pubmed-article:16185739 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:16185739 | lifeskim:mentions | umls-concept:C0042769 | lld:lifeskim |
pubmed-article:16185739 | lifeskim:mentions | umls-concept:C0567416 | lld:lifeskim |
pubmed-article:16185739 | lifeskim:mentions | umls-concept:C0027149 | lld:lifeskim |
pubmed-article:16185739 | lifeskim:mentions | umls-concept:C1546857 | lld:lifeskim |
pubmed-article:16185739 | lifeskim:mentions | umls-concept:C0449255 | lld:lifeskim |
pubmed-article:16185739 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:16185739 | pubmed:dateCreated | 2005-11-18 | lld:pubmed |
pubmed-article:16185739 | pubmed:abstractText | Downregulation of MHC class I molecules is a strategy developed by some viruses to escape cellular immune responses. Myxoma virus (MV), a poxvirus causing rabbit myxomatosis, encodes MV-LAP that is known to increase MHC-I endocytosis and degradation through a C(4)HC(3) motif critical for an E3 ubiquitin ligase activity. Here, we performed a functional mapping of MV-LAP and showed that not only the C(4)HC(3) motif is necessary for a marked downregulation of MHC-I but also a conserved region in the C-terminal part of the protein. We also showed that the putative transmembrane domains are responsible for a specific subcellular localization of the protein: they retain MV-LAP in the ER in transfected cells and in the endolysosomal compartments in infected cells. We observed that a specific MV infection context is necessary for a fully efficient downregulation of MHC-I. Our data suggest that the functionality of viral LAP factors, inherited by herpes- and poxviruses from mammalian cells, is more complex than anticipated. | lld:pubmed |
pubmed-article:16185739 | pubmed:language | eng | lld:pubmed |
pubmed-article:16185739 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16185739 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:16185739 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16185739 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16185739 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16185739 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16185739 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16185739 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16185739 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:16185739 | pubmed:month | Dec | lld:pubmed |
pubmed-article:16185739 | pubmed:issn | 0042-6822 | lld:pubmed |
pubmed-article:16185739 | pubmed:author | pubmed-author:DrexlerIngoI | lld:pubmed |
pubmed-article:16185739 | pubmed:author | pubmed-author:FoucrasGilles... | lld:pubmed |
pubmed-article:16185739 | pubmed:author | pubmed-author:GelfiJacqueli... | lld:pubmed |
pubmed-article:16185739 | pubmed:author | pubmed-author:SutterGerdG | lld:pubmed |
pubmed-article:16185739 | pubmed:author | pubmed-author:BoullierSéver... | lld:pubmed |
pubmed-article:16185739 | pubmed:author | pubmed-author:Messud-PetitF... | lld:pubmed |
pubmed-article:16185739 | pubmed:author | pubmed-author:CollinNicolas... | lld:pubmed |
pubmed-article:16185739 | pubmed:author | pubmed-author:GuérinJean-Lu... | lld:pubmed |
pubmed-article:16185739 | pubmed:author | pubmed-author:BlaniéSophieS | lld:pubmed |
pubmed-article:16185739 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:16185739 | pubmed:day | 20 | lld:pubmed |
pubmed-article:16185739 | pubmed:volume | 343 | lld:pubmed |
pubmed-article:16185739 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:16185739 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:16185739 | pubmed:pagination | 171-8 | lld:pubmed |
pubmed-article:16185739 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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pubmed-article:16185739 | pubmed:year | 2005 | lld:pubmed |
pubmed-article:16185739 | pubmed:articleTitle | The poxviral scrapin MV-LAP requires a myxoma viral infection context to efficiently downregulate MHC-I molecules. | lld:pubmed |
pubmed-article:16185739 | pubmed:affiliation | UMR 1225 Interactions Hôtes Agents pathogènes, INRA/ENVT, Ecole Nationale Vétérinaire de Toulouse, 23 chemin des Capelles, BP87614, 31076 Toulouse cedex 03, France. | lld:pubmed |
pubmed-article:16185739 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:16185739 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |