ArticleProceedings of the National Academy of Sciences of the United States of America2007
Structural elucidation of the m157 mouse cytomegalovirus ligand for Ly49 natural killer cell receptors.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed, 82 citations in OpenAlex.
- Dynamic changes of natural killer cell immunophenotypes and receptors according to the mortality in the intra-abdominal murine sepsis model.Intensive care medicine experimental · 2025Article
- Review
- Control of nutrient uptake by IRF4 orchestrates innate immune memory.Nature immunology · 2023Article
- Altered-Self MHC Class I Sensing via Functionally Disparate Paired NK Cell Receptors Counters Murine Cytomegalovirus gp34-Mediated Immune Evasion.Journal of immunology (Baltimore, Md. : 1950) · 2022Article
- Review
- 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
- Implications of a 'Third Signal' in NK Cells.Cells · 2021Review
- Natural killer cell responses to emerging viruses of zoonotic origin.Current opinion in virology · 2020Review
- α2β1 Integrin Is Required for Optimal NK Cell Proliferation during Viral Infection but Not for Acquisition of Effector Functions or NK Cell-Mediated Virus Control.Journal of immunology (Baltimore, Md. : 1950) · 2020Article
- Modulation of innate and adaptive immunity by cytomegaloviruses.Nature reviews. Immunology · 2020Review
- Memory and Memory-Like NK Cell Responses to Microbial Pathogens.Frontiers in cellular and infection microbiology · 2020Review
- The Evolutionary Arms Race between Virus and NK Cells: Diversity Enables Population-Level Virus Control.Viruses · 2019Review
- Inhibitory and Coactivating Receptors Recognising the Same Ligand: Immune Homeostasis Exploited by Pathogens and Tumours.Trends in immunology · 2018Review
- Natural Killer Cells: Development, Maturation, and Clinical Utilization.Frontiers in immunology · 2018Review
- Natural Killer Cells in Antifungal Immunity.Frontiers in immunology · 2017Review
- Antigen-specific expansion and differentiation of natural killer cells by alloantigen stimulation.The Journal of experimental medicine · 2014Article
- The structure of mouse cytomegalovirus m04 protein obtained from sparse NMR data reveals a conserved fold of the m02-m06 viral immune modulator family.Structure (London, England : 1993) · 2014Article
- The structure of the cytomegalovirus-encoded m04 glycoprotein, a prototypical member of the m02 family of immunoevasins.The Journal of biological chemistry · 2014Article
- The activating Ly49W and inhibitory Ly49G NK cell receptors display similar affinities for identical MHC class I ligands.Immunogenetics · 2014Article
- A positive cooperativity binding model between Ly49 natural killer cell receptors and the viral immunoevasin m157: kinetic and thermodynamic studies.The Journal of biological chemistry · 2014Article
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
Abstract
Natural killer (NK) cells express activating and inhibitory receptors that, in concert, survey cells for proper expression of cell surface major histocompatibility complex (MHC) class I molecules. The mouse cytomegalovirus encodes an MHC-like protein, m157, which is the only known viral antigen to date capable of engaging both activating (Ly49H) and inhibitory (Ly49I) NK cell receptors. We have determined the 3D structure of m157 and studied its biochemical and cellular interactions with the Ly49H and Ly49I receptors. m157 has a characteristic MHC-fold, yet possesses several unique structural features not found in other MHC class I-like molecules. m157 does not bind peptides or other small ligands, nor does it associate with beta(2)-microglobulin. Instead, m157 engages in extensive intra- and intermolecular interactions within and between its domains to generate a compact minimal MHC-like molecule. m157's binding affinity for Ly49I (K(d) approximately 0.2 microM) is significantly higher than that of classical inhibitory Ly49-MHC interactions. Analysis of viral escape mutations on m157 that render it resistant to NK killing reveals that it is likely to be recognized by Ly49H in a binding mode that differs from Ly49/MHC-I. In addition, Ly49H+ NK cells can efficiently lyse RMA cells expressing m157, despite the presence of native MHC class I. Collectively, our results show that m157 represents a structurally divergent form of MHC class I-like proteins that directly engage Ly49 receptors with appreciable affinity in a noncanonical fashion.
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