메뉴 건너뛰기




Volumn 5, Issue JUN, 2014, Pages

Microbe-host interactions are positively and negatively regulated by galectin-glycan interactions

Author keywords

Bacteria; Cell surface glycans; Galectin; Microbial pathogen; Virus

Indexed keywords


EID: 84905647104     PISSN: None     EISSN: 16643224     Source Type: Journal    
DOI: 10.3389/fimmu.2014.00284     Document Type: Review
Times cited : (62)

References (62)
  • 1
    • 84896725390 scopus 로고    scopus 로고
    • Cellular adhesion and the endothelium: E-selectin, L-selectin, and pan-selectin inhibitors
    • doi: 10.1016/j.hoc.2013.11.010
    • Telen MJ. Cellular adhesion and the endothelium: E-selectin, L-selectin, and pan-selectin inhibitors. Hematol Oncol Clin North Am (2014) 28:341-54. doi: 10.1016/j.hoc.2013.11.010
    • (2014) Hematol Oncol Clin North Am , vol.28 , pp. 341-354
    • Telen, M.J.1
  • 2
    • 84859416185 scopus 로고    scopus 로고
    • Multifarious roles of sialic acids in immunity
    • doi:10.1111/j.1749-6632.2012.06517.x
    • Varki A, Gagneux P. Multifarious roles of sialic acids in immunity. Ann N Y Acad Sci (2012) 1253:16-36. doi:10.1111/j.1749-6632.2012.06517.x
    • (2012) Ann N Y Acad Sci , vol.1253 , pp. 16-36
    • Varki, A.1    Gagneux, P.2
  • 3
    • 84860241831 scopus 로고    scopus 로고
    • Siglecs as sensors of self in innate and adaptive immune responses
    • doi:10.1111/j.1749-6632.2011.06362.x
    • Paulson JC, Macauley MS, Kawasaki N. Siglecs as sensors of self in innate and adaptive immune responses. Ann N Y Acad Sci (2012) 1253:37-48. doi:10.1111/j.1749-6632.2011.06362.x
    • (2012) Ann N Y Acad Sci , vol.1253 , pp. 37-48
    • Paulson, J.C.1    Macauley, M.S.2    Kawasaki, N.3
  • 4
    • 84866137250 scopus 로고    scopus 로고
    • Sialoadhesin in recognition of self and non-self
    • doi:10.1007/s00281-012-0310-3
    • Klaas M, Crocker PR. Sialoadhesin in recognition of self and non-self. Semin Immunopathol (2012) 34:353-64. doi:10.1007/s00281-012-0310-3
    • (2012) Semin Immunopathol , vol.34 , pp. 353-364
    • Klaas, M.1    Crocker, P.R.2
  • 5
    • 84880682970 scopus 로고    scopus 로고
    • Humoral pattern recognition and the complement system
    • doi:10.1111/sji.12070
    • Degn SE, Thiel S. Humoral pattern recognition and the complement system. Scand J Immunol (2013) 78:181-93. doi:10.1111/sji.12070
    • (2013) Scand J Immunol , vol.78 , pp. 181-193
    • Degn, S.E.1    Thiel, S.2
  • 6
    • 67649827438 scopus 로고    scopus 로고
    • Mannose-binding lectin and innate immunity
    • doi:10.1111/j.1600-065X.2009.00789.x
    • Ip WK, Takahashi K, Ezekowitz RA, Stuart LM. Mannose-binding lectin and innate immunity. Immunol Rev (2009) 230:9-21. doi:10.1111/j.1600-065X.2009.00789.x
    • (2009) Immunol Rev , vol.230 , pp. 9-21
    • Ip, W.K.1    Takahashi, K.2    Ezekowitz, R.A.3    Stuart, L.M.4
  • 7
    • 84860228172 scopus 로고    scopus 로고
    • An evolutionary perspective on C-type lectins in infection and immunity
    • doi:10.1111/j.1749-6632.2011.06392.x
    • van den Berg LM, Gringhuis SI, Geijtenbeek TB. An evolutionary perspective on C-type lectins in infection and immunity. Ann N Y Acad Sci (2012) 1253:149-58. doi:10.1111/j.1749-6632.2011.06392.x
    • (2012) Ann N Y Acad Sci , vol.1253 , pp. 149-158
    • van den Berg, L.M.1    Gringhuis, S.I.2    Geijtenbeek, T.B.3
  • 8
    • 67649823470 scopus 로고    scopus 로고
    • Beta-glucan recognition by the innate immune system
    • doi:10.1111/j.1600-065X.2009.00793.x
    • Goodridge HS, Wolf AJ, Underhill DM. Beta-glucan recognition by the innate immune system. Immunol Rev (2009) 230:38-50. doi:10.1111/j.1600-065X.2009.00793.x
    • (2009) Immunol Rev , vol.230 , pp. 38-50
    • Goodridge, H.S.1    Wolf, A.J.2    Underhill, D.M.3
  • 9
    • 84885967021 scopus 로고    scopus 로고
    • Sweeten PAMPs: role of sugar complexed PAMPs in innate immunity and vaccine biology
    • doi:10.3389/fimmu.2013.00248
    • Mahla RS, Reddy MC, Prasad DV, Kumar H. Sweeten PAMPs: role of sugar complexed PAMPs in innate immunity and vaccine biology. Front Immunol (2013) 4:248. doi:10.3389/fimmu.2013.00248
    • (2013) Front Immunol , vol.4 , pp. 248
    • Mahla, R.S.1    Reddy, M.C.2    Prasad, D.V.3    Kumar, H.4
  • 10
    • 80052735652 scopus 로고    scopus 로고
    • Coupling pathogen recognition to innate immunity through glycan-dependent mechanisms
    • doi:10.1016/j.intimp.2011.05.002
    • Davicino RC, Eliçabe RJ, Di Genaro MS, Rabinovich GA. Coupling pathogen recognition to innate immunity through glycan-dependent mechanisms. Int Immunopharmacol (2011) 11:1457-63. doi:10.1016/j.intimp.2011.05.002
    • (2011) Int Immunopharmacol , vol.11 , pp. 1457-1463
    • Davicino, R.C.1    Eliçabe, R.J.2    Di Genaro, M.S.3    Rabinovich, G.A.4
  • 11
    • 84884812281 scopus 로고    scopus 로고
    • The physiological role of DC-SIGN: a tale of mice and men
    • doi:10.1016/j.it.2013.03.001
    • Garcia-Vallejo JJ, van Kooyk Y. The physiological role of DC-SIGN: a tale of mice and men. Trends Immunol (2013) 34:482-6. doi:10.1016/j.it.2013.03.001
    • (2013) Trends Immunol , vol.34 , pp. 482-486
    • Garcia-Vallejo, J.J.1    van Kooyk, Y.2
  • 12
    • 84876799695 scopus 로고    scopus 로고
    • The dectin-2 family of C-type lectin-like receptors: an update
    • doi:10.1093/intimm/dxt006
    • Kerscher B, Willment JA, Brown GD. The dectin-2 family of C-type lectin-like receptors: an update. Int Immunol (2013) 25:271-7. doi:10.1093/intimm/dxt006
    • (2013) Int Immunol , vol.25 , pp. 271-277
    • Kerscher, B.1    Willment, J.A.2    Brown, G.D.3
  • 13
    • 84870430539 scopus 로고    scopus 로고
    • The mannose receptor
    • doi:10.1189/jlb.0512231
    • Martinez-Pomares L. The mannose receptor. J Leukoc Biol (2012) 92:1177-86. doi:10.1189/jlb.0512231
    • (2012) J Leukoc Biol , vol.92 , pp. 1177-1186
    • Martinez-Pomares, L.1
  • 14
    • 84891097021 scopus 로고    scopus 로고
    • Galectins as bacterial sensors in the host innate response
    • doi:10.1016/j.mib.2013.11.006
    • Chen HY, Weng IC, Hong MH, Liu FT. Galectins as bacterial sensors in the host innate response. Curr Opin Microbiol (2014) 17C:75-81. doi:10.1016/j.mib.2013.11.006
    • (2014) Curr Opin Microbiol , vol.17 C , pp. 75-81
    • Chen, H.Y.1    Weng, I.C.2    Hong, M.H.3    Liu, F.T.4
  • 15
    • 84874201705 scopus 로고    scopus 로고
    • Galectins as self/non-self recognition receptors in innate and adaptive immunity: an unresolved paradox
    • doi:10.3389/fimmu.2012.00199
    • Vasta GR, Ahmed H, Nita-Lazar M, Banerjee A, Pasek M, Shridhar S, et al. Galectins as self/non-self recognition receptors in innate and adaptive immunity: an unresolved paradox. Front Immunol (2012) 13:199. doi:10.3389/fimmu.2012.00199
    • (2012) Front Immunol , vol.13 , pp. 199
    • Vasta, G.R.1    Ahmed, H.2    Nita-Lazar, M.3    Banerjee, A.4    Pasek, M.5    Shridhar, S.6
  • 16
    • 77949890193 scopus 로고    scopus 로고
    • Lectins as pattern recognition molecules: the effects of epitope density in innate immunity
    • doi:10.1093/glycob/cwp186
    • Dam TK, Brewer CF. Lectins as pattern recognition molecules: the effects of epitope density in innate immunity. Glycobiology (2010) 20:270-9. doi:10.1093/glycob/cwp186
    • (2010) Glycobiology , vol.20 , pp. 270-279
    • Dam, T.K.1    Brewer, C.F.2
  • 17
    • 67649774331 scopus 로고    scopus 로고
    • Galectins in innate immunity: dual functions of host soluble beta-galactoside-binding lectins as damage-associated molecular patterns (DAMPs) and as receptors for pathogen-associated molecular patterns (PAMPs)
    • doi:10.1111/j.1600-065X.2009.00790.x
    • Sato S, St-Pierre C, Bhaumik P, Nieminen J. Galectins in innate immunity: dual functions of host soluble beta-galactoside-binding lectins as damage-associated molecular patterns (DAMPs) and as receptors for pathogen-associated molecular patterns (PAMPs). Immunol Rev (2009) 230:172-87. doi:10.1111/j.1600-065X.2009.00790.x
    • (2009) Immunol Rev , vol.230 , pp. 172-187
    • Sato, S.1    St-Pierre, C.2    Bhaumik, P.3    Nieminen, J.4
  • 18
    • 59149097542 scopus 로고    scopus 로고
    • Galectin-glycan lattices regulate cell-surface glycoprotein organization and signaling
    • doi:10.1042/BST0361472
    • Garner OB, Baum LG. Galectin-glycan lattices regulate cell-surface glycoprotein organization and signaling. Biochem Soc Trans (2008) 36:1472-7. doi:10.1042/BST0361472
    • (2008) Biochem Soc Trans , vol.36 , pp. 1472-1477
    • Garner, O.B.1    Baum, L.G.2
  • 19
    • 84867740441 scopus 로고    scopus 로고
    • Galectins and their ligands: negative regulators of anti-tumor immunity
    • doi:10.1007/s10719-012-9379-0
    • Cedeno-Laurent F, Dimitroff CJ. Galectins and their ligands: negative regulators of anti-tumor immunity. Glycoconj J (2012) 29:619-25. doi:10.1007/s10719-012-9379-0
    • (2012) Glycoconj J , vol.29 , pp. 619-625
    • Cedeno-Laurent, F.1    Dimitroff, C.J.2
  • 20
    • 84858766894 scopus 로고    scopus 로고
    • Regulatory circuits mediated by lectin-glycan interactions in autoimmunity and cancer
    • doi:10.1016/j.immuni.2012.03.004
    • Rabinovich GA, Croci DO. Regulatory circuits mediated by lectin-glycan interactions in autoimmunity and cancer. Immunity (2012) 36:322-35. doi:10.1016/j.immuni.2012.03.004
    • (2012) Immunity , vol.36 , pp. 322-335
    • Rabinovich, G.A.1    Croci, D.O.2
  • 21
    • 84860228899 scopus 로고    scopus 로고
    • Galectins in acute and chronic inflammation
    • doi:10.1111/j.1749-6632.2011.06386.x
    • Liu FT, Yang RY, Hsu DK. Galectins in acute and chronic inflammation. Ann N Y Acad Sci (2012) 1253:80-91. doi:10.1111/j.1749-6632.2011.06386.x
    • (2012) Ann N Y Acad Sci , vol.1253 , pp. 80-91
    • Liu, F.T.1    Yang, R.Y.2    Hsu, D.K.3
  • 22
    • 84860233524 scopus 로고    scopus 로고
    • Galectins, glycans and HIV infection
    • doi:10.1111/j.1749-6632.2012.06475.x
    • Sato S, Ouellet M, St-Pierre C, Tremblay MJ. Galectins, glycans and HIV infection. Ann N Y Acad Sci (2012) 1253:133-48. doi:10.1111/j.1749-6632.2012.06475.x
    • (2012) Ann N Y Acad Sci , vol.1253 , pp. 133-148
    • Sato, S.1    Ouellet, M.2    St-Pierre, C.3    Tremblay, M.J.4
  • 23
    • 80655125508 scopus 로고    scopus 로고
    • Host-soluble galectin-1 promotes HIV-1 replication through a direct interaction with glycans of viral gp120 and host CD4
    • doi:10.1128/JVI.05351-11
    • St-Pierre C, Manya H, Ouellet M, Clark GF, Endo T, Tremblay MJ, et al. Host-soluble galectin-1 promotes HIV-1 replication through a direct interaction with glycans of viral gp120 and host CD4. J Virol (2011) 85:11742-51. doi:10.1128/JVI.05351-11
    • (2011) J Virol , vol.85 , pp. 11742-11751
    • St-Pierre, C.1    Manya, H.2    Ouellet, M.3    Clark, G.F.4    Endo, T.5    Tremblay, M.J.6
  • 24
    • 77449124815 scopus 로고    scopus 로고
    • N- and O-glycans modulate galectin-1 binding, CD45 signaling, and T cell death
    • doi:10.1074/jbc.M109.066191
    • Earl LA, Bi S, Baum LG. N- and O-glycans modulate galectin-1 binding, CD45 signaling, and T cell death. J Biol Chem (2010) 285:2232-44. doi:10.1074/jbc.M109.066191
    • (2010) J Biol Chem , vol.285 , pp. 2232-2244
    • Earl, L.A.1    Bi, S.2    Baum, L.G.3
  • 25
    • 33749514807 scopus 로고    scopus 로고
    • Galectin-1 binds different CD43 glycoforms to cluster CD43 and regulate T cell death
    • doi:10.4049/jimmunol.177.8.5328
    • Hernandez JD, Nguyen JT, He J, Wang W, Ardman B, Green JM, et al. Galectin-1 binds different CD43 glycoforms to cluster CD43 and regulate T cell death. J Immunol (2006) 177:5328-36. doi:10.4049/jimmunol.177.8.5328
    • (2006) J Immunol , vol.177 , pp. 5328-5336
    • Hernandez, J.D.1    Nguyen, J.T.2    He, J.3    Wang, W.4    Ardman, B.5    Green, J.M.6
  • 26
    • 62649106103 scopus 로고    scopus 로고
    • HIV-1 and microvesicles from T cells share a common glycome, arguing for a common origin
    • doi:10.1038/nchembio.151
    • Krishnamoorthy L, Bess JW Jr., Preston AB, Nagashima K, Mahal LK. HIV-1 and microvesicles from T cells share a common glycome, arguing for a common origin. Nat Chem Biol (2009) 5:244-50. doi:10.1038/nchembio.151
    • (2009) Nat Chem Biol , vol.5 , pp. 244-250
    • Krishnamoorthy, L.1    Bess J.W, Jr.2    Preston, A.B.3    Nagashima, K.4    Mahal, L.K.5
  • 27
    • 79960601577 scopus 로고    scopus 로고
    • Galectin-9 binding to cell surface protein disulfide isomerase regulates the redox environment to enhance T-cell migration and HIV entry
    • doi:10.1073/pnas.1017954108
    • Bi S, Hong PW, Lee B, Baum LG. Galectin-9 binding to cell surface protein disulfide isomerase regulates the redox environment to enhance T-cell migration and HIV entry. Proc Natl Acad Sci U S A (2011) 108:10650-5. doi:10.1073/pnas.1017954108
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 10650-10655
    • Bi, S.1    Hong, P.W.2    Lee, B.3    Baum, L.G.4
  • 28
    • 58149396117 scopus 로고    scopus 로고
    • Induction of galectin-1 expression by HTLV-1 Tax and its impact on HTLV-1 infectivity
    • doi:10.1186/1742-4690-5-105
    • Gauthier S, Pelletier I, Ouellet M, Vargas A, Tremblay MJ, Sato S, et al. Induction of galectin-1 expression by HTLV-1 Tax and its impact on HTLV-1 infectivity. Retrovirology (2008) 5:105. doi:10.1186/1742-4690-5-105
    • (2008) Retrovirology , vol.5 , pp. 105
    • Gauthier, S.1    Pelletier, I.2    Ouellet, M.3    Vargas, A.4    Tremblay, M.J.5    Sato, S.6
  • 29
    • 73849137111 scopus 로고    scopus 로고
    • Biofilm-like extracellular viral assemblies mediate HTLV-1 cell-to-cell transmission at virological synapses
    • doi:10.1038/nm.2065
    • Pais-Correia AM, Sachse M, Guadagnini S, Robbiati V, Lasserre R, Gessain A, et al. Biofilm-like extracellular viral assemblies mediate HTLV-1 cell-to-cell transmission at virological synapses. Nat Med (2010) 16:83-9. doi:10.1038/nm.2065
    • (2010) Nat Med , vol.16 , pp. 83-89
    • Pais-Correia, A.M.1    Sachse, M.2    Guadagnini, S.3    Robbiati, V.4    Lasserre, R.5    Gessain, A.6
  • 30
    • 84877316106 scopus 로고    scopus 로고
    • Binding of transmembrane mucins to galectin-3 limits herpesvirus 1 infection of human corneal keratinocytes
    • doi:10.1128/JVI.00166-13
    • Woodward AM, Mauris J, Argüeso P. Binding of transmembrane mucins to galectin-3 limits herpesvirus 1 infection of human corneal keratinocytes. J Virol (2013) 87:5841-7. doi:10.1128/JVI.00166-13
    • (2013) J Virol , vol.87 , pp. 5841-5847
    • Woodward, A.M.1    Mauris, J.2    Argüeso, P.3
  • 31
    • 84867642939 scopus 로고    scopus 로고
    • Galectin-3 binds Neisseria meningitidis and increases interaction with phagocytic cells
    • doi:10.1111/j.1462-5822.2012.01838.x
    • Quattroni P, Li Y, Lucchesi D, Lucas S, Hood DW, Herrmann M, et al. Galectin-3 binds Neisseria meningitidis and increases interaction with phagocytic cells. Cell Microbiol (2012) 14:1657-75. doi:10.1111/j.1462-5822.2012.01838.x
    • (2012) Cell Microbiol , vol.14 , pp. 1657-1675
    • Quattroni, P.1    Li, Y.2    Lucchesi, D.3    Lucas, S.4    Hood, D.W.5    Herrmann, M.6
  • 32
    • 0030994616 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa lipopolysaccharide binds galectin-3 and other human corneal epithelial proteins
    • Gupta SK, Masinick S, Garrett M, Hazlett LD. Pseudomonas aeruginosa lipopolysaccharide binds galectin-3 and other human corneal epithelial proteins. Infect Immun (1997) 65:2747-53.
    • (1997) Infect Immun , vol.65 , pp. 2747-2753
    • Gupta, S.K.1    Masinick, S.2    Garrett, M.3    Hazlett, L.D.4
  • 33
    • 0037124095 scopus 로고    scopus 로고
    • Specific recognition and cleavage of galectin-3 by Leishmania major through species-specific polygalactose epitope
    • doi:10.1074/jbc.M201562200
    • Pelletier I, Sato S. Specific recognition and cleavage of galectin-3 by Leishmania major through species-specific polygalactose epitope. J Biol Chem (2002) 277:17663-70. doi:10.1074/jbc.M201562200
    • (2002) J Biol Chem , vol.277 , pp. 17663-17670
    • Pelletier, I.1    Sato, S.2
  • 34
    • 0038605468 scopus 로고    scopus 로고
    • Specific recognition of Leishmania major poly-beta-galactosyl epitopes by galectin-9: possible implication of galectin-9 in interaction between L. major and host cells
    • doi:10.1074/jbc.M302693200
    • Pelletier I, Hashidate T, Urashima T, Nishi N, Nakamura T, Futai M, et al. Specific recognition of Leishmania major poly-beta-galactosyl epitopes by galectin-9: possible implication of galectin-9 in interaction between L. major and host cells. J Biol Chem (2003) 278:22223-30. doi:10.1074/jbc.M302693200
    • (2003) J Biol Chem , vol.278 , pp. 22223-22230
    • Pelletier, I.1    Hashidate, T.2    Urashima, T.3    Nishi, N.4    Nakamura, T.5    Futai, M.6
  • 35
    • 7044247771 scopus 로고    scopus 로고
    • A role for insect galectins in parasite survival
    • doi:10.1016/j.cell.2004.10.009
    • Kamhawi S, Ramalho-Ortigao M, Pham VM, Kumar S, Lawyer PG, Turco SJ, et al. A role for insect galectins in parasite survival. Cell (2004) 119:329-41. doi:10.1016/j.cell.2004.10.009
    • (2004) Cell , vol.119 , pp. 329-341
    • Kamhawi, S.1    Ramalho-Ortigao, M.2    Pham, V.M.3    Kumar, S.4    Lawyer, P.G.5    Turco, S.J.6
  • 36
    • 7044228232 scopus 로고    scopus 로고
    • Human galectin-3 promotes Trypanosoma cruzi adhesion to human coronary artery smooth muscle cells
    • doi:10.1128/IAI.72.11.6717-6721.2004
    • Kleshchenko YY, Moody TN, Furtak VA, Ochieng J, Lima MF, Villalta F. Human galectin-3 promotes Trypanosoma cruzi adhesion to human coronary artery smooth muscle cells. Infect Immun (2004) 72:6717-21. doi:10.1128/IAI.72.11.6717-6721.2004
    • (2004) Infect Immun , vol.72 , pp. 6717-6721
    • Kleshchenko, Y.Y.1    Moody, T.N.2    Furtak, V.A.3    Ochieng, J.4    Lima, M.F.5    Villalta, F.6
  • 37
    • 84874204727 scopus 로고    scopus 로고
    • Regulation and use of the extracellular matrix by Trypanosoma cruzi during early infection
    • doi:10.3389/fimmu.2012.00337
    • Nde PN, Lima MF, Johnson CA, Pratap S, Villalta F. Regulation and use of the extracellular matrix by Trypanosoma cruzi during early infection. Front Immunol (2012) 3:337. doi:10.3389/fimmu.2012.00337
    • (2012) Front Immunol , vol.3 , pp. 337
    • Nde, P.N.1    Lima, M.F.2    Johnson, C.A.3    Pratap, S.4    Villalta, F.5
  • 38
    • 67349272266 scopus 로고    scopus 로고
    • Perspectives on the Trypanosoma cruzi-host cell receptor interactions
    • doi:10.1007/s00436-009-1383-3
    • Villalta F, Scharfstein J, Ashton AW, Tyler KM, Guan F, Mukherjee S, et al. Perspectives on the Trypanosoma cruzi-host cell receptor interactions. Parasitol Res (2009) 104:1251-60. doi:10.1007/s00436-009-1383-3
    • (2009) Parasitol Res , vol.104 , pp. 1251-1260
    • Villalta, F.1    Scharfstein, J.2    Ashton, A.W.3    Tyler, K.M.4    Guan, F.5    Mukherjee, S.6
  • 39
    • 51449101867 scopus 로고    scopus 로고
    • Galectin-1 on cervical epithelial cells is a receptor for the sexually transmitted human parasite Trichomonas vaginalis
    • doi:10.1111/j.1462-5822.2008.01190.x
    • Okumura CY, Baum LG, Johnson PJ. Galectin-1 on cervical epithelial cells is a receptor for the sexually transmitted human parasite Trichomonas vaginalis. Cell Microbiol (2008) 10:2078-90. doi:10.1111/j.1462-5822.2008.01190.x
    • (2008) Cell Microbiol , vol.10 , pp. 2078-2090
    • Okumura, C.Y.1    Baum, L.G.2    Johnson, P.J.3
  • 40
    • 21244502470 scopus 로고    scopus 로고
    • Novel innate immune functions for galectin-1: galectin-1 inhibits cell fusion by Nipah virus envelope glycoproteins and augments dendritic cell secretion of proinflammatory cytokines
    • doi:10.4049/jimmunol.175.1.413
    • Levroney EL, Aguilar HC, Fulcher JA, Kohatsu L, Pace KE, Pang M, et al. Novel innate immune functions for galectin-1: galectin-1 inhibits cell fusion by Nipah virus envelope glycoproteins and augments dendritic cell secretion of proinflammatory cytokines. J Immunol (2005) 175:413-20. doi:10.4049/jimmunol.175.1.413
    • (2005) J Immunol , vol.175 , pp. 413-420
    • Levroney, E.L.1    Aguilar, H.C.2    Fulcher, J.A.3    Kohatsu, L.4    Pace, K.E.5    Pang, M.6
  • 41
    • 22944445501 scopus 로고    scopus 로고
    • EphrinB2 is the entry receptor for Nipah virus, an emergent deadly paramyxovirus
    • doi:10.1038/nature0383
    • Negrete OA, Levroney EL, Aguilar HC, Bertolotti-Ciarlet A, Nazarian R, Tajyar S, et al. EphrinB2 is the entry receptor for Nipah virus, an emergent deadly paramyxovirus. Nature (2005) 436:401-5. doi:10.1038/nature0383
    • (2005) Nature , vol.436 , pp. 401-405
    • Negrete, O.A.1    Levroney, E.L.2    Aguilar, H.C.3    Bertolotti-Ciarlet, A.4    Nazarian, R.5    Tajyar, S.6
  • 42
    • 77957675527 scopus 로고    scopus 로고
    • Endothelial galectin-1 binds to specific glycans on Nipah virus fusion protein and inhibits maturation, mobility, and function to block syncytia formation
    • doi:10.1371/journal.ppat.1000993
    • Garner OB, Aguilar HC, Fulcher JA, Levroney EL, Harrison R, Wright L, et al. Endothelial galectin-1 binds to specific glycans on Nipah virus fusion protein and inhibits maturation, mobility, and function to block syncytia formation. PLoS Pathog (2010) 6:e1000993. doi:10.1371/journal.ppat.1000993
    • (2010) PLoS Pathog , vol.6
    • Garner, O.B.1    Aguilar, H.C.2    Fulcher, J.A.3    Levroney, E.L.4    Harrison, R.5    Wright, L.6
  • 43
    • 80054002504 scopus 로고    scopus 로고
    • Galectin-1 binds to influenza virus and ameliorates influenza virus pathogenesis
    • doi:10.1128/JVI.00301-11
    • Yang ML, Chen YH, Wang SW, Huang YJ, Leu CH, Yeh NC, et al. Galectin-1 binds to influenza virus and ameliorates influenza virus pathogenesis. J Virol (2011) 85:10010-20. doi:10.1128/JVI.00301-11
    • (2011) J Virol , vol.85 , pp. 10010-10020
    • Yang, M.L.1    Chen, Y.H.2    Wang, S.W.3    Huang, Y.J.4    Leu, C.H.5    Yeh, N.C.6
  • 44
    • 69249122444 scopus 로고    scopus 로고
    • Association of cell surface mucins with galectin-3 contributes to the ocular surface epithelial barrier
    • doi:10.1074/jbc.M109.033332
    • Argüeso P, Guzman-Aranguez A, Mantelli F, Cao Z, Ricciuto J, Panjwani N. Association of cell surface mucins with galectin-3 contributes to the ocular surface epithelial barrier. J Biol Chem (2009) 284:23037-45. doi:10.1074/jbc.M109.033332
    • (2009) J Biol Chem , vol.284 , pp. 23037-23045
    • Argüeso, P.1    Guzman-Aranguez, A.2    Mantelli, F.3    Cao, Z.4    Ricciuto, J.5    Panjwani, N.6
  • 45
    • 77958515323 scopus 로고    scopus 로고
    • Binding of Toxoplasma gondii glycosylphosphatidylinositols to galectin-3 is required for their recognition by macrophages
    • doi:10.1074/jbc.M110.137588
    • Debierre-Grockiego F, Niehus S, Coddeville B, Elass E, Poirier F, Weingart R, et al. Binding of Toxoplasma gondii glycosylphosphatidylinositols to galectin-3 is required for their recognition by macrophages. J Biol Chem (2010) 285:32744-50. doi:10.1074/jbc.M110.137588
    • (2010) J Biol Chem , vol.285 , pp. 32744-32750
    • Debierre-Grockiego, F.1    Niehus, S.2    Coddeville, B.3    Elass, E.4    Poirier, F.5    Weingart, R.6
  • 46
    • 33645311204 scopus 로고    scopus 로고
    • Lipid raft organization and function in brush borders of epithelial cells
    • doi:10.1080/09687860500445604
    • Danielsen EM, Hansen GH. Lipid raft organization and function in brush borders of epithelial cells. Mol Membr Biol (2006) 23:71-9. doi:10.1080/09687860500445604
    • (2006) Mol Membr Biol , vol.23 , pp. 71-79
    • Danielsen, E.M.1    Hansen, G.H.2
  • 47
    • 14244257721 scopus 로고    scopus 로고
    • Galectin-4 binds to sulfated glycosphingolipids and carcinoembryonic antigen in patches on the cell surface of human colon adenocarcinoma cells
    • doi:10.1074/jbc.M410362200
    • Ideo H, Seko A, Yamashita K. Galectin-4 binds to sulfated glycosphingolipids and carcinoembryonic antigen in patches on the cell surface of human colon adenocarcinoma cells. J Biol Chem (2005) 280:4730-7. doi:10.1074/jbc.M410362200
    • (2005) J Biol Chem , vol.280 , pp. 4730-4737
    • Ideo, H.1    Seko, A.2    Yamashita, K.3
  • 48
    • 70350400858 scopus 로고    scopus 로고
    • A Caenorhabditis elegans glycolipid-binding galectin functions in host defense against bacterial infection
    • doi:10.1074/jbc.M109.038257
    • Ideo H, Fukushima K, Gengyo-Ando K, Mitani S, Dejima K, Nomura K, et al. A Caenorhabditis elegans glycolipid-binding galectin functions in host defense against bacterial infection. J Biol Chem (2009) 284:26493-501. doi:10.1074/jbc.M109.038257
    • (2009) J Biol Chem , vol.284 , pp. 26493-26501
    • Ideo, H.1    Fukushima, K.2    Gengyo-Ando, K.3    Mitani, S.4    Dejima, K.5    Nomura, K.6
  • 49
    • 0036207005 scopus 로고    scopus 로고
    • Association of a macrophage galactoside-binding protein with Mycobacterium-containing phagosomes
    • doi:10.1046/j.1462-5822.2002.00183.x
    • Beatty WL, Rhoades ER, Hsu DK, Liu FT, Russell DG. Association of a macrophage galactoside-binding protein with Mycobacterium-containing phagosomes. Cell Microbiol (2002) 4:167-76. doi:10.1046/j.1462-5822.2002.00183.x
    • (2002) Cell Microbiol , vol.4 , pp. 167-176
    • Beatty, W.L.1    Rhoades, E.R.2    Hsu, D.K.3    Liu, F.T.4    Russell, D.G.5
  • 50
    • 84857071710 scopus 로고    scopus 로고
    • Galectin 8 targets damaged vesicles for autophagy to defend cells against bacterial invasion
    • doi:10.1038/nature10744
    • Thurston TL, Wandel MP, von Muhlinen N, Foeglein A, Randow F. Galectin 8 targets damaged vesicles for autophagy to defend cells against bacterial invasion. Nature (2012) 482:414-8. doi:10.1038/nature10744
    • (2012) Nature , vol.482 , pp. 414-418
    • Thurston, T.L.1    Wandel, M.P.2    von Muhlinen, N.3    Foeglein, A.4    Randow, F.5
  • 51
    • 3242781553 scopus 로고    scopus 로고
    • LacdiNAc-glycans constitute a parasite pattern for galectin-3-mediated immune recognition
    • doi:10.4049/jimmunol.173.3.1902
    • van den Berg TK, Honing H, Franke N, van Remoortere A, Schiphorst WE, Liu FT, et al. LacdiNAc-glycans constitute a parasite pattern for galectin-3-mediated immune recognition. J Immunol (2004) 173:1902-7. doi:10.4049/jimmunol.173.3.1902
    • (2004) J Immunol , vol.173 , pp. 1902-1907
    • van den Berg, T.K.1    Honing, H.2    Franke, N.3    van Remoortere, A.4    Schiphorst, W.E.5    Liu, F.T.6
  • 52
    • 84879205874 scopus 로고    scopus 로고
    • The role of galectin-3 in phagocytosis of Candida albicans and Candida parapsilosis by human neutrophils
    • doi:10.1111/cmi.12103
    • Linden JR, Kunkel D, Laforce-Nesbitt SS, Bliss JM. The role of galectin-3 in phagocytosis of Candida albicans and Candida parapsilosis by human neutrophils. Cell Microbiol (2013) 15:1127-42. doi:10.1111/cmi.12103
    • (2013) Cell Microbiol , vol.15 , pp. 1127-1142
    • Linden, J.R.1    Kunkel, D.2    Laforce-Nesbitt, S.S.3    Bliss, J.M.4
  • 53
    • 80052149749 scopus 로고    scopus 로고
    • Fungal recognition is mediated by the association of dectin-1 and galectin-3 in macrophages
    • doi:10.1073/pnas.1111415108
    • Esteban A, Popp MW, Vyas VK, Strijbis K, Ploegh HL, Fink GR. Fungal recognition is mediated by the association of dectin-1 and galectin-3 in macrophages. Proc Natl Acad Sci U S A (2011) 108:14270-5. doi:10.1073/pnas.1111415108
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 14270-14275
    • Esteban, A.1    Popp, M.W.2    Vyas, V.K.3    Strijbis, K.4    Ploegh, H.L.5    Fink, G.R.6
  • 54
    • 33749143645 scopus 로고    scopus 로고
    • Specific recognition of Candida albicans by macrophages requires galectin-3 to discriminate Saccharomyces cerevisiae and needs association with TLR2 for signaling
    • doi:10.4049/jimmunol.177.7.4679
    • Jouault T, El Abed-El Behi M, Martínez-Esparza M, Breuilh L, Trinel PA, Chamaillard M, et al. Specific recognition of Candida albicans by macrophages requires galectin-3 to discriminate Saccharomyces cerevisiae and needs association with TLR2 for signaling. J Immunol (2006) 177:4679-87. doi:10.4049/jimmunol.177.7.4679
    • (2006) J Immunol , vol.177 , pp. 4679-4687
    • Jouault, T.1    El Abed-El Behi, M.2    Martínez-Esparza, M.3    Breuilh, L.4    Trinel, P.A.5    Chamaillard, M.6
  • 55
    • 33749125248 scopus 로고    scopus 로고
    • Galectin-3 induces death of Candida species expressing specific beta-1,2-linked mannans
    • doi:10.4049/jimmunol.177.7.4718
    • Kohatsu L, Hsu DK, Jegalian AG, Liu FT, Baum LG. Galectin-3 induces death of Candida species expressing specific beta-1,2-linked mannans. J Immunol (2006) 177:4718-26. doi:10.4049/jimmunol.177.7.4718
    • (2006) J Immunol , vol.177 , pp. 4718-4726
    • Kohatsu, L.1    Hsu, D.K.2    Jegalian, A.G.3    Liu, F.T.4    Baum, L.G.5
  • 57
    • 84866768171 scopus 로고    scopus 로고
    • Galectins in the abdominal cavity of the conger eel Conger myriaster participate in the cellular encapsulation of parasitic nematodes by host cells
    • doi:10.1016/j.fsi.2012.07.003
    • Nakamura O, Watanabe M, Ogawa T, Muramoto K, Ogawa K, Tsutsui S, et al. Galectins in the abdominal cavity of the conger eel Conger myriaster participate in the cellular encapsulation of parasitic nematodes by host cells. Fish Shellfish Immunol (2012) 33:780-7. doi:10.1016/j.fsi.2012.07.003
    • (2012) Fish Shellfish Immunol , vol.33 , pp. 780-787
    • Nakamura, O.1    Watanabe, M.2    Ogawa, T.3    Muramoto, K.4    Ogawa, K.5    Tsutsui, S.6
  • 58
    • 84876004025 scopus 로고    scopus 로고
    • Density-dependent lectin-glycan interactions as a paradigm for conditional regulation by posttranslational modifications
    • doi:10.1074/mcp.R112.026989
    • Dennis JW, Brewer CF. Density-dependent lectin-glycan interactions as a paradigm for conditional regulation by posttranslational modifications. Mol Cell Proteomics (2013) 12:913-20. doi:10.1074/mcp.R112.026989
    • (2013) Mol Cell Proteomics , vol.12 , pp. 913-920
    • Dennis, J.W.1    Brewer, C.F.2
  • 59
    • 84874895754 scopus 로고    scopus 로고
    • Glycan evolution in response to collaboration, conflict, and constraint
    • doi:10.1074/jbc.R112.424523
    • Springer SA, Gagneux P. Glycan evolution in response to collaboration, conflict, and constraint. J Biol Chem (2013) 288:6904-11. doi:10.1074/jbc.R112.424523
    • (2013) J Biol Chem , vol.288 , pp. 6904-6911
    • Springer, S.A.1    Gagneux, P.2
  • 60
    • 8444249576 scopus 로고    scopus 로고
    • The acquired immune system: a vantage from beneath
    • doi:10.1016/j.immuni.2004.08.020
    • Hedrick SM. The acquired immune system: a vantage from beneath. Immunity (2004) 21:607-715. doi:10.1016/j.immuni.2004.08.020
    • (2004) Immunity , vol.21 , pp. 607-715
    • Hedrick, S.M.1
  • 61
    • 80555149784 scopus 로고    scopus 로고
    • Galectins as pattern recognition receptors: structure, function and evolution
    • doi:10.1007/978-1-4614-0106-3_2
    • Vasta GR. Galectins as pattern recognition receptors: structure, function and evolution. Adv Exp Med Biol (2012) 946:21-36. doi:10.1007/978-1-4614-0106-3_2
    • (2012) Adv Exp Med Biol , vol.946 , pp. 21-36
    • Vasta, G.R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.