic>Virus Internalization</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Terao-Muto, Yuri</creatorcontrib><creatorcontrib>Yoneda, Misako</creatorcontrib><creatorcontrib>Seki, Takahiro</creatorcontrib><creatorcontrib>Watanabe, Akira</creatorcontrib><creatorcontrib>Tsukiyama-Kohara, Kyoko</creatorcontrib><creatorcontrib>Fujita, Kentaro</creatorcontrib><creatorcontrib>Kai, Chieko</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>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Antiviral research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Terao-Muto, Yuri</au><au>Yoneda, Misako</au><au>Seki, Takahiro</au><au>Watanabe, Akira</au><au>Tsukiyama-Kohara, Kyoko</au><au>Fujita, Kentaro</au><au>Kai, Chieko</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Heparin-like glycosaminoglycans prevent the infection of measles virus in SLAM-negative cell lines</atitle><jtitle>Antiviral research</jtitle><addtitle>Antiviral Res</addtitle><date>2008-12-01</date><risdate>2008</risdate><volume>80</volume><issue>3</issue><spage>370</spage><epage>376</epage><pages>370-376</pages><issn>0166-3542</issn><eissn>1872-9096</eissn><coden>ARSRDR</coden><abstract>The wide tissue tropism of the measles virus (MV) suggests that it involves ubiquitously expressed molecules. We have constructed a recombinant MV expressing the enhanced green fluorescent protein (EGFP) (rMV-EGFP) and demonstrated that the rMV-EGFP infected several cell types (HEK-293, HepG2, Hep3B, Huh7, and WRL68 cells) that do not express the human signalling lymphocyte activation molecule (SLAM), which is known as a cellular receptor for morbilliviruses. MV infection of HEK-293 and HepG2 cells was not inhibited in an infectivity–inhibition assay using an anti-SLAM monoclonal antibody, indicating that MV could infect cells without using SLAM. Soluble heparin (HP) inhibited the rMV-EGFP infectivity in SLAM-negative cell lines in a dose-dependent manner. Direct interaction between purified virions and HP was detected in a surface plasmon resonance assay. We also demonstrated that the hemagglutinin (H) protein, but not the fusion (F) protein is responsible for the interaction between the virions and HP. Taken together, our results suggest that HP-like glycosaminoglycans bind to the H protein of MV and play a key role in the infection of SLAM-negative cells.</abstract><cop>Kidlington</cop><pub>Elsevier B.V</pub><pmid>18812191</pmid><doi>10.1016/j.antiviral.2008.08.006</doi><tpages>7</tpages></addata></record> |
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| subjects | Antibiotics. Antiinfectious agents. Antiparasitic agents Antigens, CD - metabolism Antiviral agents Biological and medical sciences Cell Line Glycosaminoglycans - metabolism Green Fluorescent Proteins - genetics Green Fluorescent Proteins - metabolism Hemagglutinin Hemagglutinins, Viral - genetics Hemagglutinins, Viral - metabolism Heparan sulphate Heparin - metabolism Humans Measles - metabolism Measles - prevention & control Measles - virology Measles virus Measles virus - genetics Measles virus - physiology Medical sciences Pharmacology. Drug treatments Protein Binding Receptors, Cell Surface - metabolism Receptors, Virus - metabolism Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism Signaling Lymphocytic Activation Molecule Family Member 1 SLAM-negative cells Viral Fusion Proteins - genetics Viral Fusion Proteins - metabolism Virus Internalization |
| title | Heparin-like glycosaminoglycans prevent the infection of measles virus in SLAM-negative cell lines |
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