Poliovirus receptor (PVR)
The protein contains 417 amino acids for an estimated molecular weight of 45303 Da.
Mediates NK cell adhesion and triggers NK cell effector functions. Binds two different NK cell receptors: CD96 and CD226. These interactions accumulates at the cell-cell contact site, leading to the formation of a mature immunological synapse between NK cell and target cell. This may trigger adhesion and secretion of lytic granules and IFN-gamma and activate cytotoxicity of activated NK cells. May also promote NK cell-target cell modular exchange, and PVR transfer to the NK cell. This transfer is more important in some tumor cells expressing a lot of PVR, and may trigger fratricide NK cell activation, providing tumors with a mechanism of immunoevasion. Plays a role in mediating tumor cell invasion and migration.', '(Microbial infection) Acts as a receptor for poliovirus. May play a role in axonal transport of poliovirus, by targeting virion-PVR-containing endocytic vesicles to the microtubular network through interaction with DYNLT1. This interaction would drive the virus-containing vesicle to the axonal retrograde transport.', '(Microbial infection) Acts as a receptor for Pseudorabies virus.', '(Microbial infection) Is prevented to reach cell surface upon infection by Human cytomegalovirus /HHV-5, presumably to escape immune recognition of infected cell by NK cells. (updated: April 22, 2020)
Protein identification was indicated in the following studies:
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
This protein is annotated as membranous in Gene Ontology, is annotated as membranous in UniProt, is predicted to be membranous by TOPCONS.
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| Variant | Description |
|---|---|
| dbSNP:rs1058402 | |
| dbSNP:rs35365841 | |
| dbSNP:rs203710 |
Biological Process
Adherens junction organization
Heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules
Homophilic cell adhesion via plasma membrane adhesion molecules
Positive regulation of natural killer cell mediated cytotoxicity
Positive regulation of natural killer cell mediated cytotoxicity directed against tumor cell target
Regulation of immune response
Susceptibility to natural killer cell mediated cytotoxicity
Susceptibility to T cell mediated cytotoxicity
The reference OMIM entry for this protein is 173850
Poliovirus receptor; pvr
Pvs
Cd155
Nectin-like protein 5; necl5
DESCRIPTION
PVR, or CD155, belongs to a large family of immunoglobulin (Ig)-like molecules called nectins and nectin-like proteins, which mediate cell-cell adhesion, cell migration, and cell polarization by homotypic contact or heterotypic interaction with other nectins. In addition, PVR serves as the entry receptor for poliovirus and thereby mediates human susceptibility to poliovirus infection (summary by Fuchs et al., 2004).CLONING
Primates are susceptible to poliomyelitis infection, but rodents are not; furthermore, human cells but not rodent cells are killed by poliovirus in vitro. Susceptibility to poliovirus is a function of the presence or absence of a cellular receptor to which the virus binds as the first step in poliovirus replication. Mendelsohn et al. (1986) succeeded in transforming a human poliovirus receptor gene into mouse L cells, which are ordinarily resistant to poliovirus infection because they do not bear a poliovirus receptor. Monoclonal antibody directed against the HeLa cell poliovirus receptor site was used in rosette assays to identify poliovirus-sensitive transformants. Mendelsohn et al. (1989) and Koike et al. (1990) isolated genomic and complementary DNAs for human poliovirus receptors (PVRs) from HeLa cells. Four mRNA isoforms, 2 membrane-bound and 2 secreted, were identified and shown to be generated by alternative splicing from the primary transcript. The PVRs are members of the immunoglobulin superfamily. Shepley et al. (1988) prepared a monoclonal antibody that identified a 100-kD membrane protein in HeLa cells and in human spinal cord involved in poliovirus attachment. They showed that the antigen identified by the monoclonal antibody was associated with the presence of human chromosome 19 in human-mouse hybrid cell lines. The monoclonal antibodies stained neurons in the reticular formation and clusters of brainstem neurons, consistent with the known pattern of damage caused by poliovirus infection in the brainstem. Furthermore, it reacted with human peripheral mononuclear cells, consistent with the known replication of poliovirus in Peyer patches and tonsils.GENE FUNCTION
By analysis of transgenic mice expressing human CD155, Gromeier et al. (2000) observed expression of CD155 within embryonic structures giving rise to spinal cord anterior horn motor neurons. They suggested that this expression may explain the restrictive host cell tropism of poliovirus for this cellular compartment of the central nervous system. Solecki et al. (2002) noted that CD155 is aberrantly expressed in neuroectodermal tumors. RT-PCR analysis showed that SHH (600725) treatment of teratocarcinoma cells upregulates CDC155 and that this upregulation requires an intact GLI (165220)-binding site. The authors proposed that their finding might help explain the normal function of CD155 during development and its expression in tumors. Bottino et al. (2003) immunized mice with natural killer (NK)-susceptible human target cells and obtained antibodies to PVR and nectin-2 (PVRL2; 600798). Binding analysis and flow cytometry demonstrated that both molecules bound strongly with DNAM1 (CD226; 605397), but not with other activating NK receptors, including NKp46 (NCR1; 604530) and NKp30 (NCR3; 611550). Expression of PVR or PVRL2 rendered cells susceptible to enhanced lysis in a DNAM1-dependent manner that was nearly abrogated in the presence of antibody to PVR, PVRL2, or DNAM1. Using flow cytometric analysis ... More on the omim web site
June 30, 2020: Protein entry updated
Automatic update: OMIM entry 173850 was added.
April 25, 2020: Protein entry updated
Automatic update: Entry updated from uniprot information.
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).