| pubmed-article:10805975 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10805975 | lifeskim:mentions | umls-concept:C0026926 | lld:lifeskim |
| pubmed-article:10805975 | lifeskim:mentions | umls-concept:C0005953 | lld:lifeskim |
| pubmed-article:10805975 | lifeskim:mentions | umls-concept:C0024432 | lld:lifeskim |
| pubmed-article:10805975 | lifeskim:mentions | umls-concept:C0019630 | lld:lifeskim |
| pubmed-article:10805975 | lifeskim:mentions | umls-concept:C0206430 | lld:lifeskim |
| pubmed-article:10805975 | lifeskim:mentions | umls-concept:C0591833 | lld:lifeskim |
| pubmed-article:10805975 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:10805975 | pubmed:dateCreated | 2000-7-6 | lld:pubmed |
| pubmed-article:10805975 | pubmed:abstractText | Infection of murine bone-marrow-derived macrophages with viable Mycobacterium tuberculosis (MTB) H37Ra inhibited surface expression of MHC class II (MHC-II) molecules and processing of exogenous antigens for presentation to CD4(+) T hybridoma cells. The inhibition was not dependent on bacterial viability, since it was also produced by exposure to dead bacilli and MTB cytosol preparations, suggesting that it was initiated by a constitutively expressed bacterial component. Northern blot analysis demonstrated that MTB bacilli or cytosol decreased MHC-II mRNA, and immunoprecipitation of biosynthetically labeled molecules confirmed that MHC-II protein synthesis was diminished. Exposure to MTB or MTB cytosol also decreased expression of H2-DM, but H2-DM expression was still sufficient to catalyze conversion of MHC-II to SDS-stable dimers, a measure of MHC-II peptide loading. Thus, infection with MTB decreased both MHC-II and H2-DM expression, but diminished MHC-II synthesis provided the major limitation to antigen processing. | lld:pubmed |
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| pubmed-article:10805975 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10805975 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10805975 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:10805975 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10805975 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:10805975 | pubmed:issn | 0008-8749 | lld:pubmed |
| pubmed-article:10805975 | pubmed:author | pubmed-author:HardingC VCV | lld:pubmed |
| pubmed-article:10805975 | pubmed:author | pubmed-author:BoopW CWC | lld:pubmed |
| pubmed-article:10805975 | pubmed:author | pubmed-author:NossE HEH | lld:pubmed |
| pubmed-article:10805975 | pubmed:copyrightInfo | Copyright 2000 Academic Press. | lld:pubmed |
| pubmed-article:10805975 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10805975 | pubmed:day | 10 | lld:pubmed |
| pubmed-article:10805975 | pubmed:volume | 201 | lld:pubmed |
| pubmed-article:10805975 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10805975 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10805975 | pubmed:pagination | 63-74 | lld:pubmed |
| pubmed-article:10805975 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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| pubmed-article:10805975 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10805975 | pubmed:articleTitle | Mycobacterium tuberculosis inhibits MHC class II antigen processing in murine bone marrow macrophages. | lld:pubmed |
| pubmed-article:10805975 | pubmed:affiliation | Department of Pathology, Case Western Reserve University, Cleveland, Ohio 44106, USA. | lld:pubmed |
| pubmed-article:10805975 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10805975 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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