| Autor: |
Lenac, Tihana, Budt, Matthias, Arapovic, Jurica, Hasan, Milena, Zimmermann, Albert, Simic, Hrvoje, Krmpotic, Astrid, Messerle, Martin, Ruzsics, Zsolt, Koszinowski, Ulrich H., Hengel, Hartmut, Jonjic, Stipan |
| Předmět: |
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| Zdroj: |
Journal of Experimental Medicine; 8/7/2006, Vol. 203 Issue 8, p1843-1850, 8p |
| Abstrakt: |
Members of the α- and β-subfamily of herpesviridae encode glycoproteins that specifically bind to the Fc part of immunoglobulin (lg)G. Plasma membrane resident herpesviral Fc receptors seem to prevent virus-specific IgG from activating antibody-dependent effector functions. We show that the mouse cytomegalovirus (MCMV) molecule fcr-1 promotes a rapid down-regulation of NKG2D ligands routine UL16-binding protein like transcript (MULT)-1 and H60 from the cell surface. Deletion of the m138/fcr-1 gene from the MCMV genome attenuates viral replication to natural killer (NK) cell response in an NKG2D-dependent manner in vivo. A distinct N-terminal module within the fcr-1 ectodomain in conjunction with the fcr-1 transmembrane domain was required to dispose MULT-1 to degradation in lysosomes. In contrast, down-modulation of H60 required the complete fcr-1 ectodomain, implying independent modes of fcr-1 interaction with the NKG2D ligands. The results establish a novel viral strategy for down-modulating NK cell responses and highlight the impressive diversity of Fc receptor functions. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Supplemental Index |
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