Abstract:
:The class II trans-activator (CIITA) is a bi- or multi-functional domain protein which plays a critical role in the expression of MHC class II genes. We report that removal of the N-terminal 151 amino acids, encompassing all of the acidic domain but leaving intact the proline/serine/threonine-rich domain, results in a mutant protein with potent suppressive properties for MHC class II expression. HeLa cells stably or transiently transfected with mutant CIITA constructs showed up to 99% suppression of MHC class II antigen induction by IFN-gamma and marked suppression of HLA-DRA mRNA expression. Transient transfection of a B lymphoma line resulted in up to 89% reduction of constitutive MHC class II expression within 5 days and suppression of HLA-DRA mRNA synthesis.
journal_name
Int Immunoljournal_title
International immunologyauthors
Yun S,Gustafsson K,Fabre JWdoi
10.1093/intimm/9.10.1545subject
Has Abstractpub_date
1997-10-01 00:00:00pages
1545-53issue
10eissn
0953-8178issn
1460-2377journal_volume
9pub_type
杂志文章abstract::Based on the similarity in primary structure between the newly characterized ligand for CD40 (CD40L) and the tumor necrosis factors (TNFs), we have modeled a detailed 3-D structure for CD40L. We used the known structure of TNF alpha as a template for the generation of the CD40L model. The soundness of the model-buildi...
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journal_title:International immunology
pub_type: 杂志文章
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journal_title:International immunology
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