High molecular weight components containing N-linked oligosaccharides of Ascaris suum extract inhibit the dendritic cells activation through DC-SIGN and MR
Carregando...
Citações na Scopus
14
Tipo de produção
article
Data de publicação
2017
Título da Revista
ISSN da Revista
Título do Volume
Editora
PERGAMON-ELSEVIER SCIENCE LTD
Autores
FAVORETTO, Bruna C.
CASABUONO, Adriana A. C.
PORTES-JUNIOR, Jose A.
COUTO, Alicia S.
FAQUIM-MAURO, Eliana L.
Citação
MOLECULAR IMMUNOLOGY, v.87, p.33-46, 2017
Resumo
Helminths, as well as their secretory/excretory products, induce a tolerogenic immune microenvironment. High molecular weight components (PI) from Ascaris suum extract down-modulate the immune response against ovalbumin (OVA). The PI exerts direct effect on dendritic cells (DCs) independent of TLR 2, 4 and MyD88 molecule and, thus, decreases the T lymphocytes response. Here, we studied the glycoconjugates in PI and the role of C-type lectin receptors (CLRs), DC-SIGN and MR, in the modulation of DCs activity. Our data showed the presence of glycoconjugates with high mannose- and complex-type N-linked oligosaccharide chains and phosphorylcholine residues on PI. In addition, these N-linked glycoconjugates inhibited the DCs maturation induced by LPS. The binding and internalization of PI-Alexa were decreased on DCs previously incubated with mannan, anti-DC-SIGN and/or anti-MR antibodies. In agreement with this, the incubation of DCs with mannan, anti-DC-SIGN and/or anti-MR antibodies abolished the down-modulatory effect of PI on these cells. It was also observed that the blockage of CLRs, DC-SIGN and MR on DCs reverted the inhibitory effect of PI in in vitro T cells proliferation. Therefore, our data show the involvement of DC-SIGN and MR in the recognition and consequent modulatory effect of N-glycosylated components of PI on DCs.
Palavras-chave
Ascaris suum, C-type lectin receptors, PI - High molecular weight components, from Ascaris suum extract, DC-Dendritic Cell, DCSIGN-Dendritic cell specifc ICAM-3, grabbing non-integrin, MR-Mannose receptor
Referências
- ALVES MJM, 1986, MOL BIOCHEM PARASIT, V21, P75
- Baldo C., 2010, PLOS NEGLECT TROP D, V6, pe727
- Brattig NW, 2004, J IMMUNOL, V173, P437
- Burgdorf S, 2007, SCIENCE, V316, P612, DOI 10.1126/science.1137971
- Chieppa M, 2003, J IMMUNOL, V171, P4552
- den Dunnen J, 2009, CANCER IMMUNOL IMMUN, V58, P1149, DOI 10.1007/s00262-008-0615-1
- Du LL, 2014, BIOMED RES INT, DOI 10.1155/2014/898646
- Duschak VG, 2009, CURR MED CHEM, V16, P3174
- Engering A, 2002, BLOOD, V100, P1780, DOI 10.1182/blood-2001-12-0179
- Erdmann H, 2009, CELL MICROBIOL, V11, P1600, DOI 10.1111/j.1462-5822.2009.01350.x
- Everts B, 2012, J EXP MED, V209, P1753, DOI 10.1084/jem.20111381
- Faquim-Mauro EL, 1998, CLIN EXP IMMUNOL, V114, P245
- Favoretto B.C., 2010, THESIS
- Favoretto BC, 2014, MOL IMMUNOL, V58, P17, DOI 10.1016/j.molimm.2013.10.011
- FERREIRA AP, 1995, CELL IMMUNOL, V162, P202, DOI 10.1006/cimm.1995.1070
- Finkelman F. D., 1991, IMMUNOL TODAY, V12, P62
- Gause WC, 1999, IMMUNOL RES, V20, P55, DOI 10.1007/BF02786507
- Geijtenbeek TBH, 2004, ANNU REV IMMUNOL, V22, P33, DOI 10.1146/annurev.immunol.22.012703.104558
- Geijtenbeek TBH, 2003, J EXP MED, V197, P7, DOI 10.1084/jem.20021229
- Geijtenbeek TBH, 2000, CELL, V100, P587, DOI 10.1016/S0092-8674(00)80694-7
- Geijtenbeek TBH, 2009, NAT REV IMMUNOL, V9, P465, DOI 10.1038/nri2569
- Gringhuis SI, 2007, IMMUNITY, V26, P605, DOI 10.1016/j.immuni.2007.03.012
- HAIG DM, 1980, PARASITE IMMUNOL, V2, P175, DOI 10.1111/j.1365-3024.1980.tb00052.x
- Halary F, 2002, IMMUNITY, V17, P653, DOI 10.1016/S1074-7613(02)00447-8
- Hamilton CM, 2009, INFECT IMMUN, V77, P2488, DOI 10.1128/IAI.00919-08
- Harnett W, 2010, TRENDS PARASITOL, V26, P114, DOI 10.1016/j.pt.2009.12.003
- Hubo M., 2013, FRONT IMMUNOL, V82, P1
- Jang-Lee J, 2007, MOL CELL PROTEOMICS, V6, P1485, DOI 10.1074/mcp.M700004-MCP200
- Klaver EJ, 2013, INT J PARASITOL, V43, P191, DOI 10.1016/j.ijpara.2012.10.021
- Maizels RM, 2003, NAT REV IMMUNOL, V3, P733, DOI 10.1038/nri1183
- McGuirk P, 2002, J EXP MED, V195, P221, DOI 10.1084/jem.20011288
- Moll H, 2003, CELL MICROBIOL, V5, P493, DOI 10.1046/j.1462-5822.2003.00291.x
- Morelle W, 2000, GLYCOBIOLOGY, V10, P941, DOI 10.1093/glycob/10.9.941
- Mosmann TR, 1996, IMMUNOL TODAY, V17, P138, DOI 10.1016/0167-5699(96)80606-2
- Nyame AK, 1998, GLYCOBIOLOGY, V8, P615, DOI 10.1093/glycob/8.6.615
- PIRAS MM, 1987, MOL BIOCHEM PARASIT, V22, P135, DOI 10.1016/0166-6851(87)90043-0
- Poltl G, 2007, FEBS J, V274, P714, DOI 10.1111/j.1742-4658.2006.05615.x
- SALLUSTO F, 1995, J EXP MED, V182, P389, DOI 10.1084/jem.182.2.389
- Schnare M, 2001, NAT IMMUNOL, V2, P947, DOI 10.1038/ni712
- Silva SR, 2006, EUR J IMMUNOL, V36, P3227, DOI 10.1002/eji.200636110
- SOARES MFM, 1992, INT ARCH ALLERGY IMM, V97, P37
- Son YI, 2002, J IMMUNOL METHODS, V262, P145, DOI 10.1016/S0022-1759(02)00013-3
- Sorvillo N, 2012, BLOOD, V119, P3828, DOI 10.1182/blood-2011-09-377754
- Svajger U, 2010, CELL SIGNAL, V22, P1397, DOI 10.1016/j.cellsig.2010.03.018
- Takeda K, 2003, ANNU REV IMMUNOL, V21, P335, DOI 10.1146/annurev.immunol.21.120601.141126
- Terrazas CA, 2013, FASEB J, V27, P4547, DOI 10.1096/fj.13-228932
- Terrazas CA, 2011, INT J BIOL SCI, V7, P1391
- Van der Kleij D, 2002, J INFECT DIS, V185, P531, DOI 10.1086/338574
- van Die I, 2006, CHEM IMMUNOL ALLERGY, V90, P91
- van Die I, 2010, METHOD ENZYMOL, V480, P117, DOI 10.1016/S0076-6879(10)80006-0
- van Kooyk Y, 2003, NAT REV IMMUNOL, V3, P697, DOI 10.1038/nri1182
- van Liempt E, 2007, MOL IMMUNOL, V44, P2605, DOI 10.1016/j.molimm.2006.12.012
- Varki A, 1997, FASEB J, V11, P248
- Varki A., 2009, ESSENTIALS GLYCOBIOL