Antigen families

C-type lectin receptors


Pattern recognition receptors (PRRs) are ancestral germline-encoded molecules that enable the organism to detect highly conserved structures of microbes and altered self. Danger signals thus perceived alert both innate and adaptive components of the immune system to mount the most appropriate response.
Major classes of PRRs are the C-type lectin receptors (CLRs), whose key importance in the immune system has recently been recognized (1). Interest in these molecules has particularly been fueled by the discovery that they are broadly represented on DCs, reflecting the positioning of this cell type as sensors at the interface of the immune system and the external environment (2).
CLRs perform a variety of essential functions in DCs.
First, the extracellular portion of CLRs feature one or several carbohydrate-recognition domains (CRDs) which enable binding to sugar moieties present on glycosylated antigens of self-tissue or invading microorganisms. CLRs can bind to monosaccharides as well as complex N- or O-linked glycosylation forms.
By virtue of the particular motifs within their intracytoplasmic tail, most CLRs subsequently internalize bound antigen through receptor-mediated endocytosis.
CLRs with antigen-receptor function in conventional DCs include the macrophage mannose receptor (mAb DENDRITICS), DEC205/CD205 (mAb DENDRITICS), DC-SIGN-like (mAb DENDRITICS), DC-ASGPR (MGL)/CD301 (mAb DENDRITICS: DDX0010, DDX0011) (3), Dectin-1, Langerin/CD207 (4) (mAb DENDRITICS), whereas pDCs utilize the CLR CD303 (mAb DENDRITICS) restricted to this DC subtype (5).
Antigen-capture by CLRs in the absence of a strong DC activation signal can lead to immune tolerance (6), a likely indication of the importance these receptors play to maintain homeostatic control to avoid autoimmunity to damaged self tissue.
A variety of pathogens, including HIV (7, 8) have been reported to bind to CLRs expressed by DCs. However, it is increasingly clear that pathogens have often evolved to subvert the function of host CLRs by inhibition of antigen presentation or modification of T cell responses to evade the immune system (9, 10).
Antigens associated with tumors often display aberrant glycosylation patterns. It has recently been demonstrated that DCs can recognize such modifications through their CLRs (11), opening up new perspectives for cancer immunotherapy. Taken together, it will be of considerable interest to evaluate to which extent CLRs can be manipulated for therapeutic strategies. It is noteworthy that some CLRs, such as DCIR (12) (mAb DENDRITICS) contain a potential immunosuppressive intracytoplasmic ITIM motif, while others (eg Dectin-1) are associated with an immunostimulatory function through the recruitment of ITAM-like motifs.
Finally, it has recently become apparent that the balance between immune silencing and activation is controlled by signaling crosstalk between the CLR and the Toll-like receptor (TLR) (mAb DENDRITICS) pathways (13, 14, 15).
 
References
1. W I. Weis, M E. Taylor, K Drickamer, The C-type lectin superfamily in the immune system, 1998 Immunol Rev 163: 19-34
2. Figdor CG, van Kooyk Y, Adema GJ., C-type lectin receptors on dendritic cells and Langerhans cells, 2002 Nature Rev Immunol 2: 77-84
3. Valladeau J, Duvert-Frances V, Pin JJ, Kleijmeer MJ, Ait-Yahia S, Ravel O, Vincent C, Vega F Jr, Helms A, Gorman D, Zurawski SM, Zurawski G, Ford J, Saeland S.
Immature human dendritic cells express asialoglycoprotein receptor isoforms for efficient receptor-mediated endocytosis., 2001 J Immunol 167: 5767-5774
4. Valladeau J, Duvert-Frances V, Pin JJ, Dezutter-Dambuyant C, Vincent C, Massacrier C, Vincent J, Yoneda K, Banchereau J, Caux C, Davoust J, Saeland S. The monoclonal antibody DCGM4 recognizes Langerin, a protein specific of Langerhans cells, and is rapidly internalized from the cell, 1999 Eur J Immunol 29: 2695-2704
5. Dzionek A, Sohma Y, Nagafune J, Cella M, Colonna M, Facchetti F, Gunther G, Johnston I, Lanzavecchia A, Nagasaka T, Okada T, Vermi W, Winkels G, Yamamoto T, Zysk M, Yamaguchi Y, Schmitz J., BDCA-2, a novel plasmacytoid dendritic cell-specific type II C-type lectin, mediates antigen capture and is a potent inhibitor of interferon alpha/beta induction. 2001 J Exp Med 194: 1823-1834
6. Hawiger D, Inaba K, Dorsett Y, Guo M, Mahnke K, Rivera M, Ravetch JV, Steinman RM, Nussenzweig MC., Dendritic cells induce peripheral T cell unresponsiveness under steady state conditions in vivo. 2001 J Exp Med 194: 769-779
7. 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., DC-SIGN, a dendritic cell-specific HIV-1-binding protein that enhances trans-infection of T cells 2000 Cell 100: 587-59
8. Turville SG, Cameron PU, Handley A, Lin G, Pohlmann S, Doms RW, Cunningham AL., Diversity of receptors binding HIV on dendritic cell subsets 2002 Nat Immunol 3: 975-83
9. van Kooyk and Geijtenbeek, DC-SIGN: escape mechanism for pathogens. 2003 Nat Rev Immunol 3: 697-709
10. van Kooyk Y, Engering A, Lekkerkerker AN, Ludwig IS, Geijtenbeek TB., Pathogens use carbohydrates to escape immunity induced by dendritic cells, 2004 Curr Opin Immunol 16: 488-93
 11. van Gisbergen KP, Aarnoudse CA, Meijer GA, Geijtenbeek TB, van Kooyk Y., Dendritic cells recognize tumor-specific glycosylation of carcinoembryonic antigen on colorectal cancer cells through dendritic cell-specific intercellular adhesion molecule-3-grabbing nonintegrin, 2005 Cancer Res 65: 5935-49
12. Bates EE, Fournier N, Garcia E, Valladeau J, Durand I, Pin JJ, Zurawski SM, Patel S, Abrams JS, Lebecque S, Garrone P, Saeland S. APCs express DCIR, a novel C-type lectin surface receptor containing an immunoreceptor tyrosine-based inhibitory motif., 1999, J. Immunol 163: 1973-1983
13. G D. Brown1, J Herre1, D L. Williams2, J A. Willment1, A S. J. Marshall1 and S Gordon1, Dectin-1 mediates the biological effects of beta-glucans». 2003, J Exp Med 197: 1119-1124
14. Gantner BN, Simmons RM, Canavera SJ, Akira S, Underhill DM., 2003 Collaborative induction of inflammatory responses by dectin-1 and Toll-like receptor J Exp Med 197: 1107-1117
15. Geijtenbeek TB, Van Vliet SJ, Koppel EA, Sanchez-Hernandez M, Vandenbroucke-Grauls CM, Appelmelk B, Van Kooyk Y., Mycobacteria target DC-SIGN to suppress dendritic cell function. 2003 J Exp Med 197: 7-17

Click on an antigen to find the related products.

  • ● CD303

    • No available product.
  • ● ASGPR/CD301

    • DDX0010 - 125A10.03
      DDX0010 125A10.03
      ASGPR/CD301
      Mouse IgG1

      Internalization

    • DDX0011 - 121A5.01
      DDX0011 121A5.01
      ASGPR/CD301
      Mouse IgG1

      Internalization

  • ● DCIR/CD367

    • DDX0180 - 111F8.04
      DDX0180 111F8.04
      DCIR/CD367
      Mouse IgG1
  • ● Langerin-associated lectin/Human Kupffer cell receptor homolog

    • DDX0350 - 109B8.02
      DDX0350 109B8.02
      Langerin-associated lectin/Human Kupffer cell receptor homolog
      Mouse IgG1

      Küpffer cell receptor

    • DDX0351 - 117E10.10
      DDX0351 117E10.10
      Langerin-associated lectin/Human Kupffer cell receptor homolog
      Mouse IgG1

      Küpffer cell receptor

  • ● DC SIGN-like/CD209-like

    • DDX0200 - 118A8.05
      DDX0200 118A8.05
      DC SIGN-like/CD209-like
      Mouse IgG1

      Bacterial antigen uptake

    • DDX0201 - 128G8
      DDX0201 128G8
      DC SIGN-like/CD209-like
      Mouse IgM
  • ● DC-SIGN/CD209

    • DDX0202 - 102E11.06
      DDX0202 102E11.06
      DC-SIGN/CD209
      Mouse IgG2b,k

      IHC for paraffin-embedded tissues

    • DDX0203 - 103G2.07
      DDX0203 103G2.07
      DC-SIGN/CD209
      Mouse IgG1k

      IHC for paraffin-embedded tissues

    • DDX0204 - 108C7.01
      DDX0204 108C7.01
      DC-SIGN/CD209
      Mouse IgG2b,k

      HIV gp120 binding studies

    • DDX0205 - 102F10.04
      DDX0205 102F10.04
      DC-SIGN/CD209
      Mouse IgG2b,k

      Internalization

    • DDX0208 - 120C11.01
      DDX0208 120C11.01
      DC-SIGN/CD209
      Mouse IgG2b,k

      Inhibits HIV gp120 binding to DC-SIGN

    • DDX0207 - 109H12.03
      DDX0207 109H12.03
      DC-SIGN/CD209
      Mouse IgG2a
    • DDX0209 - 111H2.02
      DDX0209 111H2.02
      DC-SIGN/CD209
      Mouse IgG2b

      IHC for paraffin-embedded tissues

  • ● Dec205/CD205 (NLDC145)

    • DDX0020 - NLDC-145
      DDX0020 NLDC-145
      Dec205/CD205 (NLDC145)
      Rat IgG2a
  • ● Langerin/CD207

    • DDX0360 - 808E10.01
      DDX0360 808E10.01
      Langerin/CD207
      Mouse IgG1

      Extracellular epitope (CRD)

    • DDX0361 - 310F7.02
      DDX0361 310F7.02
      Langerin/CD207
      Mouse IgG1

      Multi-species cross reactivity , Intracellular epitope, IHC for paraffin-embedded tissues

    • DDX0362 - 929F3.01
      DDX0362 929F3.01
      Langerin/CD207
      Rat IgG2a

      Multi-species cross reactivity, Extracellular epitope (neck domain) , IHC for paraffin-embedded tissues

    • DDX0363 - DCGM4/122D5
      DDX0363 DCGM4/122D5
      Langerin/CD207
      Mouse IgG1

      Extracellular epitope (CRD)

    • DDX0368 - 306G9
      DDX0368 306G9
      Langerin/CD207
      Mouse IgG1

      Intracellular epitope ; IHC for paraffin-embedded tissues

    • DDX0370 - 205C1
      DDX0370 205C1
      Langerin/CD207
      Mouse IgM

      Murine langerin extracellular domain (CRD)

    • DDX0373 - 923B7
      DDX0373 923B7
      Langerin/CD207
      Rat IgG2a

      Extracellular epitope (neck domain)

    • DDX0376 - 918A11
      DDX0376 918A11
      Langerin/CD207
      Rat IgG2a

      Extracellular epitope (neck domain)

    • DDX0377 - 817G7
      DDX0377 817G7
      Langerin/CD207
      Mouse IgG1

      Extracellular epitope (CRD)