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Volumn 71, Issue 8, 2016, Pages 1145-1155

Identification and characterization of DC-SIGN-binding glycoproteins in allergenic foods

Author keywords

DC SIGN; food allergens; peanut; peanut agglutinin; soybean

Indexed keywords

CD209 ANTIGEN; PEANUT AGGLUTININ; ALLERGEN; BIOLOGICAL MARKER; CARRIER PROTEIN; CELL ADHESION MOLECULE; CELL SURFACE RECEPTOR; DC-SPECIFIC ICAM-3 GRABBING NONINTEGRIN; GLYCOPROTEIN; IMMUNOGLOBULIN E; LECTIN; LIGAND; PLANT PROTEIN; PROTEIN BINDING;

EID: 84977611636     PISSN: 01054538     EISSN: 13989995     Source Type: Journal    
DOI: 10.1111/all.12873     Document Type: Article
Times cited : (17)

References (41)
  • 1
    • 84884812281 scopus 로고    scopus 로고
    • The physiological role of DC-SIGN: a tale of mice and men
    • Garcia-Vallejo JJ, van Kooyk Y. The physiological role of DC-SIGN: a tale of mice and men. Trends Immunol 2013;34:482–486.
    • (2013) Trends Immunol , vol.34 , pp. 482-486
    • Garcia-Vallejo, J.J.1    van Kooyk, Y.2
  • 2
    • 34248544993 scopus 로고    scopus 로고
    • C-type lectin DC-SIGN modulates Toll-like receptor signaling via Raf-1 kinase-dependent acetylation of transcription factor NF-kappaB
    • Gringhuis S, den Dunnen J, Litjens M, van Het Hof B, van Kooyk Y, Geijtenbeek T. C-type lectin DC-SIGN modulates Toll-like receptor signaling via Raf-1 kinase-dependent acetylation of transcription factor NF-kappaB. Immunity 2007;26:605–616.
    • (2007) Immunity , vol.26 , pp. 605-616
    • Gringhuis, S.1    den Dunnen, J.2    Litjens, M.3    van Het Hof, B.4    van Kooyk, Y.5    Geijtenbeek, T.6
  • 4
    • 84875633828 scopus 로고    scopus 로고
    • Glycan-based DC-SIGN targeting vaccines to enhance antigen cross-presentation
    • van Kooyk Y, Unger W, Fehres C, Kalay H, García-Vallejo J. Glycan-based DC-SIGN targeting vaccines to enhance antigen cross-presentation. Mol Immunol 2013;55:143–145.
    • (2013) Mol Immunol , vol.55 , pp. 143-145
    • van Kooyk, Y.1    Unger, W.2    Fehres, C.3    Kalay, H.4    García-Vallejo, J.5
  • 6
    • 78649855748 scopus 로고    scopus 로고
    • Allergen-specific pattern recognition receptor pathways
    • Wills-Karp M. Allergen-specific pattern recognition receptor pathways. Curr Opin Immunol 2010;22:777–782.
    • (2010) Curr Opin Immunol , vol.22 , pp. 777-782
    • Wills-Karp, M.1
  • 7
    • 84857262504 scopus 로고    scopus 로고
    • Retagging identifies dendritic cell-specific intercellular adhesion molecule-3 (ICAM3)-grabbing non-integrin (DC-SIGN) protein as a novel receptor for a major allergen from house dust mite
    • Emara M, Royer PJ, Mahdavi J, Shakib F, Ghaemmaghami AM. Retagging identifies dendritic cell-specific intercellular adhesion molecule-3 (ICAM3)-grabbing non-integrin (DC-SIGN) protein as a novel receptor for a major allergen from house dust mite. J Biol Chem 2012;287:5756–5763.
    • (2012) J Biol Chem , vol.287 , pp. 5756-5763
    • Emara, M.1    Royer, P.J.2    Mahdavi, J.3    Shakib, F.4    Ghaemmaghami, A.M.5
  • 8
    • 33748509524 scopus 로고    scopus 로고
    • The major glycoprotein allergen from arachis hypogaea, Ara h 1, Is a ligand of dendritic cell-specific ICAM-grabbing nonintegrin and acts as a Th2 adjuvant in vitro
    • Shreffler WG, Castro RR, Kucuk ZY, Charlop-Powers Z, Grishina G, Yoo S et al. The major glycoprotein allergen from arachis hypogaea, Ara h 1, Is a ligand of dendritic cell-specific ICAM-grabbing nonintegrin and acts as a Th2 adjuvant in vitro. J Immunol 2006;177:3677–3685.
    • (2006) J Immunol , vol.177 , pp. 3677-3685
    • Shreffler, W.G.1    Castro, R.R.2    Kucuk, Z.Y.3    Charlop-Powers, Z.4    Grishina, G.5    Yoo, S.6
  • 9
    • 77950878748 scopus 로고    scopus 로고
    • Functional interaction of common allergens and a C-type lectin receptor, dendritic cell-specific ICAM3-grabbing non-integrin (DC-SIGN), on human dendritic cells
    • Hsu S-C, Chen C-H, Tsai S-H, Kawasaki H, Hung C-H, Chu Y-T et al. Functional interaction of common allergens and a C-type lectin receptor, dendritic cell-specific ICAM3-grabbing non-integrin (DC-SIGN), on human dendritic cells. J Biol Chem 2010;285:7903–7910.
    • (2010) J Biol Chem , vol.285 , pp. 7903-7910
    • Hsu, S.-C.1    Chen, C.-H.2    Tsai, S.-H.3    Kawasaki, H.4    Hung, C.-H.5    Chu, Y.-T.6
  • 11
    • 77957768953 scopus 로고    scopus 로고
    • Oral tolerance to food-induced systemic anaphylaxis mediated by the C-type lectin SIGNR1
    • Zhou Y, Kawasaki H, Hsu S-C, Lee RT, Yao X, Plunkett B et al. Oral tolerance to food-induced systemic anaphylaxis mediated by the C-type lectin SIGNR1. Nat Med 2010;16:1128–1133.
    • (2010) Nat Med , vol.16 , pp. 1128-1133
    • Zhou, Y.1    Kawasaki, H.2    Hsu, S.-C.3    Lee, R.T.4    Yao, X.5    Plunkett, B.6
  • 12
    • 66149141425 scopus 로고    scopus 로고
    • Identification of two pistachio allergens, Pis v 1 and Pis v 2, belonging to the 2S albumin and 11S globulin family
    • Ahn K, Bardina L, Grishina G, Beyer K, Sampson HA. Identification of two pistachio allergens, Pis v 1 and Pis v 2, belonging to the 2S albumin and 11S globulin family. Clin Exp Allergy 2009;39:926–934.
    • (2009) Clin Exp Allergy , vol.39 , pp. 926-934
    • Ahn, K.1    Bardina, L.2    Grishina, G.3    Beyer, K.4    Sampson, H.A.5
  • 13
    • 80052494754 scopus 로고    scopus 로고
    • Soybean isoflavones regulate dendritic cell function and suppress allergic sensitization to peanut
    • Masilamani M, Wei J, Bhatt S, Paul M, Yakir S, Sampson HA. Soybean isoflavones regulate dendritic cell function and suppress allergic sensitization to peanut. J Allergy Clin Immunol 2011;128:1242–1250.
    • (2011) J Allergy Clin Immunol , vol.128 , pp. 1242-1250
    • Masilamani, M.1    Wei, J.2    Bhatt, S.3    Paul, M.4    Yakir, S.5    Sampson, H.A.6
  • 14
    • 84867739470 scopus 로고    scopus 로고
    • Isoflavones, genistein and daidzein, regulate mucosal immune response by suppressing dendritic cell function
    • Wei J, Bhatt S, Chang LM, Sampson HA, Masilamani M. Isoflavones, genistein and daidzein, regulate mucosal immune response by suppressing dendritic cell function. PLoS One 2012;7:e47979.
    • (2012) PLoS One , vol.7
    • Wei, J.1    Bhatt, S.2    Chang, L.M.3    Sampson, H.A.4    Masilamani, M.5
  • 16
    • 0034067401 scopus 로고    scopus 로고
    • Peanut and soy allergy: a clinical and therapeutic dilemma
    • Sicherer SH, Sampson HA, Burks AW. Peanut and soy allergy: a clinical and therapeutic dilemma. Allergy 2000;55:515–521.
    • (2000) Allergy , vol.55 , pp. 515-521
    • Sicherer, S.H.1    Sampson, H.A.2    Burks, A.W.3
  • 18
    • 13844267013 scopus 로고    scopus 로고
    • Allergenic proteins in soybean: processing and reduction of P34 allergenicity
    • Wilson S, Blaschek K, de Mejia E. Allergenic proteins in soybean: processing and reduction of P34 allergenicity. Nutr Rev 2005;63:47–58.
    • (2005) Nutr Rev , vol.63 , pp. 47-58
    • Wilson, S.1    Blaschek, K.2    de Mejia, E.3
  • 20
    • 33749164908 scopus 로고    scopus 로고
    • Thermodynamic analysis of three state denaturation of Peanut Agglutinin
    • Dev S, Nirmala DK, Sinha S, Surolia A. Thermodynamic analysis of three state denaturation of Peanut Agglutinin. IUBMB Life 2006;58:549–555.
    • (2006) IUBMB Life , vol.58 , pp. 549-555
    • Dev, S.1    Nirmala, D.K.2    Sinha, S.3    Surolia, A.4
  • 21
    • 0021278930 scopus 로고
    • Characterization of glycoconjugates of human gastrointestinal mucosa by lectins. I. Histochemical distribution of lectin binding sites in normal alimentary tract as well as in benign and malignant gastric neoplasms
    • Fischer J, Klein PJ, Vierbuchen M, Skutta B, Uhlenbruck G, Fischer R. Characterization of glycoconjugates of human gastrointestinal mucosa by lectins. I. Histochemical distribution of lectin binding sites in normal alimentary tract as well as in benign and malignant gastric neoplasms. J Histochem Cytochem 1984;32:681–689.
    • (1984) J Histochem Cytochem , vol.32 , pp. 681-689
    • Fischer, J.1    Klein, P.J.2    Vierbuchen, M.3    Skutta, B.4    Uhlenbruck, G.5    Fischer, R.6
  • 22
    • 0032488367 scopus 로고    scopus 로고
    • Identification of intact peanut lectin in peripheral venous blood
    • Wang Q, Yu L-G, Campbell BJ, Milton JD, Rhodes JM. Identification of intact peanut lectin in peripheral venous blood. Lancet 1998;352:1831–1832.
    • (1998) Lancet , vol.352 , pp. 1831-1832
    • Wang, Q.1    Yu, L.-G.2    Campbell, B.J.3    Milton, J.D.4    Rhodes, J.M.5
  • 23
    • 78649887557 scopus 로고    scopus 로고
    • Digestion of peanut allergens Ara h 1, Ara h 2, Ara h 3, and Ara h 6: a comparative in vitro study and partial characterization of digestion-resistant peptides
    • Koppelman SJ, Hefle SL, Taylor SL, de Jong GA. Digestion of peanut allergens Ara h 1, Ara h 2, Ara h 3, and Ara h 6: a comparative in vitro study and partial characterization of digestion-resistant peptides. Mol Nutr Food Res 2010;54:1711–1721.
    • (2010) Mol Nutr Food Res , vol.54 , pp. 1711-1721
    • Koppelman, S.J.1    Hefle, S.L.2    Taylor, S.L.3    de Jong, G.A.4
  • 24
    • 0031972947 scopus 로고    scopus 로고
    • Peanut ingestion increases rectal proliferation in individuals with mucosal expression of peanut lectin receptor
    • Ryder SD, Jacyna MR, Levi AJ, Rizzi PM, Rhodes JM. Peanut ingestion increases rectal proliferation in individuals with mucosal expression of peanut lectin receptor. Gastroenterology 1998;114:44–49.
    • (1998) Gastroenterology , vol.114 , pp. 44-49
    • Ryder, S.D.1    Jacyna, M.R.2    Levi, A.J.3    Rizzi, P.M.4    Rhodes, J.M.5
  • 25
    • 2542457449 scopus 로고    scopus 로고
    • Clinical importance of cross-reactivity in food allergy
    • van Ree R. Clinical importance of cross-reactivity in food allergy. Curr Opin Allergy Clin Immunol 2004;4:235–240.
    • (2004) Curr Opin Allergy Clin Immunol , vol.4 , pp. 235-240
    • van Ree, R.1
  • 27
    • 0346672370 scopus 로고    scopus 로고
    • Soybean allergy in patients allergic to birch pollen: clinical investigation and molecular characterization of allergens
    • Mittag D, Vieths S, Vogel L, Becker WM, Rihs HP, Helbling A et al. Soybean allergy in patients allergic to birch pollen: clinical investigation and molecular characterization of allergens. J Allergy Clin Immunol 2004;113:148–154.
    • (2004) J Allergy Clin Immunol , vol.113 , pp. 148-154
    • Mittag, D.1    Vieths, S.2    Vogel, L.3    Becker, W.M.4    Rihs, H.P.5    Helbling, A.6
  • 28
    • 84867863588 scopus 로고    scopus 로고
    • Regulation of the immune response by soybean isoflavones
    • Masilamani M, Wei J, Sampson HA. Regulation of the immune response by soybean isoflavones. Immunol Res 2012;54:95–110.
    • (2012) Immunol Res , vol.54 , pp. 95-110
    • Masilamani, M.1    Wei, J.2    Sampson, H.A.3
  • 29
    • 77955484239 scopus 로고    scopus 로고
    • Molecular determinants of T cell epitope recognition to the common Timothy grass allergen
    • Oseroff C, Sidney J, Kotturi MF, Kolla R, Alam R, Broide DH et al. Molecular determinants of T cell epitope recognition to the common Timothy grass allergen. J Immunol 2010;185:943–955.
    • (2010) J Immunol , vol.185 , pp. 943-955
    • Oseroff, C.1    Sidney, J.2    Kotturi, M.F.3    Kolla, R.4    Alam, R.5    Broide, D.H.6
  • 30
    • 0031924295 scopus 로고    scopus 로고
    • Dissection of the grass allergen–specific immune response in patients with allergies and control subjects: T-cell proliferation in patients does not correlate with specific serum IgE and skin reactivity
    • Würtzen PA, van Neerven RJJ, Arnved J, Ipsen H, Sparholt SH. Dissection of the grass allergen–specific immune response in patients with allergies and control subjects: T-cell proliferation in patients does not correlate with specific serum IgE and skin reactivity. J Allergy Clin Immunol 1998;101:241–249.
    • (1998) J Allergy Clin Immunol , vol.101 , pp. 241-249
    • Würtzen, P.A.1    van Neerven, R.J.J.2    Arnved, J.3    Ipsen, H.4    Sparholt, S.H.5
  • 31
    • 2642613459 scopus 로고    scopus 로고
    • Allergen-induced bronchial hyperreactivity and eosinophilic inflammation occur in the absence of IgE in a mouse model of asthma
    • Mehlhop PD, van de Rijn M, Goldberg AB, Brewer JP, Kurup VP, Martin TR et al. Allergen-induced bronchial hyperreactivity and eosinophilic inflammation occur in the absence of IgE in a mouse model of asthma. Proc Natl Acad Sci USA 1997;94:1344–1349.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 1344-1349
    • Mehlhop, P.D.1    van de Rijn, M.2    Goldberg, A.B.3    Brewer, J.P.4    Kurup, V.P.5    Martin, T.R.6
  • 32
    • 84863393256 scopus 로고    scopus 로고
    • Interleukin-4 production by follicular helper T cells requires the conserved Il4 enhancer hypersensitivity site V
    • Vijayanand P, Seumois G, Simpson Laura J, Abdul-Wajid S, Baumjohann D, Panduro M et al. Interleukin-4 production by follicular helper T cells requires the conserved Il4 enhancer hypersensitivity site V. Immunity 2012;36:175–187.
    • (2012) Immunity , vol.36 , pp. 175-187
    • Vijayanand, P.1    Seumois, G.2    Simpson Laura, J.3    Abdul-Wajid, S.4    Baumjohann, D.5    Panduro, M.6
  • 33
    • 84874487496 scopus 로고    scopus 로고
    • Previously undescribed grass pollen antigens are the major inducers of T helper 2 cytokine-producing T cells in allergic individuals
    • Schulten V, Greenbaum JA, Hauser M, McKinney DM, Sidney J, Kolla R et al. Previously undescribed grass pollen antigens are the major inducers of T helper 2 cytokine-producing T cells in allergic individuals. Proc Natl Acad Sci USA 2013;110:3459–3464.
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. 3459-3464
    • Schulten, V.1    Greenbaum, J.A.2    Hauser, M.3    McKinney, D.M.4    Sidney, J.5    Kolla, R.6
  • 34
    • 84988911195 scopus 로고    scopus 로고
    • Allergy-associated T cell epitope repertoires are surprisingly diverse and include non-IgE reactive antigens
    • Frazier A, Schulten V, Hinz D, Oseroff C, Sidney J, Peters B et al. Allergy-associated T cell epitope repertoires are surprisingly diverse and include non-IgE reactive antigens. World Allergy Organ J 2014;7:26.
    • (2014) World Allergy Organ J , vol.7 , pp. 26
    • Frazier, A.1    Schulten, V.2    Hinz, D.3    Oseroff, C.4    Sidney, J.5    Peters, B.6
  • 35
    • 20444503737 scopus 로고    scopus 로고
    • Selective probiotic bacteria induce IL-10-producing regulatory T cells in vitro by modulating dendritic cell function through dendritic cell-specific intercellular adhesion molecule 3-grabbing nonintegrin
    • Smits HH, Engering A, van der Kleij D, de Jong EC, Schipper K, van Capel TM et al. Selective probiotic bacteria induce IL-10-producing regulatory T cells in vitro by modulating dendritic cell function through dendritic cell-specific intercellular adhesion molecule 3-grabbing nonintegrin. J Allergy Clin Immunol 2005;115:1260–1267.
    • (2005) J Allergy Clin Immunol , vol.115 , pp. 1260-1267
    • Smits, H.H.1    Engering, A.2    van der Kleij, D.3    de Jong, E.C.4    Schipper, K.5    van Capel, T.M.6
  • 36
    • 42249084604 scopus 로고    scopus 로고
    • Mannose-capped lipoarabinomannan- and prostaglandin E2-dependent expansion of regulatory T cells in human Mycobacterium tuberculosis infection
    • Garg A, Barnes PF, Roy S, Quiroga MF, Wu S, Garcia VE et al. Mannose-capped lipoarabinomannan- and prostaglandin E2-dependent expansion of regulatory T cells in human Mycobacterium tuberculosis infection. Eur J Immunol 2008;38:459–469.
    • (2008) Eur J Immunol , vol.38 , pp. 459-469
    • Garg, A.1    Barnes, P.F.2    Roy, S.3    Quiroga, M.F.4    Wu, S.5    Garcia, V.E.6
  • 37
    • 84856886605 scopus 로고    scopus 로고
    • Bifidobacterium infantis 35624 administration induces Foxp3 T regulatory cells in human peripheral blood: potential role for myeloid and plasmacytoid dendritic cells
    • Konieczna P, Groeger D, Ziegler M, Frei R, Ferstl R, Shanahan F et al. Bifidobacterium infantis 35624 administration induces Foxp3 T regulatory cells in human peripheral blood: potential role for myeloid and plasmacytoid dendritic cells. Gut 2012;61:354–366.
    • (2012) Gut , vol.61 , pp. 354-366
    • Konieczna, P.1    Groeger, D.2    Ziegler, M.3    Frei, R.4    Ferstl, R.5    Shanahan, F.6
  • 38
    • 13844322103 scopus 로고    scopus 로고
    • Distinct functions of DC-SIGN and its homologues L-SIGN (DC-SIGNR) and mSIGNR1 in pathogen recognition and immune regulation
    • Koppel EA, van Gisbergen KP, Geijtenbeek TB, van Kooyk Y. Distinct functions of DC-SIGN and its homologues L-SIGN (DC-SIGNR) and mSIGNR1 in pathogen recognition and immune regulation. Cell Microbiol 2005;7:157–165.
    • (2005) Cell Microbiol , vol.7 , pp. 157-165
    • Koppel, E.A.1    van Gisbergen, K.P.2    Geijtenbeek, T.B.3    van Kooyk, Y.4
  • 39
    • 73149106810 scopus 로고    scopus 로고
    • Induction of Th1/Th17 immune response by Mycobacterium tuberculosis: role of dectin-1, mannose receptor, and DC-SIGN
    • Zenaro E, Donini M, Dusi S. Induction of Th1/Th17 immune response by Mycobacterium tuberculosis: role of dectin-1, mannose receptor, and DC-SIGN. J Leukoc Biol 2009;86:1393–1401.
    • (2009) J Leukoc Biol , vol.86 , pp. 1393-1401
    • Zenaro, E.1    Donini, M.2    Dusi, S.3
  • 41
    • 84929461763 scopus 로고    scopus 로고
    • Human dendritic cell DC-SIGN and TLR-2 mediate complementary immune regulatory activities in response to Lactobacillus rhamnosus JB-1
    • Konieczna P, Schiavi E, Ziegler M, Groeger D, Healy S, Grant R et al. Human dendritic cell DC-SIGN and TLR-2 mediate complementary immune regulatory activities in response to Lactobacillus rhamnosus JB-1. PLoS One 2015;10:e0120261.
    • (2015) PLoS One , vol.10
    • Konieczna, P.1    Schiavi, E.2    Ziegler, M.3    Groeger, D.4    Healy, S.5    Grant, R.6


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