| pubmed-article:19665490 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19665490 | lifeskim:mentions | umls-concept:C0206558 | lld:lifeskim |
| pubmed-article:19665490 | lifeskim:mentions | umls-concept:C1261468 | lld:lifeskim |
| pubmed-article:19665490 | lifeskim:mentions | umls-concept:C0242210 | lld:lifeskim |
| pubmed-article:19665490 | lifeskim:mentions | umls-concept:C1148586 | lld:lifeskim |
| pubmed-article:19665490 | lifeskim:mentions | umls-concept:C1550548 | lld:lifeskim |
| pubmed-article:19665490 | lifeskim:mentions | umls-concept:C1555714 | lld:lifeskim |
| pubmed-article:19665490 | lifeskim:mentions | umls-concept:C1705654 | lld:lifeskim |
| pubmed-article:19665490 | lifeskim:mentions | umls-concept:C1533157 | lld:lifeskim |
| pubmed-article:19665490 | lifeskim:mentions | umls-concept:C0664874 | lld:lifeskim |
| pubmed-article:19665490 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:19665490 | pubmed:dateCreated | 2009-9-7 | lld:pubmed |
| pubmed-article:19665490 | 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. | lld:pubmed |
| pubmed-article:19665490 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19665490 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19665490 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19665490 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19665490 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19665490 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:19665490 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19665490 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19665490 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19665490 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19665490 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19665490 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:19665490 | pubmed:issn | 1872-9096 | lld:pubmed |
| pubmed-article:19665490 | pubmed:author | pubmed-author:TiwariVaibhav... | lld:pubmed |
| pubmed-article:19665490 | pubmed:author | pubmed-author:ShuklaDeepakD | lld:pubmed |
| pubmed-article:19665490 | pubmed:author | pubmed-author:ShuklaShripaa... | lld:pubmed |
| pubmed-article:19665490 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19665490 | pubmed:volume | 84 | lld:pubmed |
| pubmed-article:19665490 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19665490 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19665490 | pubmed:pagination | 67-75 | lld:pubmed |
| pubmed-article:19665490 | pubmed:dateRevised | 2011-5-27 | lld:pubmed |
| pubmed-article:19665490 | pubmed:meshHeading | pubmed-meshheading:19665490... | lld:pubmed |
| pubmed-article:19665490 | pubmed:meshHeading | pubmed-meshheading:19665490... | lld:pubmed |
| pubmed-article:19665490 | pubmed:meshHeading | pubmed-meshheading:19665490... | lld:pubmed |
| pubmed-article:19665490 | pubmed:meshHeading | pubmed-meshheading:19665490... | lld:pubmed |
| pubmed-article:19665490 | pubmed:meshHeading | pubmed-meshheading:19665490... | lld:pubmed |
| pubmed-article:19665490 | pubmed:meshHeading | pubmed-meshheading:19665490... | lld:pubmed |
| pubmed-article:19665490 | pubmed:meshHeading | pubmed-meshheading:19665490... | lld:pubmed |
| pubmed-article:19665490 | pubmed:meshHeading | pubmed-meshheading:19665490... | lld:pubmed |
| pubmed-article:19665490 | pubmed:meshHeading | pubmed-meshheading:19665490... | lld:pubmed |
| pubmed-article:19665490 | pubmed:meshHeading | pubmed-meshheading:19665490... | lld:pubmed |
| pubmed-article:19665490 | pubmed:meshHeading | pubmed-meshheading:19665490... | lld:pubmed |
| pubmed-article:19665490 | pubmed:meshHeading | pubmed-meshheading:19665490... | lld:pubmed |
| pubmed-article:19665490 | pubmed:meshHeading | pubmed-meshheading:19665490... | lld:pubmed |
| pubmed-article:19665490 | pubmed:year | 2009 | lld:pubmed |
| pubmed-article:19665490 | pubmed:articleTitle | A sugar binding protein cyanovirin-N blocks herpes simplex virus type-1 entry and cell fusion. | lld:pubmed |
| pubmed-article:19665490 | pubmed:affiliation | Department of Ophthalmology and Visual Sciences, College of Medicine, University of Illinois at Chicago, Chicago, IL 60612, USA. | lld:pubmed |
| pubmed-article:19665490 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:19665490 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:19665490 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
