Poliovirus Receptor (PVR) is a 70 kDa type I transmembrane single-span glycoprotein that belongs to the nectin-like (Necl) family and was originally identified based on its ability to mediate the cell attachment and entry of poliovirus (PV), an etiologic agent of the central nervous system disease poliomyelitis. PVR contains three Ig-like extracellular domains, a transmembrane segment, and a cytoplasmic tail. The normal cellular function of PVR maybe the involvement of intercellular adhension between epithelial cells. Alternate splicing of the PVR mRNA yields four different isoforms (α, β, γ, and δ) with identical extracellular domains.
Poliovirus Receptor (PVR) is a 70 kDa type I transmembrane single-span glycoprotein that belongs to the nectin-like (Necl) family and was originally identified based on its ability to mediate the cell attachment and entry of poliovirus (PV); an etiologic agent of the central nervous system disease poliomyelitis. PVR contains three Ig-like extracellular domains; a transmembrane segment; and a cytoplasmic tail. The normal cellular function of PVR maybe the involvement of intercellular adhension between epithelial cells. Alternate splicing of the PVR mRNA yields four different isoforms (α; β; γ; and δ) with identical extracellular domains.
CD155; commonly known as PVR (poliovirus receptor) and Necl-5 (nectin-like molecule-5); is a type I transmembrane single-span glycoprotein; and belongs to the nectins and nectin-like (Necl) subfamily. CD155 was originally identified based on its ability to mediate the cell attachment and entry of poliovirus (PV); an etiologic agent of the central nervous system disease poliomyelitis. The normal cellular function is in the establishment of intercellular adherens junctions between epithelial cells. CD155 may assist in an efficient humoral immune response generated within the intestinal immune system. It has been demonstrated that CD155 can be recognized and bond by DNAM-1 and CD96 which promote the adhension; migration and NK-cell killing; and thus efficiently prime cell-mediated tumor-specific immunity.
CD38; also called ADP-ribosyl cyclase; is a Type II integral membrane protein with 301 amino acids in length that belongs to the ADP-ribosyl cyclase family.It synthesizes the second messagers cyclic ADP-ribose and nicotinate-adenine dinucleotide phosphate; the former a second messenger for glucose-induced insulin secretion. And also moonlights as a receptor in cells of the immune system. CD38 is expressed in B and T lymphocytes; osteoclasts; and in cardiac; pancreatic; liver and kidney cells. Through its production of cyclic ADP-ribose; CD38 modulates calcium-mediated signal transduction in many types of cells; including neutrophils and pancreatic beta cells.
The cluster of differentiation (CD) system is a glycosyl phosphatidylinositol anchored membrane protein that belongs to the CD38 family.It is generally used in immunophynotyping. CD157 was discovered in a bone marrow stromal cell line where it facilitates pre-B-cell growth. CD157 is a bifunctional ectoenzyme that exhibits both ADP-ribosyl cyclase and cyclic ADP ribose hydrolase activities followed with CD38. It plays a role in rheumatoid arthritis (RA) due to its enhanced expression in RA-derived bone marrow stromal cell lines. Studies have shown that this protein have a role in predicted to function as a cell surface receptor and an immunoregulatory molecule.
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