| pubmed-article:11836420 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11836420 | lifeskim:mentions | umls-concept:C0206558 | lld:lifeskim |
| pubmed-article:11836420 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:11836420 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
| pubmed-article:11836420 | lifeskim:mentions | umls-concept:C0907734 | lld:lifeskim |
| pubmed-article:11836420 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:11836420 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:11836420 | pubmed:dateCreated | 2002-2-11 | lld:pubmed |
| pubmed-article:11836420 | pubmed:abstractText | Herpes simplex virus (HSV) entry requires the interaction between the envelope glycoprotein D (gD) and a cellular receptor such as nectin-1 (also named herpesvirus entry mediator C [HveC]) or HveA/HVEM. Nectin-1 is a cell adhesion molecule found at adherens junctions associated with the cytoplasmic actin-binding protein afadin. Nectin-1 can act as its own ligand in a homotypic interaction to bridge cells together. We used a cell aggregation assay to map an adhesive functional site on nectin-1 and identify the effects of gD binding and HSV early infection on nectin-1 function. Soluble forms of nectin-1 and anti-nectin-1 monoclonal antibodies were used to map a functional adhesive site within the first immunoglobulin-like domain (V domain) of nectin-1. This domain also contains the gD-binding site, which appeared to overlap the adhesive site. Thus, soluble forms of gD were able to prevent nectin-1-mediated cell aggregation and to disrupt cell clumps in an affinity-dependent manner. HSV also prevented nectin-1-mediated cell aggregation by occupying the receptor. Early in infection, nectin-1 was not downregulated from the cell surface. Rather, detection of nectin-1 changed gradually over a 30-min period of infection, as reflected by a decrease in the CK41 epitope and an increase in the CK35 epitope. The level of detection of virion gD on the cell surface increased within 5 min of infection in a receptor-dependent manner. These observations suggest that cell surface nectin-1 and gD may undergo conformational changes during HSV entry as part of an evolving interaction between the viral envelope and the cell plasma membrane. | lld:pubmed |
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| pubmed-article:11836420 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11836420 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11836420 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:11836420 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11836420 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:11836420 | pubmed:issn | 0022-538X | lld:pubmed |
| pubmed-article:11836420 | pubmed:author | pubmed-author:KrummenacherC... | lld:pubmed |
| pubmed-article:11836420 | pubmed:author | pubmed-author:BaribaudIsabe... | lld:pubmed |
| pubmed-article:11836420 | pubmed:author | pubmed-author:SanzoJames... | lld:pubmed |
| pubmed-article:11836420 | pubmed:author | pubmed-author:CohenGary HGH | lld:pubmed |
| pubmed-article:11836420 | pubmed:author | pubmed-author:EisenbergRose... | lld:pubmed |
| pubmed-article:11836420 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11836420 | pubmed:volume | 76 | lld:pubmed |
| pubmed-article:11836420 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11836420 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11836420 | pubmed:pagination | 2424-33 | lld:pubmed |
| pubmed-article:11836420 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:11836420 | pubmed:meshHeading | pubmed-meshheading:11836420... | lld:pubmed |
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| pubmed-article:11836420 | pubmed:meshHeading | pubmed-meshheading:11836420... | lld:pubmed |
| pubmed-article:11836420 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:11836420 | pubmed:articleTitle | Effects of herpes simplex virus on structure and function of nectin-1/HveC. | lld:pubmed |
| pubmed-article:11836420 | pubmed:affiliation | Department of Microbiology, School of Dental Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA. krumm@biochem.dental.upenn.edu | lld:pubmed |
| pubmed-article:11836420 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11836420 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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