pubmed-article:10859362 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:10859362 | lifeskim:mentions | umls-concept:C0376526 | lld:lifeskim |
pubmed-article:10859362 | lifeskim:mentions | umls-concept:C0017355 | lld:lifeskim |
pubmed-article:10859362 | lifeskim:mentions | umls-concept:C0699040 | lld:lifeskim |
pubmed-article:10859362 | lifeskim:mentions | umls-concept:C0028778 | lld:lifeskim |
pubmed-article:10859362 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:10859362 | lifeskim:mentions | umls-concept:C0014139 | lld:lifeskim |
pubmed-article:10859362 | lifeskim:mentions | umls-concept:C1524075 | lld:lifeskim |
pubmed-article:10859362 | lifeskim:mentions | umls-concept:C0870432 | lld:lifeskim |
pubmed-article:10859362 | lifeskim:mentions | umls-concept:C1999177 | lld:lifeskim |
pubmed-article:10859362 | lifeskim:mentions | umls-concept:C1705417 | lld:lifeskim |
pubmed-article:10859362 | lifeskim:mentions | umls-concept:C1555465 | lld:lifeskim |
pubmed-article:10859362 | lifeskim:mentions | umls-concept:C2700640 | lld:lifeskim |
pubmed-article:10859362 | pubmed:issue | 14 | lld:pubmed |
pubmed-article:10859362 | pubmed:dateCreated | 2000-8-10 | lld:pubmed |
pubmed-article:10859362 | pubmed:abstractText | Down-regulation of the cell surface display of class I MHC proteins is an important mechanism of immune evasion by human and animal viruses. Herpesviruses in particular encode a variety of proteins that function to lower MHC I display by several mechanisms. These include binding and retention of MHC I chains in the endoplasmic reticulum, dislocation of class I chains from the ER, inhibition of the peptide transporter (TAP) involved in antigen presentation, and shunting of newly assembled chains to lysosomes. Kaposi's sarcoma (KS)-associated herpesvirus (KSHV) is a human herpesvirus strongly linked to the development of KS and to certain AIDS-associated lymphoproliferative disorders. Here we show that KSHV encodes two distinctive gene products that function to dramatically reduce cell surface MHC I expression. These viral proteins are localized predominantly to the ER. However, unlike previously described MHC I inhibitors, they do not interfere with the synthesis, translocation, or assembly of class I chains, nor do they retain them in the ER. Rather, they act to enhance endocytosis of MHC I from the cell surface; internalized class I chains are delivered to endolysosomal vesicles, where they undergo degradation. These KSHV proteins define a mechanism of class I down-regulation distinct from the mechanisms of other herpesviruses and are likely to contribute importantly to immune evasion during viral infection. | lld:pubmed |
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pubmed-article:10859362 | pubmed:language | eng | lld:pubmed |
pubmed-article:10859362 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10859362 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:10859362 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:10859362 | pubmed:month | Jul | lld:pubmed |
pubmed-article:10859362 | pubmed:issn | 0027-8424 | lld:pubmed |
pubmed-article:10859362 | pubmed:author | pubmed-author:GanemDD | lld:pubmed |
pubmed-article:10859362 | pubmed:author | pubmed-author:CoscoyLL | lld:pubmed |
pubmed-article:10859362 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:10859362 | pubmed:day | 5 | lld:pubmed |
pubmed-article:10859362 | pubmed:volume | 97 | lld:pubmed |
pubmed-article:10859362 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:10859362 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:10859362 | pubmed:pagination | 8051-6 | lld:pubmed |
pubmed-article:10859362 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:10859362 | pubmed:year | 2000 | lld:pubmed |
pubmed-article:10859362 | pubmed:articleTitle | Kaposi's sarcoma-associated herpesvirus encodes two proteins that block cell surface display of MHC class I chains by enhancing their endocytosis. | lld:pubmed |
pubmed-article:10859362 | pubmed:affiliation | Howard Hughes Medical Institute and Departments of Microbiology and Medicine, University of California, San Francisco, CA 94143, USA. | lld:pubmed |
pubmed-article:10859362 | pubmed:publicationType | Journal Article | lld:pubmed |
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