| pubmed-article:10364366 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10364366 | lifeskim:mentions | umls-concept:C0011315 | lld:lifeskim |
| pubmed-article:10364366 | lifeskim:mentions | umls-concept:C0332307 | lld:lifeskim |
| pubmed-article:10364366 | lifeskim:mentions | umls-concept:C0028326 | lld:lifeskim |
| pubmed-article:10364366 | lifeskim:mentions | umls-concept:C1512977 | lld:lifeskim |
| pubmed-article:10364366 | lifeskim:mentions | umls-concept:C0017968 | lld:lifeskim |
| pubmed-article:10364366 | lifeskim:mentions | umls-concept:C1327616 | lld:lifeskim |
| pubmed-article:10364366 | lifeskim:mentions | umls-concept:C1749467 | lld:lifeskim |
| pubmed-article:10364366 | lifeskim:mentions | umls-concept:C1706044 | lld:lifeskim |
| pubmed-article:10364366 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:10364366 | pubmed:dateCreated | 1999-7-23 | lld:pubmed |
| pubmed-article:10364366 | pubmed:abstractText | Nonstructural glycoprotein NS1, specified by dengue virus type 1 (Den-1), is secreted from infected green monkey kidney (Vero) cells in a major soluble form characterized by biochemical and biophysical means as a unique hexameric species. This noncovalently bound oligomer is formed by three dimeric subunits and has a molecular mass of 310 kDa and a Stokes radius of 64.4 A. During protein export, one of the two oligosaccharides of NS1 is processed into an endo-beta-N-acetylglucosaminidase F-resistant complex-type sugar while the other remains of the polymannose type, protected in the dimeric subunit from the action of maturation enzymes. Complete processing of the complex-type sugar appears to be required for efficient release of soluble NS1 into the culture fluid of infected cells, as suggested by the repressive effects of the N-glycan processing inhibitors swainsonine and deoxymannojyrimicin. These results, together with observations related to the absence of secretion of NS1 from Den-infected insect cells, suggest that maturation and secretion of hexameric NS1 depend on the glycosylation status of the host cell. | lld:pubmed |
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| pubmed-article:10364366 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:10364366 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:10364366 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10364366 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:10364366 | pubmed:issn | 0022-538X | lld:pubmed |
| pubmed-article:10364366 | pubmed:author | pubmed-author:MathieuMM | lld:pubmed |
| pubmed-article:10364366 | pubmed:author | pubmed-author:LepaultJJ | lld:pubmed |
| pubmed-article:10364366 | pubmed:author | pubmed-author:DeubelVV | lld:pubmed |
| pubmed-article:10364366 | pubmed:author | pubmed-author:MegretFF | lld:pubmed |
| pubmed-article:10364366 | pubmed:author | pubmed-author:FlamandMM | lld:pubmed |
| pubmed-article:10364366 | pubmed:author | pubmed-author:ReyF AFA | lld:pubmed |
| pubmed-article:10364366 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10364366 | pubmed:volume | 73 | lld:pubmed |
| pubmed-article:10364366 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10364366 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10364366 | pubmed:pagination | 6104-10 | lld:pubmed |
| pubmed-article:10364366 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:10364366 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10364366 | pubmed:articleTitle | Dengue virus type 1 nonstructural glycoprotein NS1 is secreted from mammalian cells as a soluble hexamer in a glycosylation-dependent fashion. | lld:pubmed |
| pubmed-article:10364366 | pubmed:affiliation | Unité des Arbovirus et Virus des Fièvres Hémorragiques, Institut Pasteur, 75724 Paris Cedex 15, 91198 Gif-sur-Yvette Cedex, France. mflamand@pasteur.fr | lld:pubmed |
| pubmed-article:10364366 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10364366 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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