| Gene Name | SIGLEC1 |
| HF Protein Name | Sialoadhesin |
| HF Function | Essential for viral entry |
| Uniprot ID | A7LCJ3 |
| Protein Sequence | View Fasta Sequence |
| NCBI Gene ID | 397623 |
| Host Factor (HF) Name in Paper | SIGLEC1 |
| Gene synonyms | SA SN |
| Ensemble Gene ID | N.A |
| Ensemble Transcript | N.A. |
| KEGG ID | Go to KEGG Database |
| Gene Ontology ID(s) | GO:0001618, GO:0005769, GO:0005770, GO:0005886, GO:0007155, GO:0016021, GO:0030139, GO:0030246, GO:0046718, GO:0046790, GO:0050765, GO:0072583, GO:0075512, |
| 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) | N.A., |
| pfam ID | PF08205, PF07679, PF13895, PF07686, |
| 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 | Involvement of sialoadhesin in entry of porcine reproductive and respiratory syndrome virus into porcine alveolar macrophages |
| Author's Name | Nathalie Vanderheijden, Peter L. Delputte, Herman W. Favoreel, Jo ?el Vandekerckhove, Jozef Van Damme, Peter A. van Woensel and Hans J. Nauwynck |
| Journal Name | Journal of Virology |
| Pubmed ID | 12857889 |
| Abstract | Porcine reproductive and respiratory syndrome virus (PRRSV) shows a very restricted tropism for cells of the monocyte/macrophage lineage. It enters cells via receptor-mediated endocytosis. A monoclonal antibody (MAb) that is able to block PRRSV infection of porcine alveolar macrophages (PAM) and that recognizes a 210-kDa protein (p210) was described previously (MAb41D3) (X. Duan, H. Nauwynck, H. Favoreel, and M. Pensaert, J. Virol. 72:4520-4523, 1998). In the present study, the p210 protein was purified from PAM by immunoaffinity using MAb41D3 and was subjected to internal peptide sequencing after tryptic digestion. Amino acid sequence identities ranging from 56 to 91% with mouse sialoadhesin, a macrophage-restricted receptor, were obtained with four p210 peptides. Using these peptide data, the full p210 cDNA sequence (5,193 bp) was subsequently determined. It shared 69 and 78% amino acid identity, respectively, with mouse and human sialoadhesins. Swine (PK-15) cells resistant to viral entry were transfected with the cloned p210 cDNA and inoculated with European or American PRRSV strains. Internalized virus particles were detected only in PK-15 cells expressing the recombinant sialoadhesin, demonstrating that this glycoprotein mediated uptake of both types of strains. However, nucleocapsid disintegration, like that observed in infected Marc-145 cells as a result of virus uncoating after fusion of the virus with the endocytic vesicle membrane, was not observed, suggesting a block in the fusion process. The ability of porcine sialoadhesin to mediate endocytosis was demonstrated by specific internalization of MAb41D3 into PAM. Altogether, these results show that sialoadhesin is involved in the entry process of PRRSV in PAM. |
| Used Model | PK-15 cells |
| DOI | 10.1128/JVI.77.15.8207-8215.2003 |
