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Volumn 95, Issue 1, 2013, Pages 33-42

Bacterial cell wall macroamphiphiles: Pathogen-/microbe-associated molecular patterns detected by mammalian innate immune system

Author keywords

Bacterial lipids; Innate immunity; Toll like receptors

Indexed keywords

AMPHOPHILE; BACTERIUM LIPOPOLYSACCHARIDE; CD14 ANTIGEN; CD36 ANTIGEN; CYSTEINE; DIACYLGLYCEROL; LIPID A; LIPOPHOSPHOGLYCAN; LIPOPOLYSACCHARIDE BINDING PROTEIN; LIPOPROTEIN; LIPOTEICHOIC ACID; MANNOSIDE; PATTERN RECOGNITION RECEPTOR; PROTEIN MD 2; TOLL LIKE RECEPTOR 1; TOLL LIKE RECEPTOR 2; TOLL LIKE RECEPTOR 4; TOLL LIKE RECEPTOR 6;

EID: 84870526465     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2012.06.007     Document Type: Review
Times cited : (78)

References (117)
  • 1
    • 35349016235 scopus 로고    scopus 로고
    • Recognition of microorganisms and activation of the immune response
    • R. Medzhitov Recognition of microorganisms and activation of the immune response Nature 449 2007 819 826
    • (2007) Nature , vol.449 , pp. 819-826
    • Medzhitov, R.1
  • 2
    • 74549167783 scopus 로고    scopus 로고
    • Regulation of adaptive immunity by the innate immune system
    • A. Iwasaki, and R. Medzhitov Regulation of adaptive immunity by the innate immune system Science 327 2010 291 295
    • (2010) Science , vol.327 , pp. 291-295
    • Iwasaki, A.1    Medzhitov, R.2
  • 3
    • 32944464648 scopus 로고    scopus 로고
    • Pathogen recognition and innate immunity
    • S. Akira, S. Uematsu, and O. Takeuchi Pathogen recognition and innate immunity Cell 124 2006 783 801
    • (2006) Cell , vol.124 , pp. 783-801
    • Akira, S.1    Uematsu, S.2    Takeuchi, O.3
  • 5
    • 79951897946 scopus 로고    scopus 로고
    • Innate immunity to intracellular pathogens: Macrophage receptors and responses to microbial entry
    • A. Pluddemann, S. Mukhopadhyay, and S. Gordon Innate immunity to intracellular pathogens: macrophage receptors and responses to microbial entry Immunol. Rev. 240 2011 11 24
    • (2011) Immunol. Rev. , vol.240 , pp. 11-24
    • Pluddemann, A.1    Mukhopadhyay, S.2    Gordon, S.3
  • 6
    • 66249119393 scopus 로고    scopus 로고
    • Lipoteichoic acid biosynthesis: Two steps forwards, one step sideways?
    • O. Rahman, L.G. Dover, and I.C. Sutcliffe Lipoteichoic acid biosynthesis: two steps forwards, one step sideways? Trends Microbiol. 17 2009 219 225
    • (2009) Trends Microbiol. , vol.17 , pp. 219-225
    • Rahman, O.1    Dover, L.G.2    Sutcliffe, I.C.3
  • 7
    • 0001575327 scopus 로고
    • Lipoteichoic acids and lipoglycans
    • J.-M. Ghuysen, R. Hakenbeck, Elsevier Science B.V. Amsterdam, The Netherlands
    • W. Fischer Lipoteichoic acids and lipoglycans J.-M. Ghuysen, R. Hakenbeck, Bacterial Cell Wall 1994 Elsevier Science B.V. Amsterdam, The Netherlands 199 215
    • (1994) Bacterial Cell Wall , pp. 199-215
    • Fischer, W.1
  • 8
    • 48749128643 scopus 로고    scopus 로고
    • Structures of the toll-like receptor family and its ligand complexes
    • M.S. Jin, and J.O. Lee Structures of the toll-like receptor family and its ligand complexes Immunity 29 2008 182 191
    • (2008) Immunity , vol.29 , pp. 182-191
    • Jin, M.S.1    Lee, J.O.2
  • 9
    • 79959447465 scopus 로고    scopus 로고
    • Structural biology of the Toll-like receptor family
    • J.Y. Kang, and J.O. Lee Structural biology of the Toll-like receptor family Annu. Rev. Biochem. 80 2011 917 941
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 917-941
    • Kang, J.Y.1    Lee, J.O.2
  • 12
    • 67349182481 scopus 로고    scopus 로고
    • The structural basis of lipopolysaccharide recognition by the TLR4-MD-2 complex
    • B.S. Park, D.H. Song, H.M. Kim, B.S. Choi, H. Lee, and J.O. Lee The structural basis of lipopolysaccharide recognition by the TLR4-MD-2 complex Nature 458 2009 1191 1195
    • (2009) Nature , vol.458 , pp. 1191-1195
    • Park, B.S.1    Song, D.H.2    Kim, H.M.3    Choi, B.S.4    Lee, H.5    Lee, J.O.6
  • 13
    • 35348856289 scopus 로고    scopus 로고
    • Regulation of interactions of Gram-negative bacterial endotoxins with mammalian cells
    • T.L. Gioannini, and J.P. Weiss Regulation of interactions of Gram-negative bacterial endotoxins with mammalian cells Immunol. Res. 39 2007 249 260
    • (2007) Immunol. Res. , vol.39 , pp. 249-260
    • Gioannini, T.L.1    Weiss, J.P.2
  • 14
    • 15744396047 scopus 로고    scopus 로고
    • Crystal structure of CD14 and its implications for lipopolysaccharide signaling
    • J.I. Kim, C.J. Lee, M.S. Jin, C.H. Lee, S.G. Paik, H. Lee, and J.O. Lee Crystal structure of CD14 and its implications for lipopolysaccharide signaling J. Biol. Chem. 280 2005 11347 11351
    • (2005) J. Biol. Chem. , vol.280 , pp. 11347-11351
    • Kim, J.I.1    Lee, C.J.2    Jin, M.S.3    Lee, C.H.4    Paik, S.G.5    Lee, H.6    Lee, J.O.7
  • 16
    • 25444528950 scopus 로고    scopus 로고
    • MD-2 mediates the ability of tetra-acylated and penta-acylated lipopolysaccharides to antagonize Escherichia coli lipopolysaccharide at the TLR4 signaling complex
    • S.R. Coats, T.T. Pham, B.W. Bainbridge, R.A. Reife, and R.P. Darveau MD-2 mediates the ability of tetra-acylated and penta-acylated lipopolysaccharides to antagonize Escherichia coli lipopolysaccharide at the TLR4 signaling complex J. Immunol. 175 2005 4490 4498
    • (2005) J. Immunol. , vol.175 , pp. 4490-4498
    • Coats, S.R.1    Pham, T.T.2    Bainbridge, B.W.3    Reife, R.A.4    Darveau, R.P.5
  • 18
    • 84862901721 scopus 로고    scopus 로고
    • A phylum level analysis reveals lipoprotein biosynthesis to be a fundamental property of bacteria
    • I.C. Sutcliffe, D.J. Harrington, and M.I. Hutchings A phylum level analysis reveals lipoprotein biosynthesis to be a fundamental property of bacteria Protein Cell 3 2012 163 170
    • (2012) Protein Cell , vol.3 , pp. 163-170
    • Sutcliffe, I.C.1    Harrington, D.J.2    Hutchings, M.I.3
  • 19
    • 0345671672 scopus 로고    scopus 로고
    • Isolation, structure elucidation, and synthesis of a macrophage stimulatory lipopeptide from Mycoplasma fermentans acting at picomolar concentration
    • P.F. Muhlradt, M. Kiess, H. Meyer, R. Sussmuth, and G. Jung Isolation, structure elucidation, and synthesis of a macrophage stimulatory lipopeptide from Mycoplasma fermentans acting at picomolar concentration J. Exp. Med. 185 1997 1951 1958
    • (1997) J. Exp. Med. , vol.185 , pp. 1951-1958
    • Muhlradt, P.F.1    Kiess, M.2    Meyer, H.3    Sussmuth, R.4    Jung, G.5
  • 20
    • 0034548225 scopus 로고    scopus 로고
    • The N-terminal lipopeptide of a 44-kDa membrane-bound lipoprotein of Mycoplasma salivarium is responsible for the expression of intercellular adhesion molecule-1 on the cell surface of normal human gingival fibroblasts
    • K. Shibata, A. Hasebe, T. Into, M. Yamada, and T. Watanabe The N-terminal lipopeptide of a 44-kDa membrane-bound lipoprotein of Mycoplasma salivarium is responsible for the expression of intercellular adhesion molecule-1 on the cell surface of normal human gingival fibroblasts J. Immunol. 165 2000 6538 6544
    • (2000) J. Immunol. , vol.165 , pp. 6538-6544
    • Shibata, K.1    Hasebe, A.2    Into, T.3    Yamada, M.4    Watanabe, T.5
  • 21
    • 12544257510 scopus 로고    scopus 로고
    • Depletion of apolipoprotein N-acyltransferase causes mislocalization of outer membrane lipoproteins in Escherichia coli
    • C. Robichon, D. Vidal-Ingigliardi, and A.P. Pugsley Depletion of apolipoprotein N-acyltransferase causes mislocalization of outer membrane lipoproteins in Escherichia coli J. Biol. Chem. 280 2005 974 983
    • (2005) J. Biol. Chem. , vol.280 , pp. 974-983
    • Robichon, C.1    Vidal-Ingigliardi, D.2    Pugsley, A.P.3
  • 22
    • 49449107199 scopus 로고    scopus 로고
    • Direct visualization of the outer membrane of mycobacteria and corynebacteria in their native state
    • B. Zuber, M. Chami, C. Houssin, J. Dubochet, G. Griffiths, and M. Daffe Direct visualization of the outer membrane of mycobacteria and corynebacteria in their native state J. Bacteriol. 190 2008 5672 5680
    • (2008) J. Bacteriol. , vol.190 , pp. 5672-5680
    • Zuber, B.1    Chami, M.2    Houssin, C.3    Dubochet, J.4    Griffiths, G.5    Daffe, M.6
  • 23
    • 41649116701 scopus 로고    scopus 로고
    • Disclosure of the mycobacterial outer membrane: Cryo-electron tomography and vitreous sections reveal the lipid bilayer structure
    • C. Hoffmann, A. Leis, M. Niederweis, J.M. Plitzko, and H. Engelhardt Disclosure of the mycobacterial outer membrane: cryo-electron tomography and vitreous sections reveal the lipid bilayer structure Proc. Natl. Acad. Sci. U.S.A. 105 2008 3963 3967
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 3963-3967
    • Hoffmann, C.1    Leis, A.2    Niederweis, M.3    Plitzko, J.M.4    Engelhardt, H.5
  • 27
    • 33750601160 scopus 로고    scopus 로고
    • CD14 directly binds to triacylated lipopeptides and facilitates recognition of the lipopeptides by the receptor complex of Toll-like receptors 2 and 1 without binding to the complex
    • T. Nakata, M. Yasuda, M. Fujita, H. Kataoka, K. Kiura, H. Sano, and K. Shibata CD14 directly binds to triacylated lipopeptides and facilitates recognition of the lipopeptides by the receptor complex of Toll-like receptors 2 and 1 without binding to the complex Cell Microbiol. 8 2006 1899 1909
    • (2006) Cell Microbiol. , vol.8 , pp. 1899-1909
    • Nakata, T.1    Yasuda, M.2    Fujita, M.3    Kataoka, H.4    Kiura, K.5    Sano, H.6    Shibata, K.7
  • 28
    • 10344222956 scopus 로고    scopus 로고
    • TLR2 recognizes a bacterial lipopeptide through direct binding
    • T. Vasselon, P.A. Detmers, D. Charron, and A. Haziot TLR2 recognizes a bacterial lipopeptide through direct binding J. Immunol. 173 2004 7401 7405
    • (2004) J. Immunol. , vol.173 , pp. 7401-7405
    • Vasselon, T.1    Detmers, P.A.2    Charron, D.3    Haziot, A.4
  • 29
    • 0036521507 scopus 로고    scopus 로고
    • Toll-like receptor 2 (TLR2) mediates activation of stress-activated MAP kinase p38
    • T. Vasselon, W.A. Hanlon, S.D. Wright, and P.A. Detmers Toll-like receptor 2 (TLR2) mediates activation of stress-activated MAP kinase p38 J. Leukoc. Biol. 71 2002 503 510
    • (2002) J. Leukoc. Biol. , vol.71 , pp. 503-510
    • Vasselon, T.1    Hanlon, W.A.2    Wright, S.D.3    Detmers, P.A.4
  • 30
    • 79960305949 scopus 로고    scopus 로고
    • Innate immune responses to bacterial ligands in the peripheral human lung-role of alveolar epithelial TLR expression and signalling
    • A.J. Thorley, D. Grandolfo, E. Lim, P. Goldstraw, A. Young, and T.D. Tetley Innate immune responses to bacterial ligands in the peripheral human lung-role of alveolar epithelial TLR expression and signalling PLoS One 6 2011 e21827
    • (2011) PLoS One , vol.6 , pp. 21827
    • Thorley, A.J.1    Grandolfo, D.2    Lim, E.3    Goldstraw, P.4    Young, A.5    Tetley, T.D.6
  • 31
    • 77952065180 scopus 로고    scopus 로고
    • The Toll-like receptor 2 (TLR2) ligand FSL-1 is internalized via the clathrin-dependent endocytic pathway triggered by CD14 and CD36 but not by TLR2
    • H.M. Shamsul, A. Hasebe, M. Iyori, M. Ohtani, K. Kiura, D. Zhang, Y. Totsuka, and K. Shibata The Toll-like receptor 2 (TLR2) ligand FSL-1 is internalized via the clathrin-dependent endocytic pathway triggered by CD14 and CD36 but not by TLR2 Immunology 130 2010 262 272
    • (2010) Immunology , vol.130 , pp. 262-272
    • Shamsul, H.M.1    Hasebe, A.2    Iyori, M.3    Ohtani, M.4    Kiura, K.5    Zhang, D.6    Totsuka, Y.7    Shibata, K.8
  • 32
    • 33846915924 scopus 로고    scopus 로고
    • Contribution of Toll-like receptors to the innate immune response to Gram-negative and Gram-positive bacteria
    • G. Elson, I. Dunn-Siegrist, B. Daubeuf, and J. Pugin Contribution of Toll-like receptors to the innate immune response to Gram-negative and Gram-positive bacteria Blood 109 2007 1574 1583
    • (2007) Blood , vol.109 , pp. 1574-1583
    • Elson, G.1    Dunn-Siegrist, I.2    Daubeuf, B.3    Pugin, J.4
  • 38
    • 34548608447 scopus 로고    scopus 로고
    • Crystal structure of the TLR1-TLR2 heterodimer induced by binding of a tri-acylated lipopeptide
    • M.S. Jin, S.E. Kim, J.Y. Heo, M.E. Lee, H.M. Kim, S.G. Paik, H. Lee, and J.O. Lee Crystal structure of the TLR1-TLR2 heterodimer induced by binding of a tri-acylated lipopeptide Cell 130 2007 1071 1082
    • (2007) Cell , vol.130 , pp. 1071-1082
    • Jin, M.S.1    Kim, S.E.2    Heo, J.Y.3    Lee, M.E.4    Kim, H.M.5    Paik, S.G.6    Lee, H.7    Lee, J.O.8
  • 39
    • 2942590448 scopus 로고    scopus 로고
    • Synthetic lipopeptide adjuvants and Toll-like receptor 2-structure-activity relationships
    • R. Spohn, U. Buwitt-Beckmann, R. Brock, G. Jung, A.J. Ulmer, and K.H. Wiesmuller Synthetic lipopeptide adjuvants and Toll-like receptor 2-structure-activity relationships Vaccine 22 2004 2494 2499
    • (2004) Vaccine , vol.22 , pp. 2494-2499
    • Spohn, R.1    Buwitt-Beckmann, U.2    Brock, R.3    Jung, G.4    Ulmer, A.J.5    Wiesmuller, K.H.6
  • 40
    • 77949887383 scopus 로고    scopus 로고
    • A network of hydrogen bonds on the surface of TLR2 controls ligand positioning and cell signaling
    • A.V. Kajava, and T. Vasselon A network of hydrogen bonds on the surface of TLR2 controls ligand positioning and cell signaling J. Biol. Chem. 285 2010 6227 6234
    • (2010) J. Biol. Chem. , vol.285 , pp. 6227-6234
    • Kajava, A.V.1    Vasselon, T.2
  • 45
    • 7944226058 scopus 로고    scopus 로고
    • Lipoproteins of Mycobacterium tuberculosis: An abundant and functionally diverse class of cell envelope components
    • I.C. Sutcliffe, and D.J. Harrington Lipoproteins of Mycobacterium tuberculosis: an abundant and functionally diverse class of cell envelope components FEMS Microbiol. Rev. 28 2004 645 659
    • (2004) FEMS Microbiol. Rev. , vol.28 , pp. 645-659
    • Sutcliffe, I.C.1    Harrington, D.J.2
  • 47
    • 0025719032 scopus 로고
    • Atypical lipoteichoic acids of gram-positive bacteria
    • I.C. Sutcliffe, and N. Shaw Atypical lipoteichoic acids of gram-positive bacteria J. Bacteriol. 173 1991 7065 7069
    • (1991) J. Bacteriol. , vol.173 , pp. 7065-7069
    • Sutcliffe, I.C.1    Shaw, N.2
  • 48
    • 0028930319 scopus 로고
    • The lipoteichoic acids and lipoglycans of Gram-positive Bacteria: A chemotaxonomic perspective
    • I.C. Sutcliffe The lipoteichoic acids and lipoglycans of Gram-positive Bacteria: a chemotaxonomic perspective Syst. Appl. Microbiol. 17 1994 467 480
    • (1994) Syst. Appl. Microbiol. , vol.17 , pp. 467-480
    • Sutcliffe, I.C.1
  • 49
    • 0347479228 scopus 로고    scopus 로고
    • A continuum of anionic charge: Structures and functions of D-alanyl-teichoic acids in gram-positive bacteria
    • F.C. Neuhaus, and J. Baddiley A continuum of anionic charge: structures and functions of D-alanyl-teichoic acids in gram-positive bacteria Microbiol. Mol. Biol. Rev. 67 2003 686 723
    • (2003) Microbiol. Mol. Biol. Rev. , vol.67 , pp. 686-723
    • Neuhaus, F.C.1    Baddiley, J.2
  • 50
    • 0030017520 scopus 로고    scopus 로고
    • Influence of lipoteichoic acid structure on recognition by the macrophage scavenger receptor
    • J.W. Greenberg, W. Fischer, and K.A. Joiner Influence of lipoteichoic acid structure on recognition by the macrophage scavenger receptor Infect. Immun. 64 1996 3318 3325
    • (1996) Infect. Immun. , vol.64 , pp. 3318-3325
    • Greenberg, J.W.1    Fischer, W.2    Joiner, K.A.3
  • 51
    • 0035808774 scopus 로고    scopus 로고
    • Structure-function relationship of cytokine induction by lipoteichoic acid from Staphylococcus aureus
    • S. Morath, A. Geyer, and T. Hartung Structure-function relationship of cytokine induction by lipoteichoic acid from Staphylococcus aureus J. Exp. Med. 193 2001 393 397
    • (2001) J. Exp. Med. , vol.193 , pp. 393-397
    • Morath, S.1    Geyer, A.2    Hartung, T.3
  • 52
    • 0036157920 scopus 로고    scopus 로고
    • Structural decomposition and heterogeneity of commercial lipoteichoic Acid preparations
    • S. Morath, A. Geyer, I. Spreitzer, C. Hermann, and T. Hartung Structural decomposition and heterogeneity of commercial lipoteichoic Acid preparations Infect. Immun. 70 2002 938 944
    • (2002) Infect. Immun. , vol.70 , pp. 938-944
    • Morath, S.1    Geyer, A.2    Spreitzer, I.3    Hermann, C.4    Hartung, T.5
  • 53
    • 0022543504 scopus 로고
    • Comparative studies of lipoteichoic acids from several Bacillus strains
    • H. Iwasaki, A. Shimada, and E. Ito Comparative studies of lipoteichoic acids from several Bacillus strains J. Bacteriol. 167 1986 508 516
    • (1986) J. Bacteriol. , vol.167 , pp. 508-516
    • Iwasaki, H.1    Shimada, A.2    Ito, E.3
  • 55
    • 0022513681 scopus 로고
    • Structural studies on lipoteichoic acids from four Listeria strains
    • K. Uchikawa, I. Sekikawa, and I. Azuma Structural studies on lipoteichoic acids from four Listeria strains J. Bacteriol. 168 1986 115 122
    • (1986) J. Bacteriol. , vol.168 , pp. 115-122
    • Uchikawa, K.1    Sekikawa, I.2    Azuma, I.3
  • 60
    • 79952740818 scopus 로고    scopus 로고
    • Chemical synthesis of bacterial lipoteichoic acids: An insight on its biological significance
    • R.R. Schmidt, C.M. Pedersen, Y. Qiao, and U. Zahringer Chemical synthesis of bacterial lipoteichoic acids: an insight on its biological significance Org. Biomol. Chem. 9 2011 2040 2052
    • (2011) Org. Biomol. Chem. , vol.9 , pp. 2040-2052
    • Schmidt, R.R.1    Pedersen, C.M.2    Qiao, Y.3    Zahringer, U.4
  • 61
    • 41549141383 scopus 로고    scopus 로고
    • A new model of pneumococcal lipoteichoic acid structure resolves biochemical, biosynthetic, and serologic inconsistencies of the current model
    • H.S. Seo, R.T. Cartee, D.G. Pritchard, and M.H. Nahm A new model of pneumococcal lipoteichoic acid structure resolves biochemical, biosynthetic, and serologic inconsistencies of the current model J. Bacteriol. 190 2008 2379 2387
    • (2008) J. Bacteriol. , vol.190 , pp. 2379-2387
    • Seo, H.S.1    Cartee, R.T.2    Pritchard, D.G.3    Nahm, M.H.4
  • 62
    • 79956141388 scopus 로고    scopus 로고
    • Location, synthesis and function of glycolipids and polyglycerolphosphate lipoteichoic acid in Gram-positive bacteria of the phylum Firmicutes
    • N.T. Reichman, and A. Grundling Location, synthesis and function of glycolipids and polyglycerolphosphate lipoteichoic acid in Gram-positive bacteria of the phylum Firmicutes FEMS Microbiol. Lett. 319 2011 97 105
    • (2011) FEMS Microbiol. Lett. , vol.319 , pp. 97-105
    • Reichman, N.T.1    Grundling, A.2
  • 63
    • 0026610897 scopus 로고
    • The structure of pneumococcal lipoteichoic acid. Improved preparation, chemical and mass spectrometric studies
    • T. Behr, W. Fischer, J. Peter-Katalinic, and H. Egge The structure of pneumococcal lipoteichoic acid. Improved preparation, chemical and mass spectrometric studies Eur. J. Biochem. 207 1992 1063 1075
    • (1992) Eur. J. Biochem. , vol.207 , pp. 1063-1075
    • Behr, T.1    Fischer, W.2    Peter-Katalinic, J.3    Egge, H.4
  • 64
    • 0036233799 scopus 로고    scopus 로고
    • Role of lipoteichoic acid in infection and inflammation
    • I. Ginsburg Role of lipoteichoic acid in infection and inflammation Lancet Infect. Dis. 2 2002 171 179
    • (2002) Lancet Infect. Dis. , vol.2 , pp. 171-179
    • Ginsburg, I.1
  • 65
    • 37749015263 scopus 로고    scopus 로고
    • Lipoteichoic acid is important in innate immune responses to gram-positive bacteria
    • H.S. Seo, S.M. Michalek, and M.H. Nahm Lipoteichoic acid is important in innate immune responses to gram-positive bacteria Infect. Immun. 76 2008 206 213
    • (2008) Infect. Immun. , vol.76 , pp. 206-213
    • Seo, H.S.1    Michalek, S.M.2    Nahm, M.H.3
  • 66
    • 0036180692 scopus 로고    scopus 로고
    • Cytokine induction by purified lipoteichoic acids from various bacterial species-role of LBP, sCD14, CD14 and failure to induce IL-12 and subsequent IFN-gamma release
    • C. Hermann, I. Spreitzer, N.W. Schroder, S. Morath, M.D. Lehner, W. Fischer, C. Schutt, R.R. Schumann, and T. Hartung Cytokine induction by purified lipoteichoic acids from various bacterial species-role of LBP, sCD14, CD14 and failure to induce IL-12 and subsequent IFN-gamma release Eur. J. Immunol. 32 2002 541 551
    • (2002) Eur. J. Immunol. , vol.32 , pp. 541-551
    • Hermann, C.1    Spreitzer, I.2    Schroder, N.W.3    Morath, S.4    Lehner, M.D.5    Fischer, W.6    Schutt, C.7    Schumann, R.R.8    Hartung, T.9
  • 67
    • 0038182550 scopus 로고    scopus 로고
    • Lipoteichoic acid (LTA) of Streptococcus pneumoniae and Staphylococcus aureus activates immune cells via Toll-like receptor (TLR)-2, lipopolysaccharide-binding protein (LBP), and CD14, whereas TLR-4 and MD-2 are not involved
    • N.W. Schroder, S. Morath, C. Alexander, L. Hamann, T. Hartung, U. Zahringer, U.B. Gobel, J.R. Weber, and R.R. Schumann Lipoteichoic acid (LTA) of Streptococcus pneumoniae and Staphylococcus aureus activates immune cells via Toll-like receptor (TLR)-2, lipopolysaccharide-binding protein (LBP), and CD14, whereas TLR-4 and MD-2 are not involved J. Biol. Chem. 278 2003 15587 15594
    • (2003) J. Biol. Chem. , vol.278 , pp. 15587-15594
    • Schroder, N.W.1    Morath, S.2    Alexander, C.3    Hamann, L.4    Hartung, T.5    Zahringer, U.6    Gobel, U.B.7    Weber, J.R.8    Schumann, R.R.9
  • 69
    • 33747806614 scopus 로고    scopus 로고
    • Not lipoteichoic acid but lipoproteins appear to be the dominant immunobiologically active compounds in Staphylococcus aureus
    • M. Hashimoto, K. Tawaratsumida, H. Kariya, A. Kiyohara, Y. Suda, F. Krikae, T. Kirikae, and F. Gotz Not lipoteichoic acid but lipoproteins appear to be the dominant immunobiologically active compounds in Staphylococcus aureus J. Immunol. 177 2006 3162 3169
    • (2006) J. Immunol. , vol.177 , pp. 3162-3169
    • Hashimoto, M.1    Tawaratsumida, K.2    Kariya, H.3    Kiyohara, A.4    Suda, Y.5    Krikae, F.6    Kirikae, T.7    Gotz, F.8
  • 70
    • 41649115159 scopus 로고    scopus 로고
    • TLR2-promiscuous or specific? A critical re-evaluation of a receptor expressing apparent broad specificity
    • U. Zahringer, B. Lindner, S. Inamura, H. Heine, and C. Alexander TLR2-promiscuous or specific? A critical re-evaluation of a receptor expressing apparent broad specificity Immunobiology 213 2008 205 224
    • (2008) Immunobiology , vol.213 , pp. 205-224
    • Zahringer, U.1    Lindner, B.2    Inamura, S.3    Heine, H.4    Alexander, C.5
  • 72
    • 68149163381 scopus 로고    scopus 로고
    • Lipoprotein lipase and hydrofluoric acid deactivate both bacterial lipoproteins and lipoteichoic acids, but platelet-activating factor-acetylhydrolase degrades only lipoteichoic acids
    • H.S. Seo, and M.H. Nahm Lipoprotein lipase and hydrofluoric acid deactivate both bacterial lipoproteins and lipoteichoic acids, but platelet-activating factor-acetylhydrolase degrades only lipoteichoic acids Clin. Vaccine Immunol. 16 2009 1187 1195
    • (2009) Clin. Vaccine Immunol. , vol.16 , pp. 1187-1195
    • Seo, H.S.1    Nahm, M.H.2
  • 73
    • 0037124358 scopus 로고    scopus 로고
    • Synthetic lipoteichoic acid from Staphylococcus aureus is a potent stimulus of cytokine release
    • S. Morath, A. Stadelmaier, A. Geyer, R.R. Schmidt, and T. Hartung Synthetic lipoteichoic acid from Staphylococcus aureus is a potent stimulus of cytokine release J. Exp. Med. 195 2002 1635 1640
    • (2002) J. Exp. Med. , vol.195 , pp. 1635-1640
    • Morath, S.1    Stadelmaier, A.2    Geyer, A.3    Schmidt, R.R.4    Hartung, T.5
  • 74
    • 78149468874 scopus 로고    scopus 로고
    • Internalization and coreceptor expression are critical for TLR2-mediated recognition of lipoteichoic acid in human peripheral blood
    • S. Bunk, S. Sigel, D. Metzdorf, O. Sharif, K. Triantafilou, M. Triantafilou, T. Hartung, S. Knapp, and S. von Aulock Internalization and coreceptor expression are critical for TLR2-mediated recognition of lipoteichoic acid in human peripheral blood J. Immunol. 185 2010 3708 3717
    • (2010) J. Immunol. , vol.185 , pp. 3708-3717
    • Bunk, S.1    Sigel, S.2    Metzdorf, D.3    Sharif, O.4    Triantafilou, K.5    Triantafilou, M.6    Hartung, T.7    Knapp, S.8    Von Aulock, S.9
  • 78
    • 0029583043 scopus 로고
    • Identification of a lipoarabinomannan-like lipoglycan in Corynebacterium matruchotii
    • I.C. Sutcliffe Identification of a lipoarabinomannan-like lipoglycan in Corynebacterium matruchotii Arch. Oral Biol. 40 1995 1119 1124
    • (1995) Arch. Oral Biol. , vol.40 , pp. 1119-1124
    • Sutcliffe, I.C.1
  • 79
    • 23344447255 scopus 로고    scopus 로고
    • A lipomannan variant with strong TLR-2-dependent pro-inflammatory activity in Saccharothrix aerocolonigenes
    • K.J. Gibson, M. Gilleron, P. Constant, B. Sichi, G. Puzo, G.S. Besra, and J. Nigou A lipomannan variant with strong TLR-2-dependent pro-inflammatory activity in Saccharothrix aerocolonigenes J. Biol. Chem. 280 2005 28347 28356
    • (2005) J. Biol. Chem. , vol.280 , pp. 28347-28356
    • Gibson, K.J.1    Gilleron, M.2    Constant, P.3    Sichi, B.4    Puzo, G.5    Besra, G.S.6    Nigou, J.7
  • 80
    • 0031951727 scopus 로고    scopus 로고
    • Mycobacterial lipoarabinomannan: An extraordinary lipoheteroglycan with profound physiological effects
    • D. Chatterjee, and K.H. Khoo Mycobacterial lipoarabinomannan: an extraordinary lipoheteroglycan with profound physiological effects Glycobiology 8 1998 113 120
    • (1998) Glycobiology , vol.8 , pp. 113-120
    • Chatterjee, D.1    Khoo, K.H.2
  • 81
    • 0037200040 scopus 로고    scopus 로고
    • A novel lipoarabinomannan from the equine pathogen Rhodococcus equi. Structure and effect on macrophage cytokine production
    • N.J. Garton, M. Gilleron, T. Brando, H.H. Dan, S. Giguere, G. Puzo, J.F. Prescott, and I.C. Sutcliffe A novel lipoarabinomannan from the equine pathogen Rhodococcus equi. Structure and effect on macrophage cytokine production J. Biol. Chem. 277 2002 31722 31733
    • (2002) J. Biol. Chem. , vol.277 , pp. 31722-31733
    • Garton, N.J.1    Gilleron, M.2    Brando, T.3    Dan, H.H.4    Giguere, S.5    Puzo, G.6    Prescott, J.F.7    Sutcliffe, I.C.8
  • 82
    • 0038175124 scopus 로고    scopus 로고
    • Lipoarabinomannans: From structure to biosynthesis
    • J. Nigou, M. Gilleron, and G. Puzo Lipoarabinomannans: from structure to biosynthesis Biochimie 85 2003 153 166
    • (2003) Biochimie , vol.85 , pp. 153-166
    • Nigou, J.1    Gilleron, M.2    Puzo, G.3
  • 83
    • 20444398128 scopus 로고    scopus 로고
    • Lipoarabinomannans-structurally diverse and functionally enigmatic macroamphiphiles of mycobacteria and related actinomycetes
    • I. Sutcliffe Lipoarabinomannans-structurally diverse and functionally enigmatic macroamphiphiles of mycobacteria and related actinomycetes Tuberculosis (Edinb) 85 2005 205 206
    • (2005) Tuberculosis (Edinb) , vol.85 , pp. 205-206
    • Sutcliffe, I.1
  • 84
    • 54349105831 scopus 로고    scopus 로고
    • Structure, biosynthesis and activities of the phosphatidyl-myo-inositol- based lipoglycans
    • M. Daffe, J. Reyrat, ASM Press Washington DC
    • M. Gilleron, M. Jackson, J. Nigou, and G. Puzo Structure, biosynthesis and activities of the phosphatidyl-myo-inositol-based lipoglycans M. Daffe, J. Reyrat, The Mycobacterial Cell Envelope 2008 ASM Press Washington DC 75 105
    • (2008) The Mycobacterial Cell Envelope , pp. 75-105
    • Gilleron, M.1    Jackson, M.2    Nigou, J.3    Puzo, G.4
  • 85
    • 80053565048 scopus 로고    scopus 로고
    • Lipoarabinomannan and related glycoconjugates: Structure, biogenesis and role in Mycobacterium tuberculosis physiology and host-pathogen interaction
    • A.K. Mishra, N.N. Driessen, B.J. Appelmelk, and G.S. Besra Lipoarabinomannan and related glycoconjugates: structure, biogenesis and role in Mycobacterium tuberculosis physiology and host-pathogen interaction FEMS Microbiol. Rev. 35 2011 1126 1157
    • (2011) FEMS Microbiol. Rev. , vol.35 , pp. 1126-1157
    • Mishra, A.K.1    Driessen, N.N.2    Appelmelk, B.J.3    Besra, G.S.4
  • 86
    • 3242876593 scopus 로고    scopus 로고
    • Mycobacterial lipoarabinomannan and related lipoglycans: From biogenesis to modulation of the immune response
    • V. Briken, S.A. Porcelli, G.S. Besra, and L. Kremer Mycobacterial lipoarabinomannan and related lipoglycans: from biogenesis to modulation of the immune response Mol. Microbiol. 53 2004 391 403
    • (2004) Mol. Microbiol. , vol.53 , pp. 391-403
    • Briken, V.1    Porcelli, S.A.2    Besra, G.S.3    Kremer, L.4
  • 87
    • 0001023242 scopus 로고    scopus 로고
    • Relationships between the structure and the roles of lipoarabinomannans and related glycoconjugates in tuberculosis pathogenesis
    • A. Vercellone, J. Nigou, and G. Puzo Relationships between the structure and the roles of lipoarabinomannans and related glycoconjugates in tuberculosis pathogenesis Front. Biosci. 3 1998 e149 163
    • (1998) Front. Biosci. , vol.3 , pp. 149-163
    • Vercellone, A.1    Nigou, J.2    Puzo, G.3
  • 88
    • 54349112644 scopus 로고    scopus 로고
    • The immunomodulatory lipoglycans, lipoarabinomannan and lipomannan, are exposed at the mycobacterial cell surface
    • S. Pitarque, G. Larrouy-Maumus, B. Payre, M. Jackson, G. Puzo, and J. Nigou The immunomodulatory lipoglycans, lipoarabinomannan and lipomannan, are exposed at the mycobacterial cell surface Tuberculosis (Edinb) 88 2008 560 565
    • (2008) Tuberculosis (Edinb) , vol.88 , pp. 560-565
    • Pitarque, S.1    Larrouy-Maumus, G.2    Payre, B.3    Jackson, M.4    Puzo, G.5    Nigou, J.6
  • 90
    • 0036065592 scopus 로고    scopus 로고
    • Mycobacterial lipoarabinomannans: Modulators of dendritic cell function and the apoptotic response
    • J. Nigou, M. Gilleron, M. Rojas, L.F. Garcia, M. Thurnher, and G. Puzo Mycobacterial lipoarabinomannans: modulators of dendritic cell function and the apoptotic response Microbes Infect. 4 2002 945 953
    • (2002) Microbes Infect. , vol.4 , pp. 945-953
    • Nigou, J.1    Gilleron, M.2    Rojas, M.3    Garcia, L.F.4    Thurnher, M.5    Puzo, G.6
  • 91
    • 1642375617 scopus 로고    scopus 로고
    • Toll-like receptor 2 (TLR2)-dependent-positive and TLR2-independent- negative regulation of proinflammatory cytokines by mycobacterial lipomannans
    • V.J. Quesniaux, D.M. Nicolle, D. Torres, L. Kremer, Y. Guerardel, J. Nigou, G. Puzo, F. Erard, and B. Ryffel Toll-like receptor 2 (TLR2)-dependent-positive and TLR2-independent-negative regulation of proinflammatory cytokines by mycobacterial lipomannans J. Immunol. 172 2004 4425 4434
    • (2004) J. Immunol. , vol.172 , pp. 4425-4434
    • Quesniaux, V.J.1    Nicolle, D.M.2    Torres, D.3    Kremer, L.4    Guerardel, Y.5    Nigou, J.6    Puzo, G.7    Erard, F.8    Ryffel, B.9
  • 92
    • 0041633850 scopus 로고    scopus 로고
    • Lipomannans, but not lipoarabinomannans, purified from Mycobacterium chelonae and Mycobacterium kansasii induce TNF-alpha and IL-8 secretion by a CD14-toll-like receptor 2-dependent mechanism
    • C. Vignal, Y. Guerardel, L. Kremer, M. Masson, D. Legrand, J. Mazurier, and E. Elass Lipomannans, but not lipoarabinomannans, purified from Mycobacterium chelonae and Mycobacterium kansasii induce TNF-alpha and IL-8 secretion by a CD14-toll-like receptor 2-dependent mechanism J. Immunol. 171 2003 2014 2023
    • (2003) J. Immunol. , vol.171 , pp. 2014-2023
    • Vignal, C.1    Guerardel, Y.2    Kremer, L.3    Masson, M.4    Legrand, D.5    Mazurier, J.6    Elass, E.7
  • 94
    • 0033458799 scopus 로고    scopus 로고
    • Toll-like receptor-2 mediates mycobacteria-induced proinflammatory signaling in macrophages
    • D.M. Underhill, A. Ozinsky, K.D. Smith, and A. Aderem Toll-like receptor-2 mediates mycobacteria-induced proinflammatory signaling in macrophages Proc. Natl. Acad. Sci. U.S.A. 96 1999 14459 14463
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 14459-14463
    • Underhill, D.M.1    Ozinsky, A.2    Smith, K.D.3    Aderem, A.4
  • 95
    • 0032716031 scopus 로고    scopus 로고
    • The CD14 ligands lipoarabinomannan and lipopolysaccharide differ in their requirement for Toll-like receptors
    • T.K. Means, E. Lien, A. Yoshimura, S. Wang, D.T. Golenbock, and M.J. Fenton The CD14 ligands lipoarabinomannan and lipopolysaccharide differ in their requirement for Toll-like receptors J. Immunol. 163 1999 6748 6755
    • (1999) J. Immunol. , vol.163 , pp. 6748-6755
    • Means, T.K.1    Lien, E.2    Yoshimura, A.3    Wang, S.4    Golenbock, D.T.5    Fenton, M.J.6
  • 97
    • 0043032571 scopus 로고    scopus 로고
    • Acylation state of the phosphatidylinositol hexamannosides from Mycobacterium bovis bacillus Calmette Guerin and mycobacterium tuberculosis H37Rv and its implication in Toll-like receptor response
    • M. Gilleron, V.F. Quesniaux, and G. Puzo Acylation state of the phosphatidylinositol hexamannosides from Mycobacterium bovis bacillus Calmette Guerin and mycobacterium tuberculosis H37Rv and its implication in Toll-like receptor response J. Biol. Chem. 278 2003 29880 29889
    • (2003) J. Biol. Chem. , vol.278 , pp. 29880-29889
    • Gilleron, M.1    Quesniaux, V.F.2    Puzo, G.3
  • 98
    • 30744468812 scopus 로고    scopus 로고
    • The acylation state of mycobacterial lipomannans modulates innate immunity response through toll-like receptor 2
    • M. Gilleron, J. Nigou, D. Nicolle, V. Quesniaux, and G. Puzo The acylation state of mycobacterial lipomannans modulates innate immunity response through toll-like receptor 2 Chem. Biol. 13 2006 39 47
    • (2006) Chem. Biol. , vol.13 , pp. 39-47
    • Gilleron, M.1    Nigou, J.2    Nicolle, D.3    Quesniaux, V.4    Puzo, G.5
  • 99
    • 25444493823 scopus 로고    scopus 로고
    • Mycobacterial lipomannan induces matrix metalloproteinase-9 expression in human macrophagic cells through a Toll-like receptor 1 (TLR1)/TLR2- and CD14-dependent mechanism
    • E. Elass, L. Aubry, M. Masson, A. Denys, Y. Guerardel, E. Maes, D. Legrand, J. Mazurier, and L. Kremer Mycobacterial lipomannan induces matrix metalloproteinase-9 expression in human macrophagic cells through a Toll-like receptor 1 (TLR1)/TLR2- and CD14-dependent mechanism Infect. Immun. 73 2005 7064 7068
    • (2005) Infect. Immun. , vol.73 , pp. 7064-7068
    • Elass, E.1    Aubry, L.2    Masson, M.3    Denys, A.4    Guerardel, Y.5    Maes, E.6    Legrand, D.7    Mazurier, J.8    Kremer, L.9
  • 102
    • 0033525121 scopus 로고    scopus 로고
    • Structural study of the lipomannans from Mycobacterium bovis BCG: Characterisation of multiacylated forms of the phosphatidyl-myo-inositol anchor
    • M. Gilleron, J. Nigou, B. Cahuzac, and G. Puzo Structural study of the lipomannans from Mycobacterium bovis BCG: characterisation of multiacylated forms of the phosphatidyl-myo-inositol anchor J. Mol. Biol. 285 1999 2147 2160
    • (1999) J. Mol. Biol. , vol.285 , pp. 2147-2160
    • Gilleron, M.1    Nigou, J.2    Cahuzac, B.3    Puzo, G.4
  • 103
    • 0033083642 scopus 로고    scopus 로고
    • Lipoarabinomannans: Characterization of the multiacylated forms of the phosphatidyl-myo-inositol anchor by NMR spectroscopy
    • J. Nigou, M. Gilleron, and G. Puzo Lipoarabinomannans: characterization of the multiacylated forms of the phosphatidyl-myo-inositol anchor by NMR spectroscopy Biochem. J. 337 Pt 3 1999 453 460
    • (1999) Biochem. J. , vol.337 , Issue.PART 3 , pp. 453-460
    • Nigou, J.1    Gilleron, M.2    Puzo, G.3
  • 104
  • 105
    • 2542438673 scopus 로고    scopus 로고
    • Tsukamurella paurometabola lipoglycan, a new lipoarabinomannan variant with pro-inflammatory activity
    • K.J. Gibson, M. Gilleron, P. Constant, T. Brando, G. Puzo, G.S. Besra, and J. Nigou Tsukamurella paurometabola lipoglycan, a new lipoarabinomannan variant with pro-inflammatory activity J. Biol. Chem. 279 2004 22973 22982
    • (2004) J. Biol. Chem. , vol.279 , pp. 22973-22982
    • Gibson, K.J.1    Gilleron, M.2    Constant, P.3    Brando, T.4    Puzo, G.5    Besra, G.S.6    Nigou, J.7
  • 106
    • 13244266949 scopus 로고    scopus 로고
    • Characterization of a truncated lipoarabinomannan from the Actinomycete Turicella otitidis
    • M. Gilleron, N.J. Garton, J. Nigou, T. Brando, G. Puzo, and I.C. Sutcliffe Characterization of a truncated lipoarabinomannan from the Actinomycete Turicella otitidis J. Bacteriol. 187 2005 854 861
    • (2005) J. Bacteriol. , vol.187 , pp. 854-861
    • Gilleron, M.1    Garton, N.J.2    Nigou, J.3    Brando, T.4    Puzo, G.5    Sutcliffe, I.C.6
  • 107
    • 0031023165 scopus 로고    scopus 로고
    • Mycobacterium smegmatis phosphoinositols-glyceroarabinomannans. Structure and localization of alkali-labile and alkali-stable phosphoinositides
    • M. Gilleron, N. Himoudi, O. Adam, P. Constant, A. Venisse, M. Riviere, and G. Puzo Mycobacterium smegmatis phosphoinositols-glyceroarabinomannans. Structure and localization of alkali-labile and alkali-stable phosphoinositides J. Biol. Chem. 272 1997 117 124
    • (1997) J. Biol. Chem. , vol.272 , pp. 117-124
    • Gilleron, M.1    Himoudi, N.2    Adam, O.3    Constant, P.4    Venisse, A.5    Riviere, M.6    Puzo, G.7
  • 108
    • 0026583133 scopus 로고
    • Structural basis of capacity of lipoarabinomannan to induce secretion of tumor necrosis factor
    • D. Chatterjee, A.D. Roberts, K. Lowell, P.J. Brennan, and I.M. Orme Structural basis of capacity of lipoarabinomannan to induce secretion of tumor necrosis factor Infect. Immun. 60 1992 1249 1253
    • (1992) Infect. Immun. , vol.60 , pp. 1249-1253
    • Chatterjee, D.1    Roberts, A.D.2    Lowell, K.3    Brennan, P.J.4    Orme, I.M.5
  • 109
    • 0034669971 scopus 로고    scopus 로고
    • Toll-like receptor 4, but not toll-like receptor 2, is a signaling receptor for Escherichia and Salmonella lipopolysaccharides
    • R.I. Tapping, S. Akashi, K. Miyake, P.J. Godowski, and P.S. Tobias Toll-like receptor 4, but not toll-like receptor 2, is a signaling receptor for Escherichia and Salmonella lipopolysaccharides J. Immunol. 165 2000 5780 5787
    • (2000) J. Immunol. , vol.165 , pp. 5780-5787
    • Tapping, R.I.1    Akashi, S.2    Miyake, K.3    Godowski, P.J.4    Tobias, P.S.5
  • 110
    • 0034662239 scopus 로고    scopus 로고
    • Cutting edge: Repurification of lipopolysaccharide eliminates signaling through both human and murine toll-like receptor 2
    • M. Hirschfeld, Y. Ma, J.H. Weis, S.N. Vogel, and J.J. Weis Cutting edge: repurification of lipopolysaccharide eliminates signaling through both human and murine toll-like receptor 2 J. Immunol. 165 2000 618 622
    • (2000) J. Immunol. , vol.165 , pp. 618-622
    • Hirschfeld, M.1    Ma, Y.2    Weis, J.H.3    Vogel, S.N.4    Weis, J.J.5
  • 111
    • 33644516283 scopus 로고    scopus 로고
    • Potent inhibition of macrophage responses to IFN-gamma by live virulent Mycobacterium tuberculosis is independent of mature mycobacterial lipoproteins but dependent on TLR2
    • N. Banaiee, E.Z. Kincaid, U. Buchwald, W.R. Jacobs Jr., and J.D. Ernst Potent inhibition of macrophage responses to IFN-gamma by live virulent Mycobacterium tuberculosis is independent of mature mycobacterial lipoproteins but dependent on TLR2 J. Immunol. 176 2006 3019 3027
    • (2006) J. Immunol. , vol.176 , pp. 3019-3027
    • Banaiee, N.1    Kincaid, E.Z.2    Buchwald, U.3    Jacobs, Jr.W.R.4    Ernst, J.D.5
  • 114
    • 34249677845 scopus 로고    scopus 로고
    • Therapeutic targeting of innate immunity with Toll-like receptor agonists and antagonists
    • H. Kanzler, F.J. Barrat, E.M. Hessel, and R.L. Coffman Therapeutic targeting of innate immunity with Toll-like receptor agonists and antagonists Nat. Med. 13 2007 552 559
    • (2007) Nat. Med. , vol.13 , pp. 552-559
    • Kanzler, H.1    Barrat, F.J.2    Hessel, E.M.3    Coffman, R.L.4
  • 116
    • 79956079190 scopus 로고    scopus 로고
    • Immunological mechanisms of vaccination
    • B. Pulendran, and R. Ahmed Immunological mechanisms of vaccination Nat. Immunol. 12 2011 509 517
    • (2011) Nat. Immunol. , vol.12 , pp. 509-517
    • Pulendran, B.1    Ahmed, R.2


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