Natural killer group 2 member D (NKG2D) is a lectin-like receptor expressed on several immune cells. The interactions of NKG2D with its ligands lead to immune activation and inflammation. The ligands are very diverse consisting of several clusters of molecules related to MHC class I. These are MHC class I chain-related (MIC) and unique long 16 binding protein (ULBP) or retinoic acid early transcript 1 (RAET1) families in human versus retinoic acid early inducible 1 (Rae1), murine UL16-binding protein-like transcript (Mult1) and H60 in murine indicating evolutional and functional divergence in the two species. There are several copies of genes in each family. NKG2D ligands are heavily glycosylated. Some human NKG2D ligand polymorphisms contain glycosylation sites leading to different glycosylation. However, functional polymorphisms of glycosylation or alternative expressions of other gene copies have not been studied or reported. The roles of NKG2D and its ligands have been intensively reported in cancer, autoimmune diseases, and infections but not so much in other inflammatory conditions such as in cardiovascular diseases and aging.
The goal of this Research Topic is to unravel the significance of functional polymorphisms especially in NKG2D ligands including those affecting glycosylation of the molecule as well as comparative genomic analysis leading to functional evolution. The role of interaction of NKG2D and its ligands will be more elaborated not only in diseases that were previously reported but also exploring in other inflammatory conditions such as in cardiovascular diseases and immunosenescence in the elderly. Signaling pathways resulted from NKG2D activation that are linked to the production of inflammatory cytokines will also be explored.
The submitted manuscripts can be either Review, Systematic Review, or Original Research articles. The scope of the topic will focus on NKG2D, NKG2D ligands and interactions of NKG2D and NKG2D ligands regarding immune responses based upon comparative genomics or transcriptomic or metabolomic analysis, functional polymorphisms and their roles in cancer, bacterial or viral infections, autoimmune diseases, immunosenescence, cardiovascular diseases, including signaling pathway related to productions of proinflammatory cytokines after NKG2D activation using current technologies such as single-cell analysis, high-throughput technologies, etc. We welcome the submission of manuscripts, covering, but not limited to, the following subtopics:
1. Molecular regulation of NKG2D and NKG2D ligands
2. Relationship between structure/genetics of NKG2D and NKG2D ligands and functionality
3. Signaling pathways of NKG2D and NKG2D ligands
4. NK/T/NKT and subpopulations of immune cells
5. The impact of the interaction of NKG2D and NKG2D ligands on immunity in health and diseases
6. The role of interaction of NKG2D and its ligands in diseases and pathological conditions e.g., cancer, autoimmunity, immunosenescence, and cardiovascular diseases
7. Functional evolution and polymorphisms of NKG2D and NKG2D ligands
Natural killer group 2 member D (NKG2D) is a lectin-like receptor expressed on several immune cells. The interactions of NKG2D with its ligands lead to immune activation and inflammation. The ligands are very diverse consisting of several clusters of molecules related to MHC class I. These are MHC class I chain-related (MIC) and unique long 16 binding protein (ULBP) or retinoic acid early transcript 1 (RAET1) families in human versus retinoic acid early inducible 1 (Rae1), murine UL16-binding protein-like transcript (Mult1) and H60 in murine indicating evolutional and functional divergence in the two species. There are several copies of genes in each family. NKG2D ligands are heavily glycosylated. Some human NKG2D ligand polymorphisms contain glycosylation sites leading to different glycosylation. However, functional polymorphisms of glycosylation or alternative expressions of other gene copies have not been studied or reported. The roles of NKG2D and its ligands have been intensively reported in cancer, autoimmune diseases, and infections but not so much in other inflammatory conditions such as in cardiovascular diseases and aging.
The goal of this Research Topic is to unravel the significance of functional polymorphisms especially in NKG2D ligands including those affecting glycosylation of the molecule as well as comparative genomic analysis leading to functional evolution. The role of interaction of NKG2D and its ligands will be more elaborated not only in diseases that were previously reported but also exploring in other inflammatory conditions such as in cardiovascular diseases and immunosenescence in the elderly. Signaling pathways resulted from NKG2D activation that are linked to the production of inflammatory cytokines will also be explored.
The submitted manuscripts can be either Review, Systematic Review, or Original Research articles. The scope of the topic will focus on NKG2D, NKG2D ligands and interactions of NKG2D and NKG2D ligands regarding immune responses based upon comparative genomics or transcriptomic or metabolomic analysis, functional polymorphisms and their roles in cancer, bacterial or viral infections, autoimmune diseases, immunosenescence, cardiovascular diseases, including signaling pathway related to productions of proinflammatory cytokines after NKG2D activation using current technologies such as single-cell analysis, high-throughput technologies, etc. We welcome the submission of manuscripts, covering, but not limited to, the following subtopics:
1. Molecular regulation of NKG2D and NKG2D ligands
2. Relationship between structure/genetics of NKG2D and NKG2D ligands and functionality
3. Signaling pathways of NKG2D and NKG2D ligands
4. NK/T/NKT and subpopulations of immune cells
5. The impact of the interaction of NKG2D and NKG2D ligands on immunity in health and diseases
6. The role of interaction of NKG2D and its ligands in diseases and pathological conditions e.g., cancer, autoimmunity, immunosenescence, and cardiovascular diseases
7. Functional evolution and polymorphisms of NKG2D and NKG2D ligands
