CD160

Official Full Name

CD160 molecule

Organism

Homo sapiens

GeneID

11126

Background

CD160 is an 27 kDa glycoprotein which was initially identified with the monoclonal antibody BY55. Its expression is tightly associated with peripheral blood NK cells and CD8 T lymphocytes with cytolytic effector activity. The cDNA sequence of CD160 predicts a cysteine-rich, glycosylphosphatidylinositol-anchored protein of 181 amino acids with a single Ig-like domain weakly homologous to KIR2DL4 molecule. CD160 is expressed at the cell surface as a tightly disulfide-linked multimer. RNA blot analysis revealed CD160 mRNAs of 1.5 and 1.6 kb whose expression was highly restricted to circulating NK and T cells, spleen and small intestine. Within NK cells CD160 is expressed by CD56dimCD16+ cells whereas among circulating T cells its expression is mainly restricted to TCRgd bearing cells and to TCRab+CD8brightCD95+CD56+CD28-CD27-cells. In tissues, CD160 is expressed on all intestinal intraepithelial lymphocytes. CD160 shows a broad specificity for binding to both classical and nonclassical MHC class I molecules. [provided by RefSeq, Jul 2008]

Synonyms

NK1; BY55; NK28;

Protein Sequence

MLLEPGRGCCALAILLAIVDIQSGGCINITSSASQEGTRLNLICTVWHKKEEAEGFVVFLCKDRSGDCSPETSLKQLRLKRDPGIDGVGEISSQLMFTISQVTPLHSGTYQCCARSQKSGIRLQGHFFSILFTETGNYTVTGLKQRQHLEFSHNEGTLSSGFLQEKVWVMLVTSLVALQAL

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Detailed Information

CD160 is a glycoprotein of approximately 27 kDa, initially recognized by the monoclonal antibody BY55. Found on human chromosome 1q21.1, the CD160 gene has six exons with non-coding sections in the first two of which. Considered to control CD160 expression, its promoter region has highly conserved transcription factor binding sites including FREAC-4, SOX17, and AML-1 (RUNX1), along with a core promoter sequence. By alternative splicing, the CD160 gene generates four isoforms: the transmembrane (CD160-TM), glycosylphosphatidylinositol (GPI)-anchored (CD160-GPI), and two truncated isoforms (CD160-ΔIg-GPI and CD160-ΔIg-TM), with different functions and distribution.

Expression and Distribution of CD160

CD160 is mainly expressed on natural killer (NK) cells and cytotoxic CD8+ T cells in peripheral blood. In NK cells, its expression is concentrated in the cytotoxic CD56dimCD16+ subset. Additionally, CD160 is expressed on all lymphocytes in the intestinal epithelium and is also found in other immune cells like γ/δ T cells and some α/β T cells. RNA blot analysis indicates that CD160 mRNA is primarily expressed in circulating NK cells and T cells, spleen, and intestinal tissues.

Molecular Structure and Function of CD160

Structurally like the KIR2DL4 receptor, CD160 is a cysteine-rich protein with a single immunoglobulin (Ig)-like domain. It may be found on the cell surface either transmembrane form or GPI anchoring. Acting as an immunological receptor, CD160 attaches to both classical and non-classical Class I major histocompatibility complex (MHC) molecules, therefore serving many functions in immune cells.

Especially crucial in antiviral innate immune responses, CD160 attaches to HLA-C molecules in NK cells to activate them, hence increasing cytotoxicity and cytokine release (e.g., IFN-γ, IL-6, and TNF-α). Furthermore, CD160 expression falls after NK cell activation, maybe acting as negative feedback to immunological activation.

In T Cells, CD160 may bind to HLA-A2 complexes in CD8+ T cells to provide co-stimulating signals increasing memory T cell activation. Sustained antigen stimulation, however, may induce CD160 to block T cell receptor (TCR) signaling, therefore causing memory T cell depletion in persistent infections. In endothelial cells, CD160 hooks on HLA-G to control angiogenesis in immune-privileged areas.

Pathological Relevance of CD160

Among the many pathophysiological events CD160 participates in include autoimmune illnesses, inflammatory disorders, atherosclerosis, persistent viral infections, and tumors. By improving the effector performance of immune cells to eliminate tumors, CD160 is thought to have antitumor actions in cancer immunity. Still, aberrant CD160 expression could help a disease worsen. For instance, overexpression of CD160 supports tumor cell survival and anti-apoptotic properties in chronic lymphocytic leukemia (CLL).

CD160 Expression in CLL

Common in industrialized nations, CLL is the most often occurring form of leukemia characterized by clonal B cell proliferation and accumulation. Tumour cell growth and treatment resistance in the CLL microenvironment depend critically on CD160. Using interactions with surrounding cells including stromal, endothelial, and mesenchymal cells, CD160 improves survival signals in CLL B cells In the CLL tumor microenvironment, CD160 also fuels immune cell fatigue.

Figure 1 illustrates B-cell receptor signaling in normal B cells and CLL cells, highlighting the differences in signaling pathways and regulatory mechanisms. Figure 1. B-cell receptor signaling in normal B cells and CLL cells. (Oumeslakht L, et al., 2022)

Clinical Significance

The limited expression of CD160 qualifies as a possible CLL diagnostic and prognostic marker. Under various treatment plans, like targeted treatments or chemotherapy mixed with immunotherapy (CIT), CD160 expression levels might be a useful metric for evaluating patient response. Tracking CD160 levels may also assist in identifying minimal remaining illness, therefore enhancing the whole remission rate and extending patient longevity.

CD160 is a possible target for new immunotherapies because of its wide influence on immunological control. Designing antibodies or small compounds targeted to CD160, for example, might allow exact control of its activity to boost antitumor immunity or increase results for patients with persistent viral infections. Moreover, because of its particular expression in CLL, CD160 might be the foundation for creating novel diagnostic reagents for dynamic monitoring of disease evolution or early identification.

References:

Oumeslakht L, Aziz AI, Bensussan A, et al. CD160 receptor in CLL: Current state and future avenues. Front Immunol. 2022 Nov 7;13:1028013.
Liu W, Garrett SC, Fedorov EV, et al. Structural Basis of CD160:HVEM Recognition. Structure. 2019 Aug 6;27(8):1286-1295.e4.

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