Source:http://linkedlifedata.com/resource/pubmed/id/19665490
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2009-9-7
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pubmed:abstractText |
Herpes simplex virus type-1 (HSV-1) causes significant health problems from periodic skin and corneal lesions to encephalitis. It is also considered a cofactor in the development of age-related secondary glaucoma. Inhibition of HSV-1 at the stage of viral entry generates a unique opportunity for preventative and/or therapeutic intervention. Here we provide evidence that a sugar binding antiviral protein, cyanovirin-N (CV-N), can act as a potent inhibitor of HSV-1 entry into natural target cells. Inhibition of entry was independent of HSV-1 gD receptor usage and it was observed in transformed as well as primary cell cultures. Evidence presented herein suggests that CV-N can not only block virus entry to cells but also, it is capable of significantly inhibiting membrane fusion mediated by HSV glycoproteins. While CV-N treated virions were significantly deficient in entering into cells, HSV-1 glycoproteins-expressing cells pretreated with CV-N demonstrated reduced cell-to-cell fusion and polykaryocytes formation. The observation that CV-N can block both entry as well as membrane fusion suggests a stronger potential for this compound in antiviral therapy against HSV-1.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
1872-9096
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:volume |
84
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
67-75
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pubmed:dateRevised |
2011-5-27
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pubmed:meshHeading |
pubmed-meshheading:19665490-Animals,
pubmed-meshheading:19665490-Antiviral Agents,
pubmed-meshheading:19665490-Bacterial Proteins,
pubmed-meshheading:19665490-CHO Cells,
pubmed-meshheading:19665490-Carrier Proteins,
pubmed-meshheading:19665490-Cell Line,
pubmed-meshheading:19665490-Cricetinae,
pubmed-meshheading:19665490-Cricetulus,
pubmed-meshheading:19665490-Herpes Simplex,
pubmed-meshheading:19665490-Herpesvirus 1, Human,
pubmed-meshheading:19665490-Humans,
pubmed-meshheading:19665490-Membrane Fusion,
pubmed-meshheading:19665490-Virus Internalization
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pubmed:year |
2009
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pubmed:articleTitle |
A sugar binding protein cyanovirin-N blocks herpes simplex virus type-1 entry and cell fusion.
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pubmed:affiliation |
Department of Ophthalmology and Visual Sciences, College of Medicine, University of Illinois at Chicago, Chicago, IL 60612, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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