Induction of conformational changes at the N-terminus of herpes simplex virus glycoprotein D upon binding to HVEM and nectin-1
Abstract Herpes simplex virus entry is initiated by glycoprotein D (gD) binding to a cellular receptor, such as HVEM or nectin-1. gD is activated by receptor-induced displacement of the C-terminus from the core of the glycoprotein. Binding of HVEM requires the formation of an N-terminal hairpin loop...
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| Veröffentlicht in: | Virology (New York, N.Y.) N.Y.), 2014-01, Vol.448, p.185-195 |
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| creator | Lazear, Eric Whitbeck, J. Charles Zuo, Yi Carfí, Andrea Cohen, Gary H Eisenberg, Roselyn J Krummenacher, Claude |
| description | Abstract Herpes simplex virus entry is initiated by glycoprotein D (gD) binding to a cellular receptor, such as HVEM or nectin-1. gD is activated by receptor-induced displacement of the C-terminus from the core of the glycoprotein. Binding of HVEM requires the formation of an N-terminal hairpin loop of gD; once formed this loop masks the nectin-1 binding site on the core of gD. We found that HVEM and nectin-1 exhibit non-reciprocal competition for binding to gD. The N-terminus of gD does not spontaneously form a stable hairpin in the absence of receptor and HVEM does not appear to rely on a pre-existing hairpin for binding to gD(3C–38C) mutants. However, HVEM function is affected by mutations that impair optimal hairpin formation. Furthermore, nectin-1 induces a new conformation of the N-terminus of gD. We conclude that the conformation of the N-terminus of gD is actively modified by the direct action of both receptors. |
| doi_str_mv | 10.1016/j.virol.2013.10.019 |
| format | Article |
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Charles ; Zuo, Yi ; Carfí, Andrea ; Cohen, Gary H ; Eisenberg, Roselyn J ; Krummenacher, Claude</creator><creatorcontrib>Lazear, Eric ; Whitbeck, J. Charles ; Zuo, Yi ; Carfí, Andrea ; Cohen, Gary H ; Eisenberg, Roselyn J ; Krummenacher, Claude</creatorcontrib><description>Abstract Herpes simplex virus entry is initiated by glycoprotein D (gD) binding to a cellular receptor, such as HVEM or nectin-1. gD is activated by receptor-induced displacement of the C-terminus from the core of the glycoprotein. Binding of HVEM requires the formation of an N-terminal hairpin loop of gD; once formed this loop masks the nectin-1 binding site on the core of gD. We found that HVEM and nectin-1 exhibit non-reciprocal competition for binding to gD. The N-terminus of gD does not spontaneously form a stable hairpin in the absence of receptor and HVEM does not appear to rely on a pre-existing hairpin for binding to gD(3C–38C) mutants. However, HVEM function is affected by mutations that impair optimal hairpin formation. Furthermore, nectin-1 induces a new conformation of the N-terminus of gD. We conclude that the conformation of the N-terminus of gD is actively modified by the direct action of both receptors.</description><identifier>ISSN: 0042-6822</identifier><identifier>EISSN: 1096-0341</identifier><identifier>DOI: 10.1016/j.virol.2013.10.019</identifier><identifier>PMID: 24314649</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Motifs ; Cell Adhesion Molecules - genetics ; Cell Adhesion Molecules - metabolism ; Cell Line ; Glycoproteins ; Herpes Simplex - genetics ; Herpes Simplex - metabolism ; Herpes Simplex - virology ; Herpes simplex virus ; Herpesvirus 1, Human - chemistry ; Herpesvirus 1, Human - genetics ; Herpesvirus 1, Human - metabolism ; Humans ; HVEM ; Infectious Disease ; Nectin ; Nectins ; Protein Binding ; Protein Conformation ; Receptors ; Receptors, Tumor Necrosis Factor, Member 14 - genetics ; Receptors, Tumor Necrosis Factor, Member 14 - metabolism ; Structure ; Viral Envelope Proteins - chemistry ; Viral Envelope Proteins - genetics ; Viral Envelope Proteins - metabolism ; Virus entry</subject><ispartof>Virology (New York, N.Y.), 2014-01, Vol.448, p.185-195</ispartof><rights>Elsevier Inc.</rights><rights>2013 Elsevier Inc.</rights><rights>2013 Published by Elsevier Inc.</rights><rights>2013 Elsevier Inc. All rights reserved. 2013</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c613t-1dc6dee07cd4cfe2d99f13701e81766442428e6f881c561caf5c824fe526a3d3</citedby><cites>FETCH-LOGICAL-c613t-1dc6dee07cd4cfe2d99f13701e81766442428e6f881c561caf5c824fe526a3d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.virol.2013.10.019$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>230,314,780,784,885,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24314649$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lazear, Eric</creatorcontrib><creatorcontrib>Whitbeck, J. Charles</creatorcontrib><creatorcontrib>Zuo, Yi</creatorcontrib><creatorcontrib>Carfí, Andrea</creatorcontrib><creatorcontrib>Cohen, Gary H</creatorcontrib><creatorcontrib>Eisenberg, Roselyn J</creatorcontrib><creatorcontrib>Krummenacher, Claude</creatorcontrib><title>Induction of conformational changes at the N-terminus of herpes simplex virus glycoprotein D upon binding to HVEM and nectin-1</title><title>Virology (New York, N.Y.)</title><addtitle>Virology</addtitle><description>Abstract Herpes simplex virus entry is initiated by glycoprotein D (gD) binding to a cellular receptor, such as HVEM or nectin-1. gD is activated by receptor-induced displacement of the C-terminus from the core of the glycoprotein. Binding of HVEM requires the formation of an N-terminal hairpin loop of gD; once formed this loop masks the nectin-1 binding site on the core of gD. We found that HVEM and nectin-1 exhibit non-reciprocal competition for binding to gD. The N-terminus of gD does not spontaneously form a stable hairpin in the absence of receptor and HVEM does not appear to rely on a pre-existing hairpin for binding to gD(3C–38C) mutants. However, HVEM function is affected by mutations that impair optimal hairpin formation. Furthermore, nectin-1 induces a new conformation of the N-terminus of gD. We conclude that the conformation of the N-terminus of gD is actively modified by the direct action of both receptors.</description><subject>Amino Acid Motifs</subject><subject>Cell Adhesion Molecules - genetics</subject><subject>Cell Adhesion Molecules - metabolism</subject><subject>Cell Line</subject><subject>Glycoproteins</subject><subject>Herpes Simplex - genetics</subject><subject>Herpes Simplex - metabolism</subject><subject>Herpes Simplex - virology</subject><subject>Herpes simplex virus</subject><subject>Herpesvirus 1, Human - chemistry</subject><subject>Herpesvirus 1, Human - genetics</subject><subject>Herpesvirus 1, Human - metabolism</subject><subject>Humans</subject><subject>HVEM</subject><subject>Infectious Disease</subject><subject>Nectin</subject><subject>Nectins</subject><subject>Protein Binding</subject><subject>Protein Conformation</subject><subject>Receptors</subject><subject>Receptors, Tumor Necrosis Factor, Member 14 - genetics</subject><subject>Receptors, Tumor Necrosis Factor, Member 14 - metabolism</subject><subject>Structure</subject><subject>Viral Envelope Proteins - chemistry</subject><subject>Viral Envelope Proteins - genetics</subject><subject>Viral Envelope Proteins - metabolism</subject><subject>Virus entry</subject><issn>0042-6822</issn><issn>1096-0341</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFUk1v1DAQjRCILoVfgIR85JLFYztOcqASagutVOBAxdVy7cmul8QOdlKxF347Dlsq4NLTaGbevPl4UxQvga6BgnyzW9-6GPo1o8BzZE2hfVSsgLaypFzA42JFqWClbBg7Kp6ltKPZr2v6tDhigoOQol0VPy-9nc3kgiehIyb4LsRBL77uidlqv8FE9ESmLZJP5YRxcH5OC3aLccy55Iaxxx8kz5Ljm35vwhjDhM6TMzKPmffGeev8hkyBXHw9_0i0t8Rj7ulLeF486XSf8MWdPS6u359fn16UV58_XJ6-uyqNBD6VYI20iLQ2VpgOmW3bDnhNARuopRSCCdag7JoGTCXB6K4yDRMdVkxqbvlxcXKgHeebAa1BP0XdqzG6Qce9CtqpfzPebdUm3Cre1i0XIhO8viOI4fuMaVKDSwb7XnsMc1JQgawrqJr2YaiQNZUNbWmG8gPUxJBSxO5-IqBq0Vjt1G-N1aLxEswa56pXfy9zX_NH1Ax4ewBgvuitw6iScegNWhfz3ZUN7oEGJ__Vm955Z3T_DfeYdmGO-TvyJioxRdWX5c2WLwNOaVW3Ff8FN6fQJw</recordid><startdate>20140105</startdate><enddate>20140105</enddate><creator>Lazear, Eric</creator><creator>Whitbeck, J. 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Charles ; Zuo, Yi ; Carfí, Andrea ; Cohen, Gary H ; Eisenberg, Roselyn J ; Krummenacher, Claude</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c613t-1dc6dee07cd4cfe2d99f13701e81766442428e6f881c561caf5c824fe526a3d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Amino Acid Motifs</topic><topic>Cell Adhesion Molecules - genetics</topic><topic>Cell Adhesion Molecules - metabolism</topic><topic>Cell Line</topic><topic>Glycoproteins</topic><topic>Herpes Simplex - genetics</topic><topic>Herpes Simplex - metabolism</topic><topic>Herpes Simplex - virology</topic><topic>Herpes simplex virus</topic><topic>Herpesvirus 1, Human - chemistry</topic><topic>Herpesvirus 1, Human - genetics</topic><topic>Herpesvirus 1, Human - metabolism</topic><topic>Humans</topic><topic>HVEM</topic><topic>Infectious Disease</topic><topic>Nectin</topic><topic>Nectins</topic><topic>Protein Binding</topic><topic>Protein Conformation</topic><topic>Receptors</topic><topic>Receptors, Tumor Necrosis Factor, Member 14 - genetics</topic><topic>Receptors, Tumor Necrosis Factor, Member 14 - metabolism</topic><topic>Structure</topic><topic>Viral Envelope Proteins - chemistry</topic><topic>Viral Envelope Proteins - genetics</topic><topic>Viral Envelope Proteins - metabolism</topic><topic>Virus entry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lazear, Eric</creatorcontrib><creatorcontrib>Whitbeck, J. 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| ispartof | Virology (New York, N.Y.), 2014-01, Vol.448, p.185-195 |
| issn | 0042-6822 1096-0341 |
| language | eng |
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| source | MEDLINE; Access via ScienceDirect (Elsevier); EZB Electronic Journals Library |
| subjects | Amino Acid Motifs Cell Adhesion Molecules - genetics Cell Adhesion Molecules - metabolism Cell Line Glycoproteins Herpes Simplex - genetics Herpes Simplex - metabolism Herpes Simplex - virology Herpes simplex virus Herpesvirus 1, Human - chemistry Herpesvirus 1, Human - genetics Herpesvirus 1, Human - metabolism Humans HVEM Infectious Disease Nectin Nectins Protein Binding Protein Conformation Receptors Receptors, Tumor Necrosis Factor, Member 14 - genetics Receptors, Tumor Necrosis Factor, Member 14 - metabolism Structure Viral Envelope Proteins - chemistry Viral Envelope Proteins - genetics Viral Envelope Proteins - metabolism Virus entry |
| title | Induction of conformational changes at the N-terminus of herpes simplex virus glycoprotein D upon binding to HVEM and nectin-1 |
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