Herpes Simplex Virus Glycoproteins Associated with Different Morphological Entities Projecting from the Virion Envelope
1 Department of Medical Microbiology, University of Cape Town Medical School, Observatory, Cape Town, South Africa 7925 and 2 Department of Molecular Genetics and Cell Biology and Committee on Virology, University of Chicago, 910 East 58th Street, Chicago, Illinois 60637, U.S.A. Spikes of different...
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Veröffentlicht in: | Journal of general virology 1987-03, Vol.68 (3), p.715-725 |
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creator | Stannard, Linda M Fuller, A. Oveta Spear, Patricia G |
description | 1 Department of Medical Microbiology, University of Cape Town Medical School, Observatory, Cape Town, South Africa 7925
and 2 Department of Molecular Genetics and Cell Biology and Committee on Virology, University of Chicago, 910 East 58th Street, Chicago, Illinois 60637, U.S.A.
Spikes of different kinds, distinct in size and appearance were detected on the surfaces of herpes simplex virions by electron microscopy of negatively stained preparations. Use of monoclonal antibodies coupled to colloidal gold permitted identification of viral glycoproteins present in different structures projecting from the virion envelope. Antibodies specific for the glycoprotein designated gB bound to the most prominent spikes, which were about 14 nm long and, in side view, had a flattened T-shaped top. Antibodies specific for gC bound to structures that, in some instances, appeared to extend as much as 24 nm from the surface of the envelope and were too thin to resolve. Antibodies specific for gD bound to structures that extended as much as 8 to 10 nm from the surface of the envelope. The gB spikes were invariably clustered, usually in protrusions of the envelope varying from small bulbous distentions to long tail-like projections. The gC components were randomly distributed and widely spaced and the gD components were irregularly clustered in patterns distinct from those of the gB spikes. These three glycoproteins therefore form structures that are different in size, morphology and distribution in the envelope.
Keywords: HSV-1, electron microscopy, spikes
Received 11 July 1986;
accepted 12 November 1986. |
doi_str_mv | 10.1099/0022-1317-68-3-715 |
format | Article |
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and 2 Department of Molecular Genetics and Cell Biology and Committee on Virology, University of Chicago, 910 East 58th Street, Chicago, Illinois 60637, U.S.A.
Spikes of different kinds, distinct in size and appearance were detected on the surfaces of herpes simplex virions by electron microscopy of negatively stained preparations. Use of monoclonal antibodies coupled to colloidal gold permitted identification of viral glycoproteins present in different structures projecting from the virion envelope. Antibodies specific for the glycoprotein designated gB bound to the most prominent spikes, which were about 14 nm long and, in side view, had a flattened T-shaped top. Antibodies specific for gC bound to structures that, in some instances, appeared to extend as much as 24 nm from the surface of the envelope and were too thin to resolve. Antibodies specific for gD bound to structures that extended as much as 8 to 10 nm from the surface of the envelope. The gB spikes were invariably clustered, usually in protrusions of the envelope varying from small bulbous distentions to long tail-like projections. The gC components were randomly distributed and widely spaced and the gD components were irregularly clustered in patterns distinct from those of the gB spikes. These three glycoproteins therefore form structures that are different in size, morphology and distribution in the envelope.
Keywords: HSV-1, electron microscopy, spikes
Received 11 July 1986;
accepted 12 November 1986.</description><identifier>ISSN: 0022-1317</identifier><identifier>EISSN: 1465-2099</identifier><identifier>DOI: 10.1099/0022-1317-68-3-715</identifier><identifier>PMID: 3029300</identifier><identifier>CODEN: JGVIAY</identifier><language>eng</language><publisher>Reading: Soc General Microbiol</publisher><subject>Antibodies, Monoclonal ; Antigen-Antibody Complex ; Biological and medical sciences ; Cells, Cultured ; Embryo, Mammalian ; Fundamental and applied biological sciences. Psychology ; Glycoproteins - analysis ; herpes simplex virus 1 ; Humans ; Microbiology ; Microscopy, Electron ; Morphology, structure, chemical composition, physicochemical properties ; Simplexvirus - ultrastructure ; Viral Proteins - analysis ; Virion - ultrastructure ; Virology</subject><ispartof>Journal of general virology, 1987-03, Vol.68 (3), p.715-725</ispartof><rights>1987 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c434t-3a32d11a3428df3c62502eed04c7d98900e80d2c491b73b4d2f73f67330f29443</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,3733,3734,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=8154627$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3029300$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Stannard, Linda M</creatorcontrib><creatorcontrib>Fuller, A. Oveta</creatorcontrib><creatorcontrib>Spear, Patricia G</creatorcontrib><title>Herpes Simplex Virus Glycoproteins Associated with Different Morphological Entities Projecting from the Virion Envelope</title><title>Journal of general virology</title><addtitle>J Gen Virol</addtitle><description>1 Department of Medical Microbiology, University of Cape Town Medical School, Observatory, Cape Town, South Africa 7925
and 2 Department of Molecular Genetics and Cell Biology and Committee on Virology, University of Chicago, 910 East 58th Street, Chicago, Illinois 60637, U.S.A.
Spikes of different kinds, distinct in size and appearance were detected on the surfaces of herpes simplex virions by electron microscopy of negatively stained preparations. Use of monoclonal antibodies coupled to colloidal gold permitted identification of viral glycoproteins present in different structures projecting from the virion envelope. Antibodies specific for the glycoprotein designated gB bound to the most prominent spikes, which were about 14 nm long and, in side view, had a flattened T-shaped top. Antibodies specific for gC bound to structures that, in some instances, appeared to extend as much as 24 nm from the surface of the envelope and were too thin to resolve. Antibodies specific for gD bound to structures that extended as much as 8 to 10 nm from the surface of the envelope. The gB spikes were invariably clustered, usually in protrusions of the envelope varying from small bulbous distentions to long tail-like projections. The gC components were randomly distributed and widely spaced and the gD components were irregularly clustered in patterns distinct from those of the gB spikes. These three glycoproteins therefore form structures that are different in size, morphology and distribution in the envelope.
Keywords: HSV-1, electron microscopy, spikes
Received 11 July 1986;
accepted 12 November 1986.</description><subject>Antibodies, Monoclonal</subject><subject>Antigen-Antibody Complex</subject><subject>Biological and medical sciences</subject><subject>Cells, Cultured</subject><subject>Embryo, Mammalian</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glycoproteins - analysis</subject><subject>herpes simplex virus 1</subject><subject>Humans</subject><subject>Microbiology</subject><subject>Microscopy, Electron</subject><subject>Morphology, structure, chemical composition, physicochemical properties</subject><subject>Simplexvirus - ultrastructure</subject><subject>Viral Proteins - analysis</subject><subject>Virion - ultrastructure</subject><subject>Virology</subject><issn>0022-1317</issn><issn>1465-2099</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1987</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUtv1DAUhS0EKtPCH0BC8gLBKtSvxMmyKqVFalUkHlsr41xPbpXEwfZ02n9fRzOaLSsvznfP9T2HkA-cfeWsac4ZE6LgkuuiqgtZaF6-IiuuqrIQWX5NVkfgLTmN8YExrlSpT8iJZKKRjK3I7gbCDJH-wnEe4In-xbCN9Hp4tn4OPgFOkV7E6C22CTq6w9TTb-gcBJgSvfNh7v3gN2jbgV5NCRNms5_BP4BNOG2oC36kqYfFGP2UmUcY_AzvyBvXDhHeH94z8uf71e_Lm-L2_vrH5cVtYZVUqZCtFB3nrVSi7py0lSiZAOiYsrpr6oYxqFknrGr4Wsu16oTT0lVaSuZEo5Q8I5_3vvmaf1uIyYwYLQxDO4HfRqO1WjJh_wW50qwq6zKDYg_a4GMM4MwccGzDs-HMLLWYJXWzpG6q2kiTa8lDHw_u2_UI3XHk0EPWPx30NuYoXWgni_GI1bxUldAZ-7LHetz0OwxgNjCNmH-yRm8eMRwXvgAIx6Ob</recordid><startdate>19870301</startdate><enddate>19870301</enddate><creator>Stannard, Linda M</creator><creator>Fuller, A. Oveta</creator><creator>Spear, Patricia G</creator><general>Soc General Microbiol</general><general>Society for General Microbiology</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>7U9</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>19870301</creationdate><title>Herpes Simplex Virus Glycoproteins Associated with Different Morphological Entities Projecting from the Virion Envelope</title><author>Stannard, Linda M ; Fuller, A. Oveta ; Spear, Patricia G</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c434t-3a32d11a3428df3c62502eed04c7d98900e80d2c491b73b4d2f73f67330f29443</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1987</creationdate><topic>Antibodies, Monoclonal</topic><topic>Antigen-Antibody Complex</topic><topic>Biological and medical sciences</topic><topic>Cells, Cultured</topic><topic>Embryo, Mammalian</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Glycoproteins - analysis</topic><topic>herpes simplex virus 1</topic><topic>Humans</topic><topic>Microbiology</topic><topic>Microscopy, Electron</topic><topic>Morphology, structure, chemical composition, physicochemical properties</topic><topic>Simplexvirus - ultrastructure</topic><topic>Viral Proteins - analysis</topic><topic>Virion - ultrastructure</topic><topic>Virology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Stannard, Linda M</creatorcontrib><creatorcontrib>Fuller, A. Oveta</creatorcontrib><creatorcontrib>Spear, Patricia G</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>Virology and AIDS Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of general virology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Stannard, Linda M</au><au>Fuller, A. Oveta</au><au>Spear, Patricia G</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Herpes Simplex Virus Glycoproteins Associated with Different Morphological Entities Projecting from the Virion Envelope</atitle><jtitle>Journal of general virology</jtitle><addtitle>J Gen Virol</addtitle><date>1987-03-01</date><risdate>1987</risdate><volume>68</volume><issue>3</issue><spage>715</spage><epage>725</epage><pages>715-725</pages><issn>0022-1317</issn><eissn>1465-2099</eissn><coden>JGVIAY</coden><abstract>1 Department of Medical Microbiology, University of Cape Town Medical School, Observatory, Cape Town, South Africa 7925
and 2 Department of Molecular Genetics and Cell Biology and Committee on Virology, University of Chicago, 910 East 58th Street, Chicago, Illinois 60637, U.S.A.
Spikes of different kinds, distinct in size and appearance were detected on the surfaces of herpes simplex virions by electron microscopy of negatively stained preparations. Use of monoclonal antibodies coupled to colloidal gold permitted identification of viral glycoproteins present in different structures projecting from the virion envelope. Antibodies specific for the glycoprotein designated gB bound to the most prominent spikes, which were about 14 nm long and, in side view, had a flattened T-shaped top. Antibodies specific for gC bound to structures that, in some instances, appeared to extend as much as 24 nm from the surface of the envelope and were too thin to resolve. Antibodies specific for gD bound to structures that extended as much as 8 to 10 nm from the surface of the envelope. The gB spikes were invariably clustered, usually in protrusions of the envelope varying from small bulbous distentions to long tail-like projections. The gC components were randomly distributed and widely spaced and the gD components were irregularly clustered in patterns distinct from those of the gB spikes. These three glycoproteins therefore form structures that are different in size, morphology and distribution in the envelope.
Keywords: HSV-1, electron microscopy, spikes
Received 11 July 1986;
accepted 12 November 1986.</abstract><cop>Reading</cop><pub>Soc General Microbiol</pub><pmid>3029300</pmid><doi>10.1099/0022-1317-68-3-715</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Antibodies, Monoclonal Antigen-Antibody Complex Biological and medical sciences Cells, Cultured Embryo, Mammalian Fundamental and applied biological sciences. Psychology Glycoproteins - analysis herpes simplex virus 1 Humans Microbiology Microscopy, Electron Morphology, structure, chemical composition, physicochemical properties Simplexvirus - ultrastructure Viral Proteins - analysis Virion - ultrastructure Virology |
title | Herpes Simplex Virus Glycoproteins Associated with Different Morphological Entities Projecting from the Virion Envelope |
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