| Gene Name | CD163 |
| HF Protein Name | Scavenger receptor cysteine-rich type 1 protein M130 |
| HF Function | Essential for viral entry |
| Uniprot ID | Q2VL90 |
| Protein Sequence | View Fasta Sequence |
| NCBI Gene ID | 397031 |
| Host Factor (HF) Name in Paper | CD163 |
| Gene synonyms | M130 |
| Ensemble Gene ID | N.A |
| Ensemble Transcript | N.A. |
| KEGG ID | Go to KEGG Database |
| Gene Ontology ID(s) | GO:0001618, GO:0005044, GO:0005576, GO:0005886, GO:0006953, GO:0016021, |
| MINT ID | N.A. |
| STRING | Click to see interaction map |
| GWAS Analysis | Click to see gwas analysis |
| OMIM ID | N.A. |
| PANTHER ID | N.A. |
| PDB ID(s) | 5HRJ, 5JFB, |
| pfam ID | PF00530, |
| Drug Bank ID | N.A., |
| ChEMBL ID | N.A. |
| Organism | Sus scrofa (Pig) |
| Virus Name | Porcine reproductive and respiratory syndrome virus |
| Virus Short Name | PRRSV |
| Order | Nidovirales |
| Virus Family | Arteriviridae |
| Virus Subfamily | N.A. |
| Genus | Porartevirus |
| Species | Porcine reproductive and respiratory syndrome virus |
| Host | Vertebrates |
| Cell Tropism | Primarily it's found in alveolar lung macrophages and macrophages of other tissues, later, is also found in testicular germ cells. |
| Associated Disease | Abortions and respiratory disease |
| Mode of Transmission | Transplacental, saliva, urine, semen and respiratory tract secretions |
| VIPR DB link | N.A. |
| ICTV DB link | https://talk.ictvonline.org/ictv-reports/ictv_9th_report/positive-sense-rna-viruses-2011/w/posrna_viruses/220/arteriviridae |
| Virus Host DB link | N.A. |
| Paper Title | Porcine, murine and human sialoadhesin (Sn/ Siglec-1/CD169): portals for porcine reproductive and respiratory syndrome virus entry into target cells |
| Author's Name | Wander Van Breedam, Mieke Verbeeck, Isaura Christiaens, Hanne Van Gorp and Hans J. Nauwynck |
| Journal Name | Journal of General Virology |
| Pubmed ID | 23740482 |
| Abstract | Porcine sialoadhesin (pSn a sialic acid-binding lectin) and porcine CD163 (pCD163) are molecules that facilitate infectious entry of porcine reproductive and respiratory syndrome virus (PRRSV) into alveolar macrophages. In this study, it was shown that murine Sn(mSn) and human Sn (hSn), like pSn, can promote PRRSV infection of pCD163-expressing cells. Intact sialic acid-binding domains are crucial, since non-sialic acid-binding mutants of pSn, mSn and hSn did not promote infection. Endodomain-deletion mutants of pSn, mSn and hSn promoted PRRSV infection less efficiently, but also showed markedly reduced expression levels, making further research into the potential role of the Sn endodomain in PRRSV receptor activity necessary. These data further complement our knowledge on Sn as an important PRRSV receptor, and suggest - in combination with other published data - that species differences in the main PRRSV entry mediators Sn and CD163 do not account for the strict host species specificity displayed by the virus. |
| Used Model | PK-15 cells |
| DOI | 10.1099/vir.0.053082-0 |
