Summary
The use of glycoproteins encoded by human cytomegalovirus as probes to isolate their cellular counterstructures has resulted in the discovery of novel immunoreceptors. The HCMV-encoded MHC class I homolog, UL18, binds to LIR-1/ILT2, an inhibitory signaling receptor for cellular MHC class I antigens with a broad distribution on leukocytes, including some NK cells. Although UL18 has been proposed to act as an inhibitor of NK cytotoxicity, this remains controversial. Another HCMV-encoded glycoprotein, UL16, binds to members of a novel non-classical MHC class I-related family, the ULBPs, as well as to MICB, a known non-classical MHC class I antigen. The MICs and ULBPs are ligands for the activating receptor, NKG2D/DAP10, expressed by NK and other immune effector cells. Ligation of NKG2D/DAP10 by ULBPs or MICs on a target cell can overcome an inhibitory signal mediated by NK recognition of MHC class I antigens and allow NK cytotoxicity. ULI6 masking of ULBP or MIC recognition may represent a mechanism of immune evasion by CMV.
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Cosman, D. et al. (2001). Interaction of human cytomegalovirus glycoproteins with immunoreceptors. In: Cooper, M.D., Takai, T., Ravetch, J.V. (eds) Activating and Inhibitory Immunoglobulin-like Receptors. Springer, Tokyo. https://doi.org/10.1007/978-4-431-53940-7_12
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DOI: https://doi.org/10.1007/978-4-431-53940-7_12
Publisher Name: Springer, Tokyo
Print ISBN: 978-4-431-67959-2
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