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Poliovirus receptor-related 2 (herpesvirus entry mediator B)
Symbols PVRL2 ; CD112; HVEB; PRR2; PVRR2
External IDs Template:OMIM5
RNA expression pattern
File:PBB GE PVRL2 203149 at tn.png
More reference expression data
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Poliovirus receptor-related 2 (herpesvirus entry mediator B), also known as PVRL2 and CD112 (Cluster of Differentiation 112), is a human gene.[1]

This gene encodes a single-pass type I membrane glycoprotein with two Ig-like C2-type domains and an Ig-like V-type domain. This protein is one of the plasma membrane components of adherens junctions. It also serves as an entry for certain mutant strains of herpes simplex virus and pseudorabies virus, and it is involved in cell to cell spreading of these viruses. Variations in this gene have been associated with differences in the severity of multiple sclerosis. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.[1]

See also


  1. 1.0 1.1 "Entrez Gene: PVRL2 poliovirus receptor-related 2 (herpesvirus entry mediator B)".

Further reading

  • Eberlé F, Dubreuil P, Mattei MG; et al. (1995). "The human PRR2 gene, related to the human poliovirus receptor gene (PVR), is the true homolog of the murine MPH gene". Gene. 159 (2): 267–72. PMID 7622062.
  • Warner MS, Geraghty RJ, Martinez WM; et al. (1998). "A cell surface protein with herpesvirus entry activity (HveB) confers susceptibility to infection by mutants of herpes simplex virus type 1, herpes simplex virus type 2, and pseudorabies virus". Virology. 246 (1): 179–89. doi:10.1006/viro.1998.9218. PMID 9657005.
  • Freistadt MS, Eberle KE (1998). "Physical association between CD155 and CD44 in human monocytes". Mol. Immunol. 34 (18): 1247–57. PMID 9683266.
  • Lopez M, Aoubala M, Jordier F; et al. (1999). "The human poliovirus receptor related 2 protein is a new hematopoietic/endothelial homophilic adhesion molecule". Blood. 92 (12): 4602–11. PMID 9845526.
  • Shukla D, Rowe CL, Dong Y; et al. (1999). "The murine homolog (Mph) of human herpesvirus entry protein B (HveB) mediates entry of pseudorabies virus but not herpes simplex virus types 1 and 2". J. Virol. 73 (5): 4493–7. PMID 10196354.
  • Takahashi K, Nakanishi H, Miyahara M; et al. (1999). "Nectin/PRR: an immunoglobulin-like cell adhesion molecule recruited to cadherin-based adherens junctions through interaction with Afadin, a PDZ domain-containing protein". J. Cell Biol. 145 (3): 539–49. PMID 10225955.
  • Freitas EM, Zhang WJ, Lalonde JP; et al. (1999). "Sequencing of 42kb of the APO E-C2 gene cluster reveals a new gene: PEREC1". DNA Seq. 9 (2): 89–100. PMID 10520737.
  • Lopez M, Cocchi F, Menotti L; et al. (2000). "Nectin2alpha (PRR2alpha or HveB) and nectin2delta are low-efficiency mediators for entry of herpes simplex virus mutants carrying the Leu25Pro substitution in glycoprotein D.". J. Virol. 74 (3): 1267–74. PMID 10627537.
  • Cocchi F, Menotti L, Dubreuil P; et al. (2000). "Cell-to-cell spread of wild-type herpes simplex virus type 1, but not of syncytial strains, is mediated by the immunoglobulin-like receptors that mediate virion entry, nectin1 (PRR1/HveC/HIgR) and nectin2 (PRR2/HveB)". J. Virol. 74 (8): 3909–17. PMID 10729168.
  • Bouchard MJ, Dong Y, McDermott BM; et al. (2000). "Defects in nuclear and cytoskeletal morphology and mitochondrial localization in spermatozoa of mice lacking nectin-2, a component of cell-cell adherens junctions". Mol. Cell. Biol. 20 (8): 2865–73. PMID 10733589.
  • Martinez WM, Spear PG (2001). "Structural features of nectin-2 (HveB) required for herpes simplex virus entry". J. Virol. 75 (22): 11185–95. doi:10.1128/JVI.75.22.11185-11195.2001. PMID 11602758.
  • Freitas EM, Phan TC, Herbison CE; et al. (2002). "The poliovirus receptor related 2 (PRR2) and apolipoprotein E genes and coronary heart disease". Journal of cardiovascular risk. 9 (1): 59–65. PMID 11984219.
  • Fabre S, Reymond N, Cocchi F; et al. (2002). "Prominent role of the Ig-like V domain in trans-interactions of nectins. Nectin3 and nectin 4 bind to the predicted C-C'-C"-D beta-strands of the nectin1 V domain". J. Biol. Chem. 277 (30): 27006–13. doi:10.1074/jbc.M203228200. PMID 12011057.
  • Struyf F, Martinez WM, Spear PG (2002). "Mutations in the N-terminal domains of nectin-1 and nectin-2 reveal differences in requirements for entry of various alphaherpesviruses and for nectin-nectin interactions". J. Virol. 76 (24): 12940–50. PMID 12438620.
  • Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
  • Bottino C, Castriconi R, Pende D; et al. (2003). "Identification of PVR (CD155) and Nectin-2 (CD112) as cell surface ligands for the human DNAM-1 (CD226) activating molecule". J. Exp. Med. 198 (4): 557–67. doi:10.1084/jem.20030788. PMID 12913096.
  • Zago A, Spear PG (2003). "Differences in the N termini of herpes simplex virus type 1 and 2 gDs that influence functional interactions with the human entry receptor Nectin-2 and an entry receptor expressed in Chinese hamster ovary cells". J. Virol. 77 (17): 9695–9. PMID 12915581.
  • Tahara-Hanaoka S, Shibuya K, Onoda Y; et al. (2005). "Functional characterization of DNAM-1 (CD226) interaction with its ligands PVR (CD155) and nectin-2 (PRR-2/CD112)". Int. Immunol. 16 (4): 533–8. PMID 15039383.
  • Brandenberger R, Wei H, Zhang S; et al. (2005). "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation". Nat. Biotechnol. 22 (6): 707–16. doi:10.1038/nbt971. PMID 15146197.
  • Rosche B, Cepok S, Stei S; et al. (2004). "The role of the polio virus receptor and the herpesvirus entry mediator B genes for the development of MS". J. Neuroimmunol. 156 (1–2): 171–7. doi:10.1016/j.jneuroim.2004.07.001. PMID 15465608.

External links

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

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