The external domain mediates cell attachment to the extracellular matrix molecule vitronectin, while its intracellular domain interacts with the dynein light chain Tctex-1/DYNLT1. The gene is specific to the primate lineage, and serves as a cellular receptor for poliovirus in the first step of poliovirus replication.[1]
Structure
CD155 is a transmembrane protein with 3 extracellular immunoglobulin-like domains, D1-D3, where D1 is recognized by the virus.[5]
Vincent Racaniello, Professor in the Department of Microbiology and Immunology at Columbia University’s College of Physicians and Surgeons responsible for initial identification of CD155 as the poliovirus receptor protein.
↑Mendelsohn CL, Wimmer E, Racaniello VR (1989). "Cellular receptor for poliovirus: molecular cloning, nucleotide sequence, and expression of a new member of the immunoglobulin superfamily". Cell. 56 (5): 855–65. doi:10.1016/0092-8674(89)90690-9. PMID2538245.
↑ 4.04.1Maier MK, Seth S, Czeloth N, et al. (2007). "The adhesion receptor CD155 determines the magnitude of humoral immune responses against orally ingested antigens". European Journal of Immunology. 37 (8): 2214–25. doi:10.1002/eji.200737072. PMID17621371.
Pende D, Spaggiari GM, Marcenaro S, et al. (2005). "Analysis of the receptor-ligand interactions in the natural killer-mediated lysis of freshly isolated myeloid or lymphoblastic leukemias: evidence for the involvement of the Poliovirus receptor (CD155) and Nectin-2 (CD112)". Blood. 105 (5): 2066–73. doi:10.1182/blood-2004-09-3548. PMID15536144.
Pezzetti F, Palmieri A, Martinelli M, et al. (2007). "Linkage disequilibrium analysis of two genes mapping on OFC3: PVR and PVRL2". Eur. J. Hum. Genet. 15 (9): 992–4. doi:10.1038/sj.ejhg.5201868. PMID17534374.
Pende D, Bottino C, Castriconi R, et al. (2005). "PVR (CD155) and Nectin-2 (CD112) as ligands of the human DNAM-1 (CD226) activating receptor: involvement in tumor cell lysis". Mol. Immunol. 42 (4): 463–9. doi:10.1016/j.molimm.2004.07.028. PMID15607800.
Kono T, Imai Y, Yasuda S, et al. (2008). "The CD155/poliovirus receptor enhances the proliferation of ras-mutated cells". Int. J. Cancer. 122 (2): 317–24. doi:10.1002/ijc.23080. PMID17893876.
Minami Y, Ikeda W, Kajita M, et al. (2007). "Necl-5/poliovirus receptor interacts in cis with integrin alphaVbeta3 and regulates its clustering and focal complex formation". J. Biol. Chem. 282 (25): 18481–96. doi:10.1074/jbc.M611330200. PMID17446174.
Yu X, Harden K, Gonzalez LC, et al. (2009). "The surface protein TIGIT suppresses T cell activation by promoting the generation of mature immunoregulatory dendritic cells". Nat. Immunol. 10 (1): 48–57. doi:10.1038/ni.1674. PMID19011627.
Carlsten M, Norell H, Bryceson YT, et al. (2009). "Primary human tumor cells expressing CD155 impair tumor targeting by down-regulating DNAM-1 on NK cells". J. Immunol. 183 (8): 4921–30. doi:10.4049/jimmunol.0901226. PMID19801517.
Kindberg E, Ax C, Fiore L, Svensson L (2009). "Ala67Thr mutation in the poliovirus receptor CD155 is a potential risk factor for vaccine and wild-type paralytic poliomyelitis". J. Med. Virol. 81 (5): 933–6. doi:10.1002/jmv.21444. PMID19319949.
Bachelet I, Munitz A, Mankutad D, Levi-Schaffer F (2006). "Mast cell costimulation by CD226/CD112 (DNAM-1/Nectin-2): a novel interface in the allergic process". J. Biol. Chem. 281 (37): 27190–6. doi:10.1074/jbc.M602359200. PMID16831868.
Meyer D, Seth S, Albrecht J, et al. (2009). "CD96 interaction with CD155 via its first Ig-like domain is modulated by alternative splicing or mutations in distal Ig-like domains". J. Biol. Chem. 284 (4): 2235–44. doi:10.1074/jbc.M807698200. PMID19056733.
Pende D, Castriconi R, Romagnani P, et al. (2006). "Expression of the DNAM-1 ligands, Nectin-2 (CD112) and poliovirus receptor (CD155), on dendritic cells: relevance for natural killer-dendritic cell interaction". Blood. 107 (5): 2030–6. doi:10.1182/blood-2005-07-2696. PMID16304049.