ArticlePLoS pathogens2010
Structure of the HCMV UL16-MICB complex elucidates select binding of a viral immunoevasin to diverse NKG2D ligands.
Article in PLoS pathogens, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 52 citations in OpenAlex.
- NK and T cell evasion mechanism of human cytomegalovirus.Archives of virology · 2025Review
- Recognition of Self and Viral Ligands by NK Cell Receptors.Immunological reviews · 2025Review
- Observational
- NKG2D discriminates diverse ligands through selectively mechano-regulated ligand conformational changes.The EMBO journal · 2022Article
- Structural Models for Roseolovirus U20 And U21: Non-Classical MHC-I Like Proteins From HHV-6A, HHV-6B, and HHV-7.Frontiers in immunology · 2022Review
- The NKG2D ligand ULBP4 is not expressed by human monocytes.PloS one · 2021Article
- Compatibility at amino acid position 98 of MICB reduces the incidence of graft-versus-host disease in conjunction with the CMV status.Bone marrow transplantation · 2020Article
- convertibleCARs: A chimeric antigen receptor system for flexible control of activity and antigen targeting.Communications biology · 2020Article
- Modulation of innate and adaptive immunity by cytomegaloviruses.Nature reviews. Immunology · 2020Review
- MICAgen Mice Recapitulate the Highly Restricted but Activation-Inducible Expression of the Paradigmatic Human NKG2D Ligand MICA.Frontiers in immunology · 2020Article
- MICA-129 Dimorphism and Soluble MICA Are Associated With the Progression of Multiple Myeloma.Frontiers in immunology · 2018Article
- Cutting an NKG2D Ligand Short: Cellular Processing of the Peculiar Human NKG2D Ligand ULBP4.Frontiers in immunology · 2018Review
- Global Mapping of O-Glycosylation of Varicella Zoster Virus, Human Cytomegalovirus, and Epstein-Barr Virus.The Journal of biological chemistry · 2016Article
- Viral Evasion of Natural Killer Cell Activation.Viruses · 2016Review
- Varicella-Zoster Virus and Herpes Simplex Virus 1 Differentially Modulate NKG2D Ligand Expression during Productive Infection.Journal of virology · 2015Article
- Cytomegalovirus immune evasion by perturbation of endosomal trafficking.Cellular & molecular immunology · 2015Review
- Classical and non-classical MHC I molecule manipulation by human cytomegalovirus: so many targets—but how many arrows in the quiver?Cellular & molecular immunology · 2015Review
- The structure of cytomegalovirus immune modulator UL141 highlights structural Ig-fold versatility for receptor binding.Acta crystallographica. Section D, Biological crystallography · 2014Article
- Structural basis for recognition of cellular and viral ligands by NK cell receptors.Frontiers in immunology · 2014Review
- Functional annotation of human cytomegalovirus gene products: an update.Frontiers in microbiology · 2014Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The activating immunoreceptor NKG2D promotes elimination of infected or malignant cells by cytotoxic lymphocytes through engagement of stress-induced MHC class I-related ligands. The human cytomegalovirus (HCMV)-encoded immunoevasin UL16 subverts NKG2D-mediated immune responses by retaining a select group of diverse NKG2D ligands inside the cell. We report here the crystal structure of UL16 in complex with the NKG2D ligand MICB at 1.8 A resolution, revealing the molecular basis for the promiscuous, but highly selective, binding of UL16 to unrelated NKG2D ligands. The immunoglobulin-like UL16 protein utilizes a three-stranded beta-sheet to engage the alpha-helical surface of the MHC class I-like MICB platform domain. Intriguingly, residues at the center of this beta-sheet mimic a central binding motif employed by the structurally unrelated C-type lectin-like NKG2D to facilitate engagement of diverse NKG2D ligands. Using surface plasmon resonance, we find that UL16 binds MICB, ULBP1, and ULBP2 with similar affinities that lie in the nanomolar range (12-66 nM). The ability of UL16 to bind its ligands depends critically on the presence of a glutamine (MICB) or closely related glutamate (ULBP1 and ULBP2) at position 169. An arginine residue at this position however, as found for example in MICA or ULBP3, would cause steric clashes with UL16 residues. The inability of UL16 to bind MICA and ULBP3 can therefore be attributed to single substitutions at key NKG2D ligand locations. This indicates that selective pressure exerted by viral immunoevasins such as UL16 contributed to the diversification of NKG2D ligands.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.