Human cytomegalovirus structural components: intracellular and intraviral localization of p28 and p65-69 by immunoelectron microscopy
Using specific monoclonal antibodies, we have localized two structural proteins (p65-69 and p28) of human cytomegalovirus in infected cells and in virions and/or virus-related particles by immunoelectron microscopy using protein A-gold. Protein p65-69 is present in some roundish structures in the nu...
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Veröffentlicht in: | Virus research 1987-07, Vol.8 (1), p.15-23 |
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description | Using specific monoclonal antibodies, we have localized two structural proteins (p65-69 and p28) of human cytomegalovirus in infected cells and in virions and/or virus-related particles by immunoelectron microscopy using protein A-gold. Protein p65-69 is present in some roundish structures in the nuclei, often in contact with the viroplasm, and in the cytoplasm, exclusively within the dense body matrix. Protein p28 is present only in the outline of cytoplasmic capsids, and reaches the highest density in the large aggregates of virions and dense bodies which are particularly numerous during the late phases of the viral replication cycle. |
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P ; SEVERI, B ; FURLINI, G ; BADIALI DE GIORGI, L</creator><creatorcontrib>LANDINI, M. P ; SEVERI, B ; FURLINI, G ; BADIALI DE GIORGI, L</creatorcontrib><description>Using specific monoclonal antibodies, we have localized two structural proteins (p65-69 and p28) of human cytomegalovirus in infected cells and in virions and/or virus-related particles by immunoelectron microscopy using protein A-gold. Protein p65-69 is present in some roundish structures in the nuclei, often in contact with the viroplasm, and in the cytoplasm, exclusively within the dense body matrix. Protein p28 is present only in the outline of cytoplasmic capsids, and reaches the highest density in the large aggregates of virions and dense bodies which are particularly numerous during the late phases of the viral replication cycle.</description><identifier>ISSN: 0168-1702</identifier><identifier>EISSN: 1872-7492</identifier><identifier>PMID: 2821705</identifier><identifier>CODEN: VIREDF</identifier><language>eng</language><publisher>London: Elsevier</publisher><subject>Antibodies, Monoclonal ; Biological and medical sciences ; Capsid - metabolism ; Cell Nucleus - microbiology ; Cells, Cultured ; Cytomegalovirus - growth & development ; Cytomegalovirus - ultrastructure ; Cytoplasm - microbiology ; Fundamental and applied biological sciences. Psychology ; Humans ; Immunohistochemistry ; Microbiology ; Microscopy, Electron ; Morphology, structure, chemical composition, physicochemical properties ; Viral Proteins - immunology ; Viral Proteins - metabolism ; Virion - ultrastructure ; Virology</subject><ispartof>Virus research, 1987-07, Vol.8 (1), p.15-23</ispartof><rights>1987 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=8332603$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2821705$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>LANDINI, M. P</creatorcontrib><creatorcontrib>SEVERI, B</creatorcontrib><creatorcontrib>FURLINI, G</creatorcontrib><creatorcontrib>BADIALI DE GIORGI, L</creatorcontrib><title>Human cytomegalovirus structural components: intracellular and intraviral localization of p28 and p65-69 by immunoelectron microscopy</title><title>Virus research</title><addtitle>Virus Res</addtitle><description>Using specific monoclonal antibodies, we have localized two structural proteins (p65-69 and p28) of human cytomegalovirus in infected cells and in virions and/or virus-related particles by immunoelectron microscopy using protein A-gold. Protein p65-69 is present in some roundish structures in the nuclei, often in contact with the viroplasm, and in the cytoplasm, exclusively within the dense body matrix. Protein p28 is present only in the outline of cytoplasmic capsids, and reaches the highest density in the large aggregates of virions and dense bodies which are particularly numerous during the late phases of the viral replication cycle.</description><subject>Antibodies, Monoclonal</subject><subject>Biological and medical sciences</subject><subject>Capsid - metabolism</subject><subject>Cell Nucleus - microbiology</subject><subject>Cells, Cultured</subject><subject>Cytomegalovirus - growth & development</subject><subject>Cytomegalovirus - ultrastructure</subject><subject>Cytoplasm - microbiology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Humans</subject><subject>Immunohistochemistry</subject><subject>Microbiology</subject><subject>Microscopy, Electron</subject><subject>Morphology, structure, chemical composition, physicochemical properties</subject><subject>Viral Proteins - immunology</subject><subject>Viral Proteins - metabolism</subject><subject>Virion - ultrastructure</subject><subject>Virology</subject><issn>0168-1702</issn><issn>1872-7492</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1987</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kEtLxDAUhYso4zj6E4QsxF0hTfpI3MngCwZc6L7cpqlE8qh5CHXv_zY6g5t74ZzvXjjnqFhXrCNlV3NyXKxx1bKy6jA5Lc5CeMcYt7RrV8WKMJLlZl18PyYDFoklOiPfQLtP5VNAIfokYvKgkXBmdlbaGG6QstGDkFonDR6BHfdKvsmgdgK0-oKonEVuQjNhf8jcNmXL0bAgZUyyTmopos-MUcK7INy8nBcnE-ggLw57U7zc371uH8vd88PT9nZXzow0JW_kgDmGaeSDqAbKCYccBxORZ81pBaxmAx-GjoipaSkFwUF0jGAx1hPQTXG9_zp795FkiL1R4TcNWOlS6FmF69xKncHLA5gGI8d-9sqAX_pDa9m_OvgQcubJgxUq_GOMUtJiSn8AyWF5UA</recordid><startdate>198707</startdate><enddate>198707</enddate><creator>LANDINI, M. P</creator><creator>SEVERI, B</creator><creator>FURLINI, G</creator><creator>BADIALI DE GIORGI, L</creator><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>7X8</scope></search><sort><creationdate>198707</creationdate><title>Human cytomegalovirus structural components: intracellular and intraviral localization of p28 and p65-69 by immunoelectron microscopy</title><author>LANDINI, M. P ; SEVERI, B ; FURLINI, G ; BADIALI DE GIORGI, L</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p825-95eb090afd9bc1b3929a37602c3764931a848b9bb72cf5633ac9ac7820cd4fa3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1987</creationdate><topic>Antibodies, Monoclonal</topic><topic>Biological and medical sciences</topic><topic>Capsid - metabolism</topic><topic>Cell Nucleus - microbiology</topic><topic>Cells, Cultured</topic><topic>Cytomegalovirus - growth & development</topic><topic>Cytomegalovirus - ultrastructure</topic><topic>Cytoplasm - microbiology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Humans</topic><topic>Immunohistochemistry</topic><topic>Microbiology</topic><topic>Microscopy, Electron</topic><topic>Morphology, structure, chemical composition, physicochemical properties</topic><topic>Viral Proteins - immunology</topic><topic>Viral Proteins - metabolism</topic><topic>Virion - ultrastructure</topic><topic>Virology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>LANDINI, M. P</creatorcontrib><creatorcontrib>SEVERI, B</creatorcontrib><creatorcontrib>FURLINI, G</creatorcontrib><creatorcontrib>BADIALI DE GIORGI, L</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>MEDLINE - Academic</collection><jtitle>Virus research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>LANDINI, M. P</au><au>SEVERI, B</au><au>FURLINI, G</au><au>BADIALI DE GIORGI, L</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Human cytomegalovirus structural components: intracellular and intraviral localization of p28 and p65-69 by immunoelectron microscopy</atitle><jtitle>Virus research</jtitle><addtitle>Virus Res</addtitle><date>1987-07</date><risdate>1987</risdate><volume>8</volume><issue>1</issue><spage>15</spage><epage>23</epage><pages>15-23</pages><issn>0168-1702</issn><eissn>1872-7492</eissn><coden>VIREDF</coden><abstract>Using specific monoclonal antibodies, we have localized two structural proteins (p65-69 and p28) of human cytomegalovirus in infected cells and in virions and/or virus-related particles by immunoelectron microscopy using protein A-gold. Protein p65-69 is present in some roundish structures in the nuclei, often in contact with the viroplasm, and in the cytoplasm, exclusively within the dense body matrix. Protein p28 is present only in the outline of cytoplasmic capsids, and reaches the highest density in the large aggregates of virions and dense bodies which are particularly numerous during the late phases of the viral replication cycle.</abstract><cop>London</cop><cop>Shannon</cop><cop>Amsterdam</cop><pub>Elsevier</pub><pmid>2821705</pmid><tpages>9</tpages></addata></record> |
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subjects | Antibodies, Monoclonal Biological and medical sciences Capsid - metabolism Cell Nucleus - microbiology Cells, Cultured Cytomegalovirus - growth & development Cytomegalovirus - ultrastructure Cytoplasm - microbiology Fundamental and applied biological sciences. Psychology Humans Immunohistochemistry Microbiology Microscopy, Electron Morphology, structure, chemical composition, physicochemical properties Viral Proteins - immunology Viral Proteins - metabolism Virion - ultrastructure Virology |
title | Human cytomegalovirus structural components: intracellular and intraviral localization of p28 and p65-69 by immunoelectron microscopy |
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