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DC-SIGN
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<h2 id="function">Function</h2> <p>DC-SIGN is a C-type lectin and has a high affinity for the <a href="/facts/ICAM3/xdlyw3R7">ICAM3</a> molecule.<a class="footnote-ref" id="fnref:3" href="#fn:3"><sup>3</sup></a> It binds various microorganisms by recognizing high-<a href="/facts/Mannose/U05bJ7p8">mannose</a>-containing <a href="/facts/Glycoprotein/bKPzzW7m">glycoproteins</a> on their surface, and can function as a co-receptor for several viruses such as <a href="/facts/HIV/ulY2rgzu">HIV</a> and <a href="/facts/Hepatitis_C/kwb7IIht">Hepatitis C</a>.<a class="footnote-ref" id="fnref:4" href="#fn:4"><sup>4</sup></a><a class="footnote-ref" id="fnref:5" href="#fn:5"><sup>5</sup></a><a class="footnote-ref" id="fnref:6" href="#fn:6"><sup>6</sup></a> Binding to DC-SIGN can promote HIV and Hepatitis C virus to infect target cells (T-cells and hepatocytes, respectively).<a class="footnote-ref" id="fnref:7" href="#fn:7"><sup>7</sup></a><a class="footnote-ref" id="fnref:8" href="#fn:8"><sup>8</sup></a> </p><p>Besides functioning as an <a href="/facts/Cell_adhesion/Vg4alzxb">adhesion</a> molecule, recent studies have also shown that DC-SIGN can initiate innate immunity by modulating <a href="/facts/Toll-like_receptor/hj4qIWP8">toll-like receptors</a>,<a class="footnote-ref" id="fnref:9" href="#fn:9"><sup>9</sup></a> though the detailed mechanism is not yet known. DC-SIGN together with other C-type lectins is involved in recognition of tumors by dendritic cells. DC-SIGN is also a potential engineering target for dendritic cell based cancer vaccine.<a class="footnote-ref" id="fnref:10" href="#fn:10"><sup>10</sup></a> </p> <h2 id="clinical-significance">Clinical significance</h2> <h3>HIV infection</h3> <p>This <a href="/facts/Molecule/N9ljSfFq">molecule</a> is involved in the initial stages of the <a href="/facts/HIV/ulY2rgzu">human immunodeficiency virus</a> infection, as the HIV <a href="/facts/Gp120/WMsnFax4">gp120</a> molecule causes co-internalization of the DC-SIGN molecule and HIV virus particle (virion). The dendritic cell then migrates to the cognate lymphoid organ, whereupon recycling of the DC-SIGN/HIV virion complex to the cell periphery facilitates HIV infection of CD4+ T cells by interaction between DC-SIGN and ICAM-3.<a class="footnote-ref" id="fnref:11" href="#fn:11"><sup>11</sup></a> </p> <h3>Ebola infection</h3> <p>Different studies have demonstrated that the <a href="/facts/Zaire_ebolavirus/BneCtC2m">ebola virus</a> infection process starts when the virus reaches the cellular DC-SIGN receptor to infect the dendritic cells (of the immune system). In 2015 European researchers designed a “giant” molecule formed by thirteen fullerenes covered by carbohydrates which, by blocking DC-SIGN receptor, are able to inhibit the cell infection by an artificial ebola virus model. These antiviral molecules decorated with specific carbohydrates (sugars) present affinity by the receptor used as an entry point to infect the cell and act blocking it, thus inhibiting the infection in a sub-nanomolar range.<a class="footnote-ref" id="fnref:12" href="#fn:12"><sup>12</sup></a> </p> <h3>SARS-CoV-2</h3> <p>Similarly to HIV-1 gp120 binding, both DC-SIGN and its homologue <a href="/facts/CLEC4M/59lmuo7a">L-SIGN (CD209L or CD299)</a> have also been identified as receptors facilitating the entry of <a href="/facts/SARS-CoV-2/DxF8rDc1">Severe acute respiratory syndrome coronavirus 2</a> (SARS-CoV-2) into human cells.<a class="footnote-ref" id="fnref:13" href="#fn:13"><sup>13</sup></a> Significant CD209L expression has been revealed in lung and kidney epithelia and endothelia and interactions with <a href="/facts/Coronavirus_spike_protein/JTcbvUn2">SARS-CoV-2 Spike protein</a> (S protein) have been demonstrated in vitro.<a class="footnote-ref" id="fnref:14" href="#fn:14"><sup>14</sup></a><a class="footnote-ref" id="fnref:15" href="#fn:15"><sup>15</sup></a> CD209L also exhibits interaction with <a href="/facts/Angiotensin-converting_enzyme_2/jCDTv3ur">Angiotensin-converting enzyme-2</a> (ACE2), suggesting a potential role for CD209L-ACE2 heterodimerization in SARS-CoV-2 entry and infection in cell types expressing both proteins.<a class="footnote-ref" id="fnref:16" href="#fn:16"><sup>16</sup></a> It is shown that DC/L-SIGN can enhance viral infection and dissemination by contributing to additional routes of infection mediated by the S protein in a process called trans-infection.<a class="footnote-ref" id="fnref:17" href="#fn:17"><sup>17</sup></a> This process seems to be exclusive for DC/L-SIGN interaction. This complexity in the recognition patterns and functions of these C-lectin receptors is similar to what has been described for other viruses (like HIV and Ebola virus) and thus both DC/L-SIGN are considered as <a href="/facts/Pattern_recognition_receptor/ItopNrK0">pattern recognition receptors (PRR)</a>. </p> <h2 id="gene-family">Gene family</h2> <p>DC-SIGN/CD209 is an animal "C-lectin", a large and diverse family of proteins found in both <a href="/facts/Prokaryote/oYyvaDDH">prokaryotes</a> and <a href="/facts/Eukaryote/SkwyPLMA">eukaryotes</a> most of which are functional <a href="/facts/Lectins/I7Clqx4X">lectins</a>, meaning they bind carbohydrate <a href="/facts/Ligand_(biochemistry)/44QLL4eU">ligands</a>, and whose ligand-binding affinity requires calcium (hence "C-lectin"). Among the animal C-lectins, a subfamily known as the ASGR (<a href="/facts/Asialoglycoprotein_receptor/SvQEXJ3T">asialoglycoprotein receptors</a>) group contains several sub-sub-families, many of which are important to <a href="/facts/Innate_immunity/lz4BpSQI">innate immunity</a>. </p><p>A cluster of genes in both humans and mice contains three related members of the "DC Receptor" class, so named because of their homology to DC-SIGN. Of these, <a href="/facts/CD23/sdk79KrG">CD23</a> is, however, not expressed on dendritic cells but is a characteristic surface molecule of <a href="/facts/B_lymphocyte/6Y1tgwwp">B lymphocytes</a>, and LSectin (CLEC4G) is expressed on the sinusoidal endothelium of the liver. The third gene group consists of multiple <a href="/facts/Homology_(biology)/muctKlyT">paralogues</a> of CD209. Thus, both primates and mice have multiple paralogues of CD209 more closely related to each other within the species than to their <a href="/facts/Homology_(biology)/muctKlyT">orthologous</a> counterparts in the other species. Higher primates have at least three DC-SIGN genes, DC-SIGN, <a href="/facts/CLEC4M/59lmuo7a">DC-SIGNL1</a> (also known as DC-SIGNR or L-SIGN<a class="footnote-ref" id="fnref:18" href="#fn:18"><sup>18</sup></a>) and DC-SIGNL2, although not all three are present in every species; DC-SIGNL2 has not been detected in humans. Eight paralogous of DC-SIGN have been reported in the laboratory mouse strain C57BL/6; these go by the names DC-SIGN, DC-SIGNR2...DC-SIGNR8. DC-SIGNR6 is a pseudogene. The genes labeled "DC-SIGN" in the human and mouse are thus not unique orthologues, although they resemble each other functionally and by being expressed on dendritic cells. Other members of the mouse CD209 gene group are differentially expressed on different cell types. For example, DC-SIGNR1 is expressed largely on macrophages in the marginal zones of the spleen and in the medulla of lymph nodes.<a class="footnote-ref" id="fnref:19" href="#fn:19"><sup>19</sup></a> </p> <h2 id="further-reading">Further reading</h2> <ul><li>Geijtenbeek TB, Engering A, Van Kooyk Y (June 2002). <a href="https://doi.org/10.1189%2Fjlb.71.6.921">"DC-SIGN, a C-type lectin on dendritic cells that unveils many aspects of dendritic cell biology"</a>. <i>Journal of Leukocyte Biology</i>. 71 (6): 921–931. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1189%2Fjlb.71.6.921">10.1189/jlb.71.6.921</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/12050176">12050176</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:42418837">42418837</a>.</li> <li>Baribaud F, Doms RW, Pöhlmann S (August 2002). "The role of DC-SIGN and DC-SIGNR in HIV and Ebola virus infection: can potential therapeutics block virus transmission and dissemination?". <i>Expert Opinion on Therapeutic Targets</i>. 6 (4): 423–431. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1517%2F14728222.6.4.423">10.1517/14728222.6.4.423</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/12223058">12223058</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:21541850">21541850</a>.</li> <li>Bénichou S, Benmerah A (January 2003). <a href="https://doi.org/10.1051%2Fmedsci%2F2003191100">"[The HIV nef and the Kaposi-sarcoma-associated virus K3/K5 proteins: "parasites"of the endocytosis pathway]"</a>. <i>Médecine/Sciences</i>. 19 (1): 100–106. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1051%2Fmedsci%2F2003191100">10.1051/medsci/2003191100</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/12836198">12836198</a>.</li> <li>van Kooyk Y, Geijtenbeek TB (September 2003). "DC-SIGN: escape mechanism for pathogens". <i>Nature Reviews. Immunology</i>. 3 (9): 697–709. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1038%2Fnri1182">10.1038/nri1182</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/12949494">12949494</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:13547669">13547669</a>.</li> <li>Turville S, Wilkinson J, Cameron P, Dable J, Cunningham AL (November 2003). <a href="https://doi.org/10.1189%2Fjlb.0503208">"The role of dendritic cell C-type lectin receptors in HIV pathogenesis"</a>. <i>Journal of Leukocyte Biology</i>. 74 (5): 710–718. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1189%2Fjlb.0503208">10.1189/jlb.0503208</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/12960229">12960229</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:44539239">44539239</a>.</li> <li>Cambi A, Figdor CG (October 2003). "Dual function of C-type lectin-like receptors in the immune system". <i>Current Opinion in Cell Biology</i>. 15 (5): 539–546. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2Fj.ceb.2003.08.004">10.1016/j.ceb.2003.08.004</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/14519388">14519388</a>.</li> <li>Joseph AM, Kumar M, Mitra D (January 2005). "Nef: "necessary and enforcing factor" in HIV infection". <i>Current HIV Research</i>. 3 (1): 87–94. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.2174%2F1570162052773013">10.2174/1570162052773013</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/15638726">15638726</a>.</li> <li>Stove V, Verhasselt B (January 2006). "Modelling thymic HIV-1 Nef effects". <i>Current HIV Research</i>. 4 (1): 57–64. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.2174%2F157016206775197583">10.2174/157016206775197583</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/16454711">16454711</a>.</li> <li>Ortiz M, Kaessmann H, Zhang K, Bashirova A, Carrington M, Quintana-Murci L, et al. (September 2008). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2701223">"The evolutionary history of the CD209 (DC-SIGN) family in humans and non-human primates"</a>. <i>Genes and Immunity</i>. 9 (6): 483–492. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1038%2Fgene.2008.40">10.1038/gene.2008.40</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2701223">2701223</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/18528403">18528403</a>.</li> <li>Becer CR, Gibson MI, Geng J, Ilyas R, Wallis R, Mitchell DA, et al. (November 2010). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3091610">"High-affinity glycopolymer binding to human DC-SIGN and disruption of DC-SIGN interactions with HIV envelope glycoprotein"</a>. <i>Journal of the American Chemical Society</i>. 132 (43): 15130–15132. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1021%2Fja1056714">10.1021/ja1056714</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3091610">3091610</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/20932025">20932025</a>.</li></ul> <h2 id="external-links">External links</h2> <ul><li><a href="https://meshb.nlm.nih.gov/record/ui?name=DC-SIGN">DC-SIGN</a> at the U.S. National Library of Medicine <a href="/facts/Medical_Subject_Headings/C57g2JuF">Medical Subject Headings</a> (MeSH)</li></ul> <p><i>This article incorporates text from the <a href="/facts/United_States_National_Library_of_Medicine/Hzty0MCX">United States National Library of Medicine</a>, which is in the <a href="/facts/Public_domain/YWKMDKw4">public domain</a>.</i> </p> <h2 id="references">References</h2> <ol> <li id="fn:1"><p>Curtis BM, Scharnowske S, Watson AJ (September 1992). "Sequence and expression of a membrane-associated C-type lectin that exhibits CD4-independent binding of human immunodeficiency virus envelope glycoprotein gp120". Proceedings of the National Academy of Sciences of the United States of America. 89 (17): 8356–8360. Bibcode:1992PNAS...89.8356C. doi:10.1073/pnas.89.17.8356. PMC 49917. PMID 1518869. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC49917" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC49917</a> <a href="#fnref:1" class="footnote-back-ref">↩</a></p></li> <li id="fn:2"><p>McGreal EP, Miller JL, Gordon S (February 2005). "Ligand recognition by antigen-presenting cell C-type lectin receptors". Current Opinion in Immunology. 17 (1): 18–24. doi:10.1016/j.coi.2004.12.001. PMC 7126011. 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