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Glycoprotein D Homologs in Herpes Simplex Virus Type 1, Pseudorabies Virus, and Bovine Herpes Virus Type 1 Bind Directly to Human HveC (Nectin-1) with Different Affinities
Distinct subsets of human receptors for alphaherpesviruses mediate the entry of herpes simplex virus (HSV), pseudorabies virus (PrV), or bovine herpes virus type 1 (BHV-1) into cells. Glycoprotein D (gD) is essential for receptor-mediated entry of all three viruses into cells. However, the gD homolo...
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| Published in: | Virology (New York, N.Y.) N.Y.), 2001-02, Vol.280 (1), p.7-18 |
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| container_title | Virology (New York, N.Y.) |
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| creator | Connolly, Sarah A. Whitbeck, J.Charles Rux, Ann H. Krummenacher, Claude van Drunen Littel-van den Hurk, Sylvia Cohen, Gary H. Eisenberg, Roselyn J. |
| description | Distinct subsets of human receptors for alphaherpesviruses mediate the entry of herpes simplex virus (HSV), pseudorabies virus (PrV), or bovine herpes virus type 1 (BHV-1) into cells. Glycoprotein D (gD) is essential for receptor-mediated entry of all three viruses into cells. However, the gD homologs of these viruses share only 22–33% amino acid identity. Several entry receptors for HSV have been identified. Two of these, HveA (HVEM) and HveC (nectin-1), mediate entry of most HSV-1 and HSV-2 strains and are bound directly by HSV gD. A third receptor, HveB (nectin-2), mediates entry of HSV-2 and only a limited number of HSV-1 strains. HveB and HveC can also serve as entry receptors for PrV, whereas only HveC can serve this function for BHV-1. We show here that gD from PrV and BHV-1 binds directly to the human receptors that mediate PrV and BHV-1 entry. We expressed soluble forms of PrV gD and BHV-1 gD using recombinant baculoviruses and purified each protein. Using ELISA, we detected direct binding of PrV gD to HveB and HveC and direct binding of BHV-1 gD to HveC. Biosensor analysis revealed that PrV gD had a 10-fold higher affinity than HSV-1 gD for human HveC. In contrast, the binding of BHV-1 gD to HveC was weak. PrV gD and HSV-1 gD competed for binding to the V domain of HveC and both inhibited entry of the homologous and heterologous viruses. These data suggest that the two forms of gD bind to a common region on human HveC despite their low amino acid similarity. Based on affinities for human HveC, we predict a porcine HveC homolog may be important for PrV infection in its natural host, whereas a BHV-1 infection in its natural host may be mediated by a receptor other than a bovine HveC homolog. |
| doi_str_mv | 10.1006/viro.2000.0747 |
| format | article |
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Glycoprotein D (gD) is essential for receptor-mediated entry of all three viruses into cells. However, the gD homologs of these viruses share only 22–33% amino acid identity. Several entry receptors for HSV have been identified. Two of these, HveA (HVEM) and HveC (nectin-1), mediate entry of most HSV-1 and HSV-2 strains and are bound directly by HSV gD. A third receptor, HveB (nectin-2), mediates entry of HSV-2 and only a limited number of HSV-1 strains. HveB and HveC can also serve as entry receptors for PrV, whereas only HveC can serve this function for BHV-1. We show here that gD from PrV and BHV-1 binds directly to the human receptors that mediate PrV and BHV-1 entry. We expressed soluble forms of PrV gD and BHV-1 gD using recombinant baculoviruses and purified each protein. Using ELISA, we detected direct binding of PrV gD to HveB and HveC and direct binding of BHV-1 gD to HveC. Biosensor analysis revealed that PrV gD had a 10-fold higher affinity than HSV-1 gD for human HveC. In contrast, the binding of BHV-1 gD to HveC was weak. PrV gD and HSV-1 gD competed for binding to the V domain of HveC and both inhibited entry of the homologous and heterologous viruses. These data suggest that the two forms of gD bind to a common region on human HveC despite their low amino acid similarity. Based on affinities for human HveC, we predict a porcine HveC homolog may be important for PrV infection in its natural host, whereas a BHV-1 infection in its natural host may be mediated by a receptor other than a bovine HveC homolog.</description><identifier>ISSN: 0042-6822</identifier><identifier>EISSN: 1096-0341</identifier><identifier>DOI: 10.1006/viro.2000.0747</identifier><identifier>PMID: 11162814</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Antibodies, Monoclonal - metabolism ; Antibodies, Viral - metabolism ; BHV-1 ; Binding Sites ; Binding, Competitive ; Bovine herpesvirus 1 ; Cattle ; Cell Adhesion Molecules - metabolism ; Cell Line ; CHO Cells ; Cricetinae ; entry ; Enzyme-Linked Immunosorbent Assay - methods ; Glycoprotein D ; glycoprotein gD ; Herpes simplex virus 1 ; Herpesvirus 1, Bovine - metabolism ; Herpesvirus 1, Human - metabolism ; Herpesvirus 1, Suid - metabolism ; HSV ; Humans ; HveB ; HveC ; nectin-1 ; nectin-2 ; Nectins ; PrV ; Pseudorabies virus ; Receptors, Virus - metabolism ; Solubility ; Spodoptera - cytology ; Swine ; Viral Envelope Proteins - biosynthesis ; Viral Envelope Proteins - genetics ; Viral Envelope Proteins - metabolism ; Viral Proteins - biosynthesis ; Viral Proteins - genetics ; Viral Proteins - metabolism</subject><ispartof>Virology (New York, N.Y.), 2001-02, Vol.280 (1), p.7-18</ispartof><rights>2001 Academic Press</rights><rights>Copyright 2001 Academic Press.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c440t-2531a39d5d10d41881a0d45d826d01d2c123f7c93fc66ca8a6f2748e92db9f8d3</citedby><cites>FETCH-LOGICAL-c440t-2531a39d5d10d41881a0d45d826d01d2c123f7c93fc66ca8a6f2748e92db9f8d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,786,790,27957,27958</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11162814$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Connolly, Sarah A.</creatorcontrib><creatorcontrib>Whitbeck, J.Charles</creatorcontrib><creatorcontrib>Rux, Ann H.</creatorcontrib><creatorcontrib>Krummenacher, Claude</creatorcontrib><creatorcontrib>van Drunen Littel-van den Hurk, Sylvia</creatorcontrib><creatorcontrib>Cohen, Gary H.</creatorcontrib><creatorcontrib>Eisenberg, Roselyn J.</creatorcontrib><title>Glycoprotein D Homologs in Herpes Simplex Virus Type 1, Pseudorabies Virus, and Bovine Herpes Virus Type 1 Bind Directly to Human HveC (Nectin-1) with Different Affinities</title><title>Virology (New York, N.Y.)</title><addtitle>Virology</addtitle><description>Distinct subsets of human receptors for alphaherpesviruses mediate the entry of herpes simplex virus (HSV), pseudorabies virus (PrV), or bovine herpes virus type 1 (BHV-1) into cells. Glycoprotein D (gD) is essential for receptor-mediated entry of all three viruses into cells. However, the gD homologs of these viruses share only 22–33% amino acid identity. Several entry receptors for HSV have been identified. Two of these, HveA (HVEM) and HveC (nectin-1), mediate entry of most HSV-1 and HSV-2 strains and are bound directly by HSV gD. A third receptor, HveB (nectin-2), mediates entry of HSV-2 and only a limited number of HSV-1 strains. HveB and HveC can also serve as entry receptors for PrV, whereas only HveC can serve this function for BHV-1. We show here that gD from PrV and BHV-1 binds directly to the human receptors that mediate PrV and BHV-1 entry. We expressed soluble forms of PrV gD and BHV-1 gD using recombinant baculoviruses and purified each protein. Using ELISA, we detected direct binding of PrV gD to HveB and HveC and direct binding of BHV-1 gD to HveC. Biosensor analysis revealed that PrV gD had a 10-fold higher affinity than HSV-1 gD for human HveC. In contrast, the binding of BHV-1 gD to HveC was weak. PrV gD and HSV-1 gD competed for binding to the V domain of HveC and both inhibited entry of the homologous and heterologous viruses. These data suggest that the two forms of gD bind to a common region on human HveC despite their low amino acid similarity. Based on affinities for human HveC, we predict a porcine HveC homolog may be important for PrV infection in its natural host, whereas a BHV-1 infection in its natural host may be mediated by a receptor other than a bovine HveC homolog.</description><subject>Animals</subject><subject>Antibodies, Monoclonal - metabolism</subject><subject>Antibodies, Viral - metabolism</subject><subject>BHV-1</subject><subject>Binding Sites</subject><subject>Binding, Competitive</subject><subject>Bovine herpesvirus 1</subject><subject>Cattle</subject><subject>Cell Adhesion Molecules - metabolism</subject><subject>Cell Line</subject><subject>CHO Cells</subject><subject>Cricetinae</subject><subject>entry</subject><subject>Enzyme-Linked Immunosorbent Assay - methods</subject><subject>Glycoprotein D</subject><subject>glycoprotein gD</subject><subject>Herpes simplex virus 1</subject><subject>Herpesvirus 1, Bovine - metabolism</subject><subject>Herpesvirus 1, Human - metabolism</subject><subject>Herpesvirus 1, Suid - metabolism</subject><subject>HSV</subject><subject>Humans</subject><subject>HveB</subject><subject>HveC</subject><subject>nectin-1</subject><subject>nectin-2</subject><subject>Nectins</subject><subject>PrV</subject><subject>Pseudorabies virus</subject><subject>Receptors, Virus - metabolism</subject><subject>Solubility</subject><subject>Spodoptera - cytology</subject><subject>Swine</subject><subject>Viral Envelope Proteins - biosynthesis</subject><subject>Viral Envelope Proteins - genetics</subject><subject>Viral Envelope Proteins - metabolism</subject><subject>Viral Proteins - biosynthesis</subject><subject>Viral Proteins - genetics</subject><subject>Viral Proteins - metabolism</subject><issn>0042-6822</issn><issn>1096-0341</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><recordid>eNqFkUFv1DAQhS0EokvhyhH5hEBqlrGTdZxju4UuUgVIFK6W1x6DURKndrKwv4k_idNdBBfEaWTP995I7xHylMGSAYhXOx_DkgPAEuqqvkcWDBpRQFmx-2QBUPFCSM5PyKOUvmWqqmt4SE4YY4JLVi3Iz6t2b8IQw4i-p5d0E7rQhi-J5tcG44CJfvTd0OIP-tnHKdGb_YCUndEPCScbot76jNytzqjuLb0IO9_jb-3fGnrh8_7SRzRju6djoJup0_nMDtf0xbv86_uCvaTf_fg1Y85hxH6k58753o_5zGPywOk24ZPjPCWf3ry-WW-K6_dXb9fn14WpKhgLviqZLhu7sgxsxaRkOs-VlVxYYJYbxktXm6Z0RgijpRaO15XEhttt46QtT8nzg2-O5XbCNKrOJ4Ntq3sMU1I1iJJzCf8FWS2hFnwGlwfQxJBSRKeG6Dsd94qBmntUc49q7lHNPWbBs6PztO3Q_sGPxWVAHgDMQew8RpWMx96gvctX2eD_5f0LiyqsgA</recordid><startdate>20010201</startdate><enddate>20010201</enddate><creator>Connolly, Sarah A.</creator><creator>Whitbeck, J.Charles</creator><creator>Rux, Ann H.</creator><creator>Krummenacher, Claude</creator><creator>van Drunen Littel-van den Hurk, Sylvia</creator><creator>Cohen, Gary H.</creator><creator>Eisenberg, Roselyn J.</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</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>7U9</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>20010201</creationdate><title>Glycoprotein D Homologs in Herpes Simplex Virus Type 1, Pseudorabies Virus, and Bovine Herpes Virus Type 1 Bind Directly to Human HveC (Nectin-1) with Different Affinities</title><author>Connolly, Sarah A. ; 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Glycoprotein D (gD) is essential for receptor-mediated entry of all three viruses into cells. However, the gD homologs of these viruses share only 22–33% amino acid identity. Several entry receptors for HSV have been identified. Two of these, HveA (HVEM) and HveC (nectin-1), mediate entry of most HSV-1 and HSV-2 strains and are bound directly by HSV gD. A third receptor, HveB (nectin-2), mediates entry of HSV-2 and only a limited number of HSV-1 strains. HveB and HveC can also serve as entry receptors for PrV, whereas only HveC can serve this function for BHV-1. We show here that gD from PrV and BHV-1 binds directly to the human receptors that mediate PrV and BHV-1 entry. We expressed soluble forms of PrV gD and BHV-1 gD using recombinant baculoviruses and purified each protein. Using ELISA, we detected direct binding of PrV gD to HveB and HveC and direct binding of BHV-1 gD to HveC. Biosensor analysis revealed that PrV gD had a 10-fold higher affinity than HSV-1 gD for human HveC. In contrast, the binding of BHV-1 gD to HveC was weak. PrV gD and HSV-1 gD competed for binding to the V domain of HveC and both inhibited entry of the homologous and heterologous viruses. These data suggest that the two forms of gD bind to a common region on human HveC despite their low amino acid similarity. Based on affinities for human HveC, we predict a porcine HveC homolog may be important for PrV infection in its natural host, whereas a BHV-1 infection in its natural host may be mediated by a receptor other than a bovine HveC homolog.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>11162814</pmid><doi>10.1006/viro.2000.0747</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Virology (New York, N.Y.), 2001-02, Vol.280 (1), p.7-18 |
| issn | 0042-6822 1096-0341 |
| language | eng |
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| source | BACON - Elsevier - GLOBAL_SCIENCEDIRECT-OPENACCESS; ScienceDirect Freedom Collection 2022-2024 |
| subjects | Animals Antibodies, Monoclonal - metabolism Antibodies, Viral - metabolism BHV-1 Binding Sites Binding, Competitive Bovine herpesvirus 1 Cattle Cell Adhesion Molecules - metabolism Cell Line CHO Cells Cricetinae entry Enzyme-Linked Immunosorbent Assay - methods Glycoprotein D glycoprotein gD Herpes simplex virus 1 Herpesvirus 1, Bovine - metabolism Herpesvirus 1, Human - metabolism Herpesvirus 1, Suid - metabolism HSV Humans HveB HveC nectin-1 nectin-2 Nectins PrV Pseudorabies virus Receptors, Virus - metabolism Solubility Spodoptera - cytology Swine Viral Envelope Proteins - biosynthesis Viral Envelope Proteins - genetics Viral Envelope Proteins - metabolism Viral Proteins - biosynthesis Viral Proteins - genetics Viral Proteins - metabolism |
| title | Glycoprotein D Homologs in Herpes Simplex Virus Type 1, Pseudorabies Virus, and Bovine Herpes Virus Type 1 Bind Directly to Human HveC (Nectin-1) with Different Affinities |
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