메뉴 건너뛰기




Volumn 8, Issue 6, 2000, Pages 585-592

A conserved structural motif for lipopolysaccharide recognition by procaryotic and eucaryotic proteins

Author keywords

Innate immune response; Lipopolysaccharide; Septic shock; Siderophore mediated iron acquisition; TonB dependent receptor

Indexed keywords

LIPOPOLYSACCHARIDE;

EID: 0034660537     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(00)00143-X     Document Type: Article
Times cited : (186)

References (39)
  • 2
    • 0004041866 scopus 로고    scopus 로고
    • H. Brade, D.C. Morrison, S. Opal, Vogel S. New York: Marcel Dekker Inc
    • Holst O. Endotoxin in Health and Disease. Brade H., Morrison D.C., Opal S., Vogel S. 1999;115-154 Marcel Dekker Inc, New York.
    • (1999) Endotoxin in Health and Disease , pp. 115-154
    • Holst, O.1
  • 4
    • 0030666222 scopus 로고    scopus 로고
    • Innate immunity: The virtues of a nonclonal system of recognition
    • Medzhitov R., Janeway C.A. Jr. Innate immunity: the virtues of a nonclonal system of recognition. Cell. 91:1997;295-298.
    • (1997) Cell , vol.91 , pp. 295-298
    • Medzhitov, R.1    Janeway, C.a.jr.2
  • 6
    • 0031803840 scopus 로고    scopus 로고
    • TonB-dependent iron acquisition: Mechanisms of siderophore-mediated active transport
    • Moeck G.S., Coulton J.W. TonB-dependent iron acquisition: mechanisms of siderophore-mediated active transport. Mol. Microbiol. 28:1998;675-681.
    • (1998) Mol. Microbiol. , vol.28 , pp. 675-681
    • Moeck, G.S.1    Coulton, J.W.2
  • 7
    • 0032545324 scopus 로고    scopus 로고
    • Siderophore-mediated iron transport: Crystal structure of FhuA with bound lipopolysaccharide
    • Ferguson A.D., Hofmann E., Coulton J.W., Diederichs K., Welte W. Siderophore-mediated iron transport: crystal structure of FhuA with bound lipopolysaccharide. Science. 282:1998;2215-2220.
    • (1998) Science , vol.282 , pp. 2215-2220
    • Ferguson, A.D.1    Hofmann, E.2    Coulton, J.W.3    Diederichs, K.4    Welte, W.5
  • 9
    • 0029782024 scopus 로고    scopus 로고
    • Conformation of lipid A, the endotoxic center of bacterial lipopolysaccharide
    • Brandenburg K., Rietschel E.T.et al. Conformation of lipid A, the endotoxic center of bacterial lipopolysaccharide. J. Endotoxin Res. 3:1996;173-178.
    • (1996) J. Endotoxin Res. , vol.3 , pp. 173-178
    • Brandenburg, K.1    Rietschel, E.T.2
  • 10
    • 0032414254 scopus 로고    scopus 로고
    • Transmembrane signaling across the ligand-gated FhuA receptor: Crystal structures of free and ferrichrome-bound states reveal allosteric changes
    • Locher K.P., Moras D.et al. Transmembrane signaling across the ligand-gated FhuA receptor: crystal structures of free and ferrichrome-bound states reveal allosteric changes. Cell. 95:1998;771-778.
    • (1998) Cell , vol.95 , pp. 771-778
    • Locher, K.P.1    Moras, D.2
  • 12
    • 0026319774 scopus 로고
    • Recognition of a cell-surface oligosaccharide of pathogenic Salmonella by an antibody Fab fragment
    • Cygler M., Rose D.R., Bundle D.R. Recognition of a cell-surface oligosaccharide of pathogenic Salmonella by an antibody Fab fragment. Science. 253:1991;442-445.
    • (1991) Science , vol.253 , pp. 442-445
    • Cygler, M.1    Rose, D.R.2    Bundle, D.R.3
  • 13
    • 0025762735 scopus 로고
    • Molecular modelling of bacterial deep rough mutant lipopolysaccharide of Escherichia coli
    • Kastowsky M., Sabisch A., Gutberlet T., Bradaczek H. Molecular modelling of bacterial deep rough mutant lipopolysaccharide of Escherichia coli. Eur. J. Biochem. 197:1991;707-716.
    • (1991) Eur. J. Biochem. , vol.197 , pp. 707-716
    • Kastowsky, M.1    Sabisch, A.2    Gutberlet, T.3    Bradaczek, H.4
  • 14
    • 0032538292 scopus 로고    scopus 로고
    • Lipid A acylation and bacterial resistance against vertebrate antimicrobial peptides
    • Guo L., Miller S.I.et al. Lipid A acylation and bacterial resistance against vertebrate antimicrobial peptides. Cell. 95:1998;189-198.
    • (1998) Cell , vol.95 , pp. 189-198
    • Guo, L.1    Miller, S.I.2
  • 15
    • 0032454840 scopus 로고    scopus 로고
    • Structure-function relationships of antimicrobial peptides
    • Hwang P.M., Vogel H.J. Structure-function relationships of antimicrobial peptides. Biochem. Cell Biol. 76:1998;235-246.
    • (1998) Biochem. Cell Biol. , vol.76 , pp. 235-246
    • Hwang, P.M.1    Vogel, H.J.2
  • 18
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zou J.Y., Cowan S.W., Kjeldgaard G. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A. 47:1991;110-119.
    • (1991) Acta Crystallogr. a , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, G.4
  • 19
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Brünger A.T., Warren G.L.et al. Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr. D. 54:1998;905-921.
    • (1998) Acta Crystallogr. D , vol.54 , pp. 905-921
    • Brünger, A.T.1    Warren, G.L.2
  • 20
    • 0033613813 scopus 로고    scopus 로고
    • Recognition of spatial motifs in protein structures
    • Kleywegt G. Recognition of spatial motifs in protein structures. J. Mol. Biol. 285:1999;1887-1897.
    • (1999) J. Mol. Biol. , vol.285 , pp. 1887-1897
    • Kleywegt, G.1
  • 21
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24:1991;946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 22
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D photorealistic molecular graphics
    • Merrit E.A., Bacon D.J. Raster3D photorealistic molecular graphics. Methods Enzymol. 277:1997;505-524.
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merrit, E.A.1    Bacon, D.J.2
  • 23
    • 0028154017 scopus 로고
    • Functional domains of recombinant bactericidal/permeability increasing protein (rBPI23)
    • Little R.G., Kelner D.N., Lim E., Burke D.J., Conlon P.J. Functional domains of recombinant bactericidal/permeability increasing protein (rBPI23). J. Biol. Chem. 269:1994;1865-1872.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1865-1872
    • Little, R.G.1    Kelner, D.N.2    Lim, E.3    Burke, D.J.4    Conlon, P.J.5
  • 24
    • 0031967690 scopus 로고    scopus 로고
    • The BPI/LBP family of proteins: A structural analysis of conserved regions
    • Beamer L.J., Carroll S.F., Eisenberg D. The BPI/LBP family of proteins: a structural analysis of conserved regions. Protein Sci. 7:1998;906-914.
    • (1998) Protein Sci. , vol.7 , pp. 906-914
    • Beamer, L.J.1    Carroll, S.F.2    Eisenberg, D.3
  • 25
    • 0029028016 scopus 로고
    • Lipopolysaccharide (LPS) neutralizing peptides reveal a lipid A binding site of LPS binding protein
    • Taylor A.H., Ghrayeb J.et al. Lipopolysaccharide (LPS) neutralizing peptides reveal a lipid A binding site of LPS binding protein. J. Biol. Chem. 270:1995;17934-17938.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17934-17938
    • Taylor, A.H.1    Ghrayeb, J.2
  • 26
    • 0030588577 scopus 로고    scopus 로고
    • Effects of site-directed mutagenesis of basic residues (Arg94, Lys95, Lys99) of lipopolysaccharide (LPS)-binding protein on binding and transfer of LPS and subsequent immune cell activation
    • Lamping N., Schumann R.R.et al. Effects of site-directed mutagenesis of basic residues (Arg94, Lys95, Lys99) of lipopolysaccharide (LPS)-binding protein on binding and transfer of LPS and subsequent immune cell activation. J. Immunol. 157:1996;4648-4656.
    • (1996) J. Immunol. , vol.157 , pp. 4648-4656
    • Lamping, N.1    Schumann, R.R.2
  • 27
    • 0028365405 scopus 로고
    • Lactoferrin is a lipid A binding protein
    • Appelmelk J., Nuijens J.H.et al. Lactoferrin is a lipid A binding protein. Infect. Immun. 62:1994;2628-2632.
    • (1994) Infect. Immun. , vol.62 , pp. 2628-2632
    • Appelmelk, J.1    Nuijens, J.H.2
  • 28
    • 0024389662 scopus 로고
    • Structure of human lactoferrin: Crystallographic structure analysis and refinement at 2.8 Å resolution
    • Anderson B.F., Baker H.M., Norris G.E., Rice D.W., Baker E.N. Structure of human lactoferrin: Crystallographic structure analysis and refinement at 2.8 Å resolution. J. Mol. Biol. 209:1989;711-734.
    • (1989) J. Mol. Biol. , vol.209 , pp. 711-734
    • Anderson, B.F.1    Baker, H.M.2    Norris, G.E.3    Rice, D.W.4    Baker, E.N.5
  • 29
    • 0030664951 scopus 로고    scopus 로고
    • N-terminal stretch Arg2, Arg3, Arg4 and Arg5 of human lactoferrin is essential for binding to heparin, bacterial lipopolysaccharide, human lysozyme and DNA
    • Van Berkel P.H.C., Nuijens J.H.et al. N-terminal stretch Arg2, Arg3, Arg4 and Arg5 of human lactoferrin is essential for binding to heparin, bacterial lipopolysaccharide, human lysozyme and DNA. Biochem. J. 328:1997;145-151.
    • (1997) Biochem. J. , vol.328 , pp. 145-151
    • Van Berkel, P.H.C.1    Nuijens, J.H.2
  • 30
    • 0031883875 scopus 로고    scopus 로고
    • Lactoferrin inhibits the endotoxin interaction with CD14 by competition with the lipopolysaccharide-binding protein
    • Elass-Rochard E., Spik G.et al. Lactoferrin inhibits the endotoxin interaction with CD14 by competition with the lipopolysaccharide-binding protein. Infect. Immun. 66:1998;486-491.
    • (1998) Infect. Immun. , vol.66 , pp. 486-491
    • Elass-Rochard, E.1    Spik, G.2
  • 31
    • 0029930976 scopus 로고    scopus 로고
    • Antibacterial activity of peptides homologous to a loop region in human lactoferrin
    • Odell E.W., Sarra R., Foxworthy M., Chapple D.S., Evans R.W. Antibacterial activity of peptides homologous to a loop region in human lactoferrin. FEBS Lett. 382:1996;175-178.
    • (1996) FEBS Lett. , vol.382 , pp. 175-178
    • Odell, E.W.1    Sarra, R.2    Foxworthy, M.3    Chapple, D.S.4    Evans, R.W.5
  • 32
    • 0032401651 scopus 로고    scopus 로고
    • Biophysical characterisation of lysozyme binding to LPS Re and lipid A
    • Brandenburg K., Koch M.H.J., Seydel U. Biophysical characterisation of lysozyme binding to LPS Re and lipid A. Eur. J. Biochem. 258:1998;686-695.
    • (1998) Eur. J. Biochem. , vol.258 , pp. 686-695
    • Brandenburg, K.1    Koch, M.H.J.2    Seydel, U.3
  • 33
    • 0019816864 scopus 로고
    • Refinement of human lysozyme at 1.5 Å resolution. Analysis of nonbonded and hydrogen-bond interactions
    • Artymiuk P.J., Blake C.C.F. Refinement of human lysozyme at 1.5 Å resolution. Analysis of nonbonded and hydrogen-bond interactions. J. Mol. Biol. 152:1981;733-762.
    • (1981) J. Mol. Biol. , vol.152 , pp. 733-762
    • Artymiuk, P.J.1    Blake, C.C.F.2
  • 34
    • 0013852463 scopus 로고
    • Structure of hen egg-white lysozyme
    • Blake C.C.F., Sarma V.R.et al. Structure of hen egg-white lysozyme. Nature. 206:1965;757-761.
    • (1965) Nature , vol.206 , pp. 757-761
    • Blake, C.C.F.1    Sarma, V.R.2
  • 35
    • 0020629394 scopus 로고
    • Goose lysozyme structure: An evolutionary link between hen and bacteriophage lysozymes?
    • Grütter M.G., Weaver L.H., Matthews B.W. Goose lysozyme structure: an evolutionary link between hen and bacteriophage lysozymes? Nature. 303:1983;828-831.
    • (1983) Nature , vol.303 , pp. 828-831
    • Grütter, M.G.1    Weaver, L.H.2    Matthews, B.W.3
  • 36
    • 0346436100 scopus 로고
    • The three-dimensional structure of the lysozyme from bacteriophage T4
    • Matthews B.W., Remington S.J. The three-dimensional structure of the lysozyme from bacteriophage T4. Proc. Natl Acad. Sci. USA. 71:1974;4178-4182.
    • (1974) Proc. Natl Acad. Sci. USA , vol.71 , pp. 4178-4182
    • Matthews, B.W.1    Remington, S.J.2
  • 37
    • 0026780772 scopus 로고
    • Binding and neutralization of endotoxin by Limulus antilipopolysaccharide factor
    • Warren H.S., Novitsky T.J.et al. Binding and neutralization of endotoxin by Limulus antilipopolysaccharide factor. Infect. Immun. 60:1992;2506-2513.
    • (1992) Infect. Immun. , vol.60 , pp. 2506-2513
    • Warren, H.S.1    Novitsky, T.J.2
  • 38
    • 0027171383 scopus 로고
    • Crystal structure of an endotoxin-neutralizing protein from the horseshoe crab, Limulus anti-LPS factor, at 1.5 Å resolution
    • Hoess A., Watson S., Siber G.R., Liddington R. Crystal structure of an endotoxin-neutralizing protein from the horseshoe crab, Limulus anti-LPS factor, at 1.5 Å resolution. EMBO J. 12:1993;3351-3356.
    • (1993) EMBO J. , vol.12 , pp. 3351-3356
    • Hoess, A.1    Watson, S.2    Siber, G.R.3    Liddington, R.4
  • 39
    • 0029902934 scopus 로고    scopus 로고
    • High affinity endotoxin-binding and neutralizing peptides based on the crystals structure of recombinant Limulus anti-lipopolysaccharide factor
    • Ried C., Hoess A.et al. High affinity endotoxin-binding and neutralizing peptides based on the crystals structure of recombinant Limulus anti-lipopolysaccharide factor. J. Biol. Chem. 271:1996;28120-28127.
    • (1996) J. Biol. Chem. , vol.271 , pp. 28120-28127
    • Ried, C.1    Hoess, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.