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Cd209a  -  CD209a antigen

Mus musculus

Synonyms: CD209, CD209 antigen-like protein A, CDSIGN, CIRE, Cire, ...
 
 
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Disease relevance of Cd209a

 

High impact information on Cd209a

  • Previous experiments have shown that antibody to specific intracellular adhesion molecule-grabbing nonintegrin (SIGN)-R1 inhibits uptake of capsular polysaccharide by marginal zone macrophages, suggesting a role for SIGN-R1 in this process [2].
  • Low doses of alphaDEC-gag, but not control Ig-gag, stimulated proliferation and IFN-gamma production by CD8(+) T cells isolated from the blood of HIV-infected donors. alphaCD205 fusion mAb was more effective for cross-presentation than alphaCD209/DC-SIGN, another abundant DC uptake receptor [4].
  • The C-type lectin SIGN-R1 mediates uptake of the capsular polysaccharide of Streptococcus pneumoniae in the marginal zone of mouse spleen [5].
  • We now find that encapsulated Streptococcus pneumoniae are rapidly cleared by these macrophages from the bloodstream, and that capture also takes place when different cell lines express SIGN-R1 after transfection [5].
  • The finding that neither SIGNR1 nor SIGNR5 binds with high affinity to specific ligands in a large panel of mammalian glycans is consistent with the suggestion that these receptors bind surface polysaccharides on bacterial and fungal pathogens in a manner analogous to serum mannose-binding protein [6].
 

Chemical compound and disease context of Cd209a

  • However, we could detect no role for CIRE/mDC-SIGN in T cell-DC interactions and the protein did not bind to pathogens known to interact with hDC-SIGN, including Leishmania mexicana, cytomegalovirus, HIV and lentiviral particles bearing the Ebolavirus glycoprotein [7].
 

Biological context of Cd209a

  • In addition to five SIGNR proteins previously described, a pseudogene, encoding a hypothetical SIGNR6, and a further two expressed proteins, SIGNR7 and SIGNR8, have been identified [6].
  • All the genes of mouse DC-SIGN and SIGNRs map to adjacent regions of chromosome 8 A1.2-1 [8].
 

Anatomical context of Cd209a

  • Taken together, this study shows that ICAM-2 strongly supports transmigration of immature DC across resting endothelium by interacting with ligands that are distinct from beta(2)-integrins and DC-SIGN homologues [9].
  • Only one gene, named mouse DC-SIGN, is highly expressed in DC, and is not found in a panel of mouse macrophage and lymphocyte cell lines [8].
  • Thus, DC-SIGN could be an efficient target for antibody-mediated delivery of T cell epitopes in vaccine development [10].
  • Certain viruses, bacteria, fungi and parasites target dendritic cells through the interaction with the cellular attachment factor DC-SIGN, making this C-type lectin an attractive target for therapeutic intervention [11].
  • Here we use carbohydrate arrays as a new approach to discovering the ligands of three recently described C-type lectin-type receptors on antigen-presenting cells: murine SIGN-R1, SIGN-R3 and langerin [12].
 

Associations of Cd209a with chemical compounds

  • The polysaccharide dextran, known from classical studies to elicit a T-independent response, and whose cellular uptake has been shown recently to be mediated by membrane-associated SIGN-R1, gave no binding signals with the soluble form of the protein [12].
  • Here, we investigated the interaction of mDC-SIGN, also termed CIRE, with the Ebolavirus glycoprotein (EBOV-GP), a ligand of hDC-SIGN [11].
 

Other interactions of Cd209a

 

Analytical, diagnostic and therapeutic context of Cd209a

  • Northern blot analysis revealed that CIRE is almost exclusively expressed in DC and was not detected in organs such as heart, brain, kidney, liver, and thymus [14].
  • Semi-quantitative RT-PCR suggested that CIRE is down-regulated upon activation [14].
  • A physical association between SIGNR1 and the TLR4-MD-2 complex was also observed by immunoprecipitation [3].

References

  1. Specific ICAM-3 grabbing nonintegrin-related 1 (SIGNR1) expressed by marginal zone macrophages is essential for defense against pulmonary Streptococcus pneumoniae infection. Koppel, E.A., Wieland, C.W., van den Berg, V.C., Litjens, M., Florquin, S., van Kooyk, Y., van der Poll, T., Geijtenbeek, T.B. Eur. J. Immunol. (2005) [Pubmed]
  2. SIGN-R1 contributes to protection against lethal pneumococcal infection in mice. Lanoue, A., Clatworthy, M.R., Smith, P., Green, S., Townsend, M.J., Jolin, H.E., Smith, K.G., Fallon, P.G., McKenzie, A.N. J. Exp. Med. (2004) [Pubmed]
  3. Association of SIGNR1 with TLR4-MD-2 enhances signal transduction by recognition of LPS in gram-negative bacteria. Nagaoka, K., Takahara, K., Tanaka, K., Yoshida, H., Steinman, R.M., Saitoh, S., Akashi-Takamura, S., Miyake, K., Kang, Y.S., Park, C.G., Inaba, K. Int. Immunol. (2005) [Pubmed]
  4. DEC-205 receptor on dendritic cells mediates presentation of HIV gag protein to CD8+ T cells in a spectrum of human MHC I haplotypes. Bozzacco, L., Trumpfheller, C., Siegal, F.P., Mehandru, S., Markowitz, M., Carrington, M., Nussenzweig, M.C., Piperno, A.G., Steinman, R.M. Proc. Natl. Acad. Sci. U.S.A. (2007) [Pubmed]
  5. The C-type lectin SIGN-R1 mediates uptake of the capsular polysaccharide of Streptococcus pneumoniae in the marginal zone of mouse spleen. Kang, Y.S., Kim, J.Y., Bruening, S.A., Pack, M., Charalambous, A., Pritsker, A., Moran, T.M., Loeffler, J.M., Steinman, R.M., Park, C.G. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  6. Widely divergent biochemical properties of the complete set of mouse DC-SIGN-related proteins. Powlesland, A.S., Ward, E.M., Sadhu, S.K., Guo, Y., Taylor, M.E., Drickamer, K. J. Biol. Chem. (2006) [Pubmed]
  7. Functional comparison of mouse CIRE/mouse DC-SIGN and human DC-SIGN. Caminschi, I., Corbett, A.J., Zahra, C., Lahoud, M., Lucas, K.M., Sofi, M., Vremec, D., Gramberg, T., Pöhlmann, S., Curtis, J., Handman, E., van Dommelen, S.L., Fleming, P., Degli-Esposti, M.A., Shortman, K., Wright, M.D. Int. Immunol. (2006) [Pubmed]
  8. Five mouse homologues of the human dendritic cell C-type lectin, DC-SIGN. Park, C.G., Takahara, K., Umemoto, E., Yashima, Y., Matsubara, K., Matsuda, Y., Clausen, B.E., Inaba, K., Steinman, R.M. Int. Immunol. (2001) [Pubmed]
  9. Migration of immature mouse DC across resting endothelium is mediated by ICAM-2 but independent of beta(2)-integrins and murine DC-SIGN homologues. Wethmar, K., Helmus, Y., L??hn, K., Jones, C., Laskowska, A., Varga, G., Grabbe, S., Lyck, R., Engelhardt, B., Bixel, M.G., Butz, S., Loser, K., Beissert, S., Ipe, U., Vestweber, D., Wild, M.K. Eur. J. Immunol. (2006) [Pubmed]
  10. A mouse C kappa-specific T cell clone indicates that DC-SIGN is an efficient target for antibody-mediated delivery of T cell epitopes for MHC class II presentation. Schjetne, K.W., Thompson, K.M., Aarvak, T., Fleckenstein, B., Sollid, L.M., Bogen, B. Int. Immunol. (2002) [Pubmed]
  11. Evidence that multiple defects in murine DC-SIGN inhibit a functional interaction with pathogens. Gramberg, T., Caminschi, I., Wegele, A., Hofmann, H., Pöhlmann, S. Virology (2006) [Pubmed]
  12. High and low affinity carbohydrate ligands revealed for murine SIGN-R1 by carbohydrate array and cell binding approaches, and differing specificities for SIGN-R3 and langerin. Galustian, C., Park, C.G., Chai, W., Kiso, M., Bruening, S.A., Kang, Y.S., Steinman, R.M., Feizi, T. Int. Immunol. (2004) [Pubmed]
  13. Antitumor effects induced by dendritic cell-based immunotherapy against established pancreatic cancer in hamsters. Akiyama, Y., Maruyama, K., Nara, N., Hojo, T., Cheng, J.Y., Mori, T., Wiltrout, R.H., Yamaguchi, K. Cancer Lett. (2002) [Pubmed]
  14. Molecular cloning of a C-type lectin superfamily protein differentially expressed by CD8alpha(-) splenic dendritic cells. Caminschi, I., Lucas, K.M., O'Keeffe, M.A., Hochrein, H., Laâbi, Y., Brodnicki, T.C., Lew, A.M., Shortman, K., Wright, M.D. Mol. Immunol. (2001) [Pubmed]
 
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