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==Function==
==Function==
DC-SIGN is a C-type lectin and has a high affinity for ICAM-3 molecule.[1] It binds various microorganisms by recognizing high-mannose-containing glycoproteins on their envelops and especially functions as receptor for several viruses such as HIV and Hepatitis C.[2] [3, 4] Binding to DC-SIGN can promote HIV and Hepatitis C virus to infect T-cell from dendritic cells. [3, 4] Thus binding to DC-SIGN is an essential process for HIV infection.[5] Besides functioning as an adhesion molecule, recently some study has also shown that DC-SIGN can initiate innate immunity by modulating Toll like receptors.[6] But the detailed mechanism is not known yet. DC-SIGN together with other C-type lectins is involved in recognition of tumors by dendritic cells. And DC-SIGN is a potential engineering target for dendritic cell based cancer vaccine.[7]
DC-SIGN is a C-type lectin and has a high affinity for ICAM-3 molecule.<ref name="pmid18458800">{{cite journal | author = Khoo US, Chan KY, Chan VS, Lin CL | title = DC-SIGN and L-SIGN: the SIGNs for infection | journal = J. Mol. Med. | volume = 86 | issue = 8 | pages = 861–74 | year = 2008 | month = August | pmid = 18458800 | doi = 10.1007/s00109-008-0350-2 | url = | issn = }}</ref> It binds various microorganisms by recognizing high-mannose-containing glycoproteins on their envelops and especially functions as receptor for several viruses such as HIV and Hepatitis C.<ref name="pmid17502670">{{cite journal | author = Lozach PY, Burleigh L, Staropoli I, Amara A | title = The C type lectins DC-SIGN and L-SIGN: receptors for viral glycoproteins | journal = Methods Mol. Biol. | volume = 379 | issue = | pages = 51–68 | year = 2007 | pmid = 17502670 | doi = | url = | issn = }}</ref><ref name="pmid15166245">{{cite journal | author = Lozach PY, Amara A, Bartosch B, Virelizier JL, Arenzana-Seisdedos F, Cosset FL, Altmeyer R | title = C-type lectins L-SIGN and DC-SIGN capture and transmit infectious hepatitis C virus pseudotype particles | journal = J. Biol. Chem. | volume = 279 | issue = 31 | pages = 32035–45 | year = 2004 | month = July | pmid = 15166245 | doi = 10.1074/jbc.M402296200 | url = | issn = }}</ref><ref name="pmid10721995">{{cite journal | author = Geijtenbeek TB, Kwon DS, Torensma R, van Vliet SJ, van Duijnhoven GC, Middel J, Cornelissen IL, Nottet HS, KewalRamani VN, Littman DR, Figdor CG, van Kooyk Y | title = DC-SIGN, a dendritic cell-specific HIV-1-binding protein that enhances trans-infection of T cells | journal = Cell | volume = 100 | issue = 5 | pages = 587–97 | year = 2000 | month = March | pmid = 10721995 | doi = | url = http://linkinghub.elsevier.com/retrieve/pii/S0092-8674(00)80694-7 | issn = }}</ref> Binding to DC-SIGN can promote HIV and Hepatitis C virus to infect T-cell from dendritic cells.<ref name="pmid15166245"/><ref name="pmid10721995"/> Thus binding to DC-SIGN is an essential process for HIV infection.<ref name="pmid12021323">{{cite journal | author = Wu L, Martin TD, Vazeux R, Unutmaz D, KewalRamani VN | title = Functional evaluation of DC-SIGN monoclonal antibodies reveals DC-SIGN interactions with ICAM-3 do not promote human immunodeficiency virus type 1 transmission | journal = J. Virol. | volume = 76 | issue = 12 | pages = 5905–14 | year = 2002 | month = June | pmid = 12021323 | pmc = 136240 | doi = | url = http://jvi.asm.org/cgi/pmidlookup?view=long&pmid=12021323 | issn = }}</ref> Besides functioning as an adhesion molecule, recently some study has also shown that DC-SIGN can initiate innate immunity by modulating Toll like receptors.<ref name="pmid18998127">{{cite journal | author = den Dunnen J, Gringhuis SI, Geijtenbeek TB | title = Innate signaling by the C-type lectin DC-SIGN dictates immune responses | journal = Cancer Immunol. Immunother. | volume = | issue = | pages = | year = 2008 | month = November | pmid = 18998127 | doi = 10.1007/s00262-008-0615-1 | url = | issn = }}</ref> But the detailed mechanism is not known yet. DC-SIGN together with other C-type lectins is involved in recognition of tumors by dendritic cells. And DC-SIGN is a potential engineering target for dendritic cell based cancer vaccine.<ref name="pmid16303292">{{cite journal | author = Aarnoudse CA, Garcia Vallejo JJ, Saeland E, van Kooyk Y | title = Recognition of tumor glycans by antigen-presenting cells | journal = Curr. Opin. Immunol. | volume = 18 | issue = 1 | pages = 105–11 | year = 2006 | month = February | pmid = 16303292 | doi = 10.1016/j.coi.2005.11.001 | url = | issn = }}</ref>
⚫
<!-- ==Gene and protein structure== -->
1. Khoo, U.S., et al., DC-SIGN and L-SIGN: the SIGNs for infection. J Mol Med, 2008. 86(8): p. 861-74.
⚫
<!-- ==Tissue expression and regulation== -->
2. Lozach, P.Y., et al., The C type lectins DC-SIGN and L-SIGN: receptors for viral glycoproteins. Methods Mol Biol, 2007. 379: p. 51-68.
3. Lozach, P.Y., et al., C-type lectins L-SIGN and DC-SIGN capture and transmit infectious hepatitis C virus pseudotype particles. J Biol Chem, 2004. 279(31): p. 32035-45.
4. Geijtenbeek, T.B., et al., DC-SIGN, a dendritic cell-specific HIV-1-binding protein that enhances trans-infection of T cells. Cell, 2000. 100(5): p. 587-97.
5. Wu, L., et al., Functional evaluation of DC-SIGN monoclonal antibodies reveals DC-SIGN interactions with ICAM-3 do not promote human immunodeficiency virus type 1 transmission. J Virol, 2002. 76(12): p. 5905-14.
6. den Dunnen, J., S.I. Gringhuis, and T.B. Geijtenbeek, Innate signaling by the C-type lectin DC-SIGN dictates immune responses. Cancer Immunol Immunother, 2008.
7. Aarnoudse, C.A., et al., Recognition of tumor glycans by antigen-presenting cells. Curr Opin Immunol, 2006. 18(1): p. 105-11.



⚫
==Gene and protein structure==
⚫
==Tissue expression and regulation== -->


==Role in HIV infection==
==Role in HIV infection==

Revision as of 21:32, 6 January 2009

Template:PBB DC-SIGN (Dendritic Cell-Specific Intercellular adhesion molecule-3-Grabbing Non-integrin) also known as CD209 (Cluster of Differentiation 209) is a protein which in humans is encoded by the CD209 gene.[1]

DC-SIGN is a C-type lectin receptor present on both macrophages and dendritic cells. DC-SIGN on macrophages recognises and binds to mannose type carbohydrates, a class of Pathogen associated molecular patterns PAMPs commonly found on viruses, bacteria and fungi. This binding interaction activates phagocytosis.[2] On myeloid and pre-plasmacytoid dendritic cells DC-SIGN mediates dendritic cell rolling interactions with blood endothelium and activation of CD4+ T cells, as well as recognition of pathogen haptens.

Function

DC-SIGN is a C-type lectin and has a high affinity for ICAM-3 molecule.[3] It binds various microorganisms by recognizing high-mannose-containing glycoproteins on their envelops and especially functions as receptor for several viruses such as HIV and Hepatitis C.[4][5][6] Binding to DC-SIGN can promote HIV and Hepatitis C virus to infect T-cell from dendritic cells.[5][6] Thus binding to DC-SIGN is an essential process for HIV infection.[7] Besides functioning as an adhesion molecule, recently some study has also shown that DC-SIGN can initiate innate immunity by modulating Toll like receptors.[8] But the detailed mechanism is not known yet. DC-SIGN together with other C-type lectins is involved in recognition of tumors by dendritic cells. And DC-SIGN is a potential engineering target for dendritic cell based cancer vaccine.[9]

Role in HIV infection

This molecule is involved in the initial stages of the human immunodeficiency virus infection, as the HIV gp120 molecule causes co-internalization of the DC-SIGN molecule and HIV 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 T cells by interaction between DC-SIGN and ICAM-3.

Gene family

DC-SIGN/CD209 is a animal "C-lectin", a large and diverse family of proteins found in both prokaryotes and eukaryotes most of which are functional lectins, meaning they bind carbohydrate ligands, and whose ligand-binding affinity requires calcium (hence "C-lectin"). Among the animal C-lectins, a subfamily known as the ASGR (asialoglycoprotein receptors) group contains several sub-sub-families, many of which are important to innate immunity. 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, CD23 is, however, not expressed on dendritic cells but is a characteristic surface molecule of B lymphocytes, and LSectin is expressed on the sinusoidal endothelium of the liver. The third gene group consists of multiple paralogues of CD209. Thus, both primates and mice have multiple paralogues of CD209 more closely related to each other within the species than to their orthologous counterparts in the other species. Higher primates have at least three DC-SIGN genes, DC-SIGN, DC-SIGNL1 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 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.[10]

References

  1. ^ Curtis BM, Scharnowske S, Watson AJ (1992). "Sequence and expression of a membrane-associated C-type lectin that exhibits CD4-independent binding of human immunodeficiency virus envelope glycoprotein gp120". Proc. Natl. Acad. Sci. U.S.A. 89 (17): 8356–60. PMC 49917. PMID 1518869. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)
  2. ^ McGreal E, Miller J, Gordon S (2005). "Ligand recognition by antigen-presenting cell C-type lectin receptors". Curr Opin Immunol. 17 (1): 18–24. doi:10.1016/j.coi.2004.12.001. PMID 15653305.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  3. ^ Khoo US, Chan KY, Chan VS, Lin CL (2008). "DC-SIGN and L-SIGN: the SIGNs for infection". J. Mol. Med. 86 (8): 861–74. doi:10.1007/s00109-008-0350-2. PMID 18458800. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)
  4. ^ Lozach PY, Burleigh L, Staropoli I, Amara A (2007). "The C type lectins DC-SIGN and L-SIGN: receptors for viral glycoproteins". Methods Mol. Biol. 379: 51–68. PMID 17502670.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  5. ^ a b Lozach PY, Amara A, Bartosch B, Virelizier JL, Arenzana-Seisdedos F, Cosset FL, Altmeyer R (2004). "C-type lectins L-SIGN and DC-SIGN capture and transmit infectious hepatitis C virus pseudotype particles". J. Biol. Chem. 279 (31): 32035–45. doi:10.1074/jbc.M402296200. PMID 15166245. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link) CS1 maint: unflagged free DOI (link)
  6. ^ a b Geijtenbeek TB, Kwon DS, Torensma R, van Vliet SJ, van Duijnhoven GC, Middel J, Cornelissen IL, Nottet HS, KewalRamani VN, Littman DR, Figdor CG, van Kooyk Y (2000). "DC-SIGN, a dendritic cell-specific HIV-1-binding protein that enhances trans-infection of T cells". Cell. 100 (5): 587–97. PMID 10721995. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)
  7. ^ Wu L, Martin TD, Vazeux R, Unutmaz D, KewalRamani VN (2002). "Functional evaluation of DC-SIGN monoclonal antibodies reveals DC-SIGN interactions with ICAM-3 do not promote human immunodeficiency virus type 1 transmission". J. Virol. 76 (12): 5905–14. PMC 136240. PMID 12021323. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)
  8. ^ den Dunnen J, Gringhuis SI, Geijtenbeek TB (2008). "Innate signaling by the C-type lectin DC-SIGN dictates immune responses". Cancer Immunol. Immunother. doi:10.1007/s00262-008-0615-1. PMID 18998127. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)
  9. ^ Aarnoudse CA, Garcia Vallejo JJ, Saeland E, van Kooyk Y (2006). "Recognition of tumor glycans by antigen-presenting cells". Curr. Opin. Immunol. 18 (1): 105–11. doi:10.1016/j.coi.2005.11.001. PMID 16303292. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)
  10. ^ Ortiz M, Kaessmann H, Zhang K, Bashirova A, Carrington M, Quintana-Murci L, Telenti A (2008). "The evolutionary history of the CD209 (DC-SIGN) family in humans and non-human primates". Genes Immun. 9 (6): 483–92. doi:10.1038/gene.2008.40. PMID 18528403. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)

Further reading

Template:PBB Further reading

  • Ortiz M, Kaessmann H, Zhang K, Bashirova A, Carrington M, Quintana-Murci L, Telenti A. (2008). "The evolutionary history of the CD209 (DC-SIGN) family in humans and non-human primates". Genes Immun. 9 (6): 483–492. PMID 18528403.{{cite journal}}: CS1 maint: multiple names: authors list (link)


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


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