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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

The herpesviral Fc receptor fcr-1 down-regulates the NKG2D ligands MULT-1 and H60.

Members of the alpha- and beta-subfamily of herpesviridae encode glycoproteins that specifically bind to the Fc part of immunoglobulin (Ig)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 murine 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.[1]


  1. The herpesviral Fc receptor fcr-1 down-regulates the NKG2D ligands MULT-1 and H60. Lenac, T., Budt, M., Arapovic, J., Hasan, M., Zimmermann, A., Simic, H., Krmpotic, A., Messerle, M., Ruzsics, Z., Koszinowski, U.H., Hengel, H., Jonjic, S. J. Exp. Med. (2006) [Pubmed]
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