CD155

CD155 (cluster of differentiation 155) also known as the poliovirus receptor is a protein that in humans is encoded by the PVR gene.[3][4]

PVR
Available structures
PDBHuman UniProt search: PDBe RCSB
Identifiers
AliasesPVR, CD155, HVED, NECL5, Necl-5, PVS, TAGE4, poliovirus receptor, PVR cell adhesion molecule
External IDsOMIM: 173850 HomoloGene: 9672 GeneCards: PVR
Gene location (Human)
Chr.Chromosome 19 (human)[1]
Band19q13.31Start44,643,798 bp[1]
End44,666,162 bp[1]
Orthologs
SpeciesHumanMouse
Entrez

5817

n/a

Ensembl

ENSG00000073008

n/a

UniProt

P15151

n/a

RefSeq (mRNA)

NM_001135768
NM_001135769
NM_001135770
NM_006505

n/a

RefSeq (protein)

NP_001129240
NP_001129241
NP_001129242
NP_006496

n/a

Location (UCSC)Chr 19: 44.64 – 44.67 Mbn/a
PubMed search[2]n/a
Wikidata
View/Edit Human

Function

CD155 is a Type I transmembrane glycoprotein in the immunoglobulin superfamily.[5] Commonly known as Poliovirus Receptor (PVR) due to its involvement in the cellular poliovirus infection in primates, CD155's normal cellular function is in the establishment of intercellular adherens junctions between epithelial cells.[6] The role of CD155 in the immune system is unclear, though it may be involved in intestinal humoral immune responses.[6] Subsequent data has also suggested that CD155 may also be used to positively select MHC-independent T cells in the thymus.

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.[3]

Structure

CD155 is a transmembrane protein with 3 extracellular immunoglobulin-like domains, D1-D3, where D1 is recognized by the virus.[7]

Low resolution structures of CD155 complexed with poliovirus have been obtained using electron microscopy[8] while a high resolution structures of the ectodomain D1 and D2 of CD155 were solved by x-ray crystallography.[7]

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See also

  • 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.

References

  1. GRCh38: Ensembl release 89: ENSG00000073008 - Ensembl, May 2017
  2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. "Entrez Gene: poliovirus receptor".
  4. Koike S, Horie H, Ise I, Okitsu A, Yoshida M, Iizuka N, Takeuchi K, Takegami T, Nomoto A (October 1990). "The poliovirus receptor protein is produced both as membrane-bound and secreted forms". EMBO J. 9 (10): 3217–24. doi:10.1002/j.1460-2075.1990.tb07520.x. PMC 552052. PMID 2170108.
  5. 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. PMID 2538245.
  6. Maier 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. PMID 17621371.
  7. PDB: 3epc, 3epd, 3epf, 3eow; Zhang P, Mueller S, Morais MC, Bator CM, Bowman VD, Hafenstein S, Wimmer E, Rossmann MG (November 2008). "Crystal structure of CD155 and electron microscopic studies of its complexes with polioviruses". Proc. Natl. Acad. Sci. U.S.A. 105 (47): 18284–9. Bibcode:2008PNAS..10518284Z. doi:10.1073/pnas.0807848105. PMC 2587566. PMID 19011098.
  8. PDB: 1DGI; He Y, Bowman VD, Mueller S, Bator CM, Bella J, Peng X, Baker TS, Wimmer E, Kuhn RJ, Rossmann MG (January 2000). "Interaction of the poliovirus receptor with poliovirus". Proc. Natl. Acad. Sci. U.S.A. 97 (1): 79–84. doi:10.1073/pnas.97.1.79. PMC 26619. PMID 10618374.

Further reading

This article incorporates text from the United States National Library of Medicine, which is in the public domain.


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