HBV infection of cell culture: evidence for multivalent and cooperative attachment
Hepadnaviruses do not infect cultured cells, therefore our knowledge of the mechanism of the early stages of virus–cell interaction is rather poor. In this study, we show that dimethylsulfoxide (DMSO)‐treated HepG2 hepatoblastoma cells are infected efficiently by serum‐derived hepatitis B virus (HBV...
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| description | Hepadnaviruses do not infect cultured cells, therefore our knowledge of the mechanism of the early stages of virus–cell interaction is rather poor. In this study, we show that dimethylsulfoxide (DMSO)‐treated HepG2 hepatoblastoma cells are infected efficiently by serum‐derived hepatitis B virus (HBV) as monitored by viral gene expression and replication markers. To measure virus attachment, a variety of HBV surface proteins (HBsAgs) were conjugated to polystyrene beads and their capacity to attach cells was visualized and quantified by light microscopy at a single‐cell resolution. Remarkably, DMSO increases the attachment efficiency by >200‐fold. We further identify the QLDPAF sequence within preS1 as the receptor‐binding viral domain epitope. Interestingly, a similar sequence is shared by several cellular, bacterial and viral proteins involved in cell adhesion, attachment and fusion. We also found that the small HBsAg contains a secondary attachment site that recognizes a distinct receptor on the cell membrane. Furthermore, we provide evidence in support of multivalent HBV attachment with synergistic interplay. Our data depict a mechanistic view of virus attachment and ingestion. |
| doi_str_mv | 10.1093/emboj/20.16.4443 |
| format | Article |
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In this study, we show that dimethylsulfoxide (DMSO)‐treated HepG2 hepatoblastoma cells are infected efficiently by serum‐derived hepatitis B virus (HBV) as monitored by viral gene expression and replication markers. To measure virus attachment, a variety of HBV surface proteins (HBsAgs) were conjugated to polystyrene beads and their capacity to attach cells was visualized and quantified by light microscopy at a single‐cell resolution. Remarkably, DMSO increases the attachment efficiency by >200‐fold. We further identify the QLDPAF sequence within preS1 as the receptor‐binding viral domain epitope. Interestingly, a similar sequence is shared by several cellular, bacterial and viral proteins involved in cell adhesion, attachment and fusion. We also found that the small HBsAg contains a secondary attachment site that recognizes a distinct receptor on the cell membrane. Furthermore, we provide evidence in support of multivalent HBV attachment with synergistic interplay. Our data depict a mechanistic view of virus attachment and ingestion.</description><identifier>ISSN: 0261-4189</identifier><identifier>ISSN: 1460-2075</identifier><identifier>EISSN: 1460-2075</identifier><identifier>DOI: 10.1093/emboj/20.16.4443</identifier><identifier>PMID: 11500372</identifier><identifier>CODEN: EMJODG</identifier><language>eng</language><publisher>Chichester, UK: John Wiley & Sons, Ltd</publisher><subject>Amino Acid Sequence ; Binding Sites ; Cell Culture Techniques ; Detergents - pharmacology ; Dimethyl Sulfoxide - pharmacology ; Endocytosis ; HBsAg proteins ; HBV infection ; Hepatitis B Surface Antigens - genetics ; Hepatitis B Surface Antigens - metabolism ; Hepatitis B virus ; Hepatitis B virus - genetics ; Hepatitis B virus - metabolism ; Humans ; Ingestion ; Light microscopy ; Membrane Fusion - physiology ; Molecular Sequence Data ; Protein Precursors - genetics ; Protein Precursors - metabolism ; QLDPAF motif ; Recombinant Fusion Proteins - genetics ; Recombinant Fusion Proteins - metabolism ; Tumor Cells, Cultured ; Virion ; virus attachment</subject><ispartof>The EMBO journal, 2001-08, Vol.20 (16), p.4443-4453</ispartof><rights>European Molecular Biology organization 2001</rights><rights>Copyright © 2001 European Molecular Biology organization</rights><rights>Copyright Oxford University Press(England) Aug 15, 2001</rights><rights>Copyright © 2001 European Molecular Biology Organization 2001</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c6672-85b4ff211785cad14f017a8a916d1cc1b76b972f8f7fcc79c777e207f90960483</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC125578/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC125578/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,1417,1433,27924,27925,45574,45575,46409,46833,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11500372$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Paran, Nir</creatorcontrib><creatorcontrib>Geiger, Benjamin</creatorcontrib><creatorcontrib>Shaul, Yosef</creatorcontrib><title>HBV infection of cell culture: evidence for multivalent and cooperative attachment</title><title>The EMBO journal</title><addtitle>EMBO J</addtitle><addtitle>EMBO J</addtitle><description>Hepadnaviruses do not infect cultured cells, therefore our knowledge of the mechanism of the early stages of virus–cell interaction is rather poor. In this study, we show that dimethylsulfoxide (DMSO)‐treated HepG2 hepatoblastoma cells are infected efficiently by serum‐derived hepatitis B virus (HBV) as monitored by viral gene expression and replication markers. To measure virus attachment, a variety of HBV surface proteins (HBsAgs) were conjugated to polystyrene beads and their capacity to attach cells was visualized and quantified by light microscopy at a single‐cell resolution. Remarkably, DMSO increases the attachment efficiency by >200‐fold. We further identify the QLDPAF sequence within preS1 as the receptor‐binding viral domain epitope. Interestingly, a similar sequence is shared by several cellular, bacterial and viral proteins involved in cell adhesion, attachment and fusion. We also found that the small HBsAg contains a secondary attachment site that recognizes a distinct receptor on the cell membrane. Furthermore, we provide evidence in support of multivalent HBV attachment with synergistic interplay. Our data depict a mechanistic view of virus attachment and ingestion.</description><subject>Amino Acid Sequence</subject><subject>Binding Sites</subject><subject>Cell Culture Techniques</subject><subject>Detergents - pharmacology</subject><subject>Dimethyl Sulfoxide - pharmacology</subject><subject>Endocytosis</subject><subject>HBsAg proteins</subject><subject>HBV infection</subject><subject>Hepatitis B Surface Antigens - genetics</subject><subject>Hepatitis B Surface Antigens - metabolism</subject><subject>Hepatitis B virus</subject><subject>Hepatitis B virus - genetics</subject><subject>Hepatitis B virus - metabolism</subject><subject>Humans</subject><subject>Ingestion</subject><subject>Light microscopy</subject><subject>Membrane Fusion - physiology</subject><subject>Molecular Sequence Data</subject><subject>Protein Precursors - genetics</subject><subject>Protein Precursors - metabolism</subject><subject>QLDPAF motif</subject><subject>Recombinant Fusion Proteins - genetics</subject><subject>Recombinant Fusion Proteins - 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Academic</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>Paran, Nir</au><au>Geiger, Benjamin</au><au>Shaul, Yosef</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>HBV infection of cell culture: evidence for multivalent and cooperative attachment</atitle><jtitle>The EMBO journal</jtitle><stitle>EMBO J</stitle><addtitle>EMBO J</addtitle><date>2001-08-15</date><risdate>2001</risdate><volume>20</volume><issue>16</issue><spage>4443</spage><epage>4453</epage><pages>4443-4453</pages><issn>0261-4189</issn><issn>1460-2075</issn><eissn>1460-2075</eissn><coden>EMJODG</coden><abstract>Hepadnaviruses do not infect cultured cells, therefore our knowledge of the mechanism of the early stages of virus–cell interaction is rather poor. In this study, we show that dimethylsulfoxide (DMSO)‐treated HepG2 hepatoblastoma cells are infected efficiently by serum‐derived hepatitis B virus (HBV) as monitored by viral gene expression and replication markers. To measure virus attachment, a variety of HBV surface proteins (HBsAgs) were conjugated to polystyrene beads and their capacity to attach cells was visualized and quantified by light microscopy at a single‐cell resolution. Remarkably, DMSO increases the attachment efficiency by >200‐fold. We further identify the QLDPAF sequence within preS1 as the receptor‐binding viral domain epitope. Interestingly, a similar sequence is shared by several cellular, bacterial and viral proteins involved in cell adhesion, attachment and fusion. We also found that the small HBsAg contains a secondary attachment site that recognizes a distinct receptor on the cell membrane. Furthermore, we provide evidence in support of multivalent HBV attachment with synergistic interplay. Our data depict a mechanistic view of virus attachment and ingestion.</abstract><cop>Chichester, UK</cop><pub>John Wiley & Sons, Ltd</pub><pmid>11500372</pmid><doi>10.1093/emboj/20.16.4443</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Sequence Binding Sites Cell Culture Techniques Detergents - pharmacology Dimethyl Sulfoxide - pharmacology Endocytosis HBsAg proteins HBV infection Hepatitis B Surface Antigens - genetics Hepatitis B Surface Antigens - metabolism Hepatitis B virus Hepatitis B virus - genetics Hepatitis B virus - metabolism Humans Ingestion Light microscopy Membrane Fusion - physiology Molecular Sequence Data Protein Precursors - genetics Protein Precursors - metabolism QLDPAF motif Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism Tumor Cells, Cultured Virion virus attachment |
| title | HBV infection of cell culture: evidence for multivalent and cooperative attachment |
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