메뉴 건너뛰기




Volumn 45, Issue 36, 2006, Pages 10957-10962

Prediction of glycolipid-binding domains from the amino acid sequence of lipid raft-associated proteins: Application to HpaA, a protein involved in the adhesion of Helicobacter pylori to gastrointestinal cells

Author keywords

[No Author keywords available]

Indexed keywords

ADHESION; AMINO ACIDS; BACTERIA; BONDING; CELLS; PATHOLOGY; PROTEINS;

EID: 33748513877     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi060762s     Document Type: Article
Times cited : (61)

References (35)
  • 1
    • 18744387685 scopus 로고    scopus 로고
    • Microbial entry through caveolae: Variations on a theme
    • Duncan, M. J., Shin, J.-S., and Abraham, S. N. (2002) Microbial entry through caveolae: variations on a theme, Cell. Microbiol. 4, 783-791.
    • (2002) Cell. Microbiol. , vol.4 , pp. 783-791
    • Duncan, M.J.1    Shin, J.-S.2    Abraham, S.N.3
  • 2
    • 33847738814 scopus 로고    scopus 로고
    • Lipid rafts: Structure, function and role in HIV, Alzheimer's and prion diseases
    • Fantini, J., Garmy, N., Mahfoud, R., and Yahi, N. (2002) Lipid rafts: structure, function and role in HIV, Alzheimer's and prion diseases, Exp. Rev. Mol. Med. 2002, 1-22.
    • (2002) Exp. Rev. Mol. Med. , vol.2002 , pp. 1-22
    • Fantini, J.1    Garmy, N.2    Mahfoud, R.3    Yahi, N.4
  • 3
    • 0037192816 scopus 로고    scopus 로고
    • Identification of a common sphingolipid-binding domain in Alzheimer, prion, and HIV-1 proteins
    • Mahfoud, R., Garmy, N., Maresca, M., Yahi, N., and Fantini, J. (2002) Identification of a common sphingolipid-binding domain in Alzheimer, prion, and HIV-1 proteins, J. Biol. Chem. 277, 11292-11296.
    • (2002) J. Biol. Chem. , vol.277 , pp. 11292-11296
    • Mahfoud, R.1    Garmy, N.2    Maresca, M.3    Yahi, N.4    Fantini, J.5
  • 4
    • 4344583947 scopus 로고    scopus 로고
    • A galactosylceramide binding domain is involved in trafficking of CLN3 from Golgi to rafts via recycling endosomes
    • Persaud-Sawin, D.-A., McNamara, J. O., II, Rylova, S., Vandongen, A., and Boustany, R.-M. N. (2004) A galactosylceramide binding domain is involved in trafficking of CLN3 from Golgi to rafts via recycling endosomes, Pediatr. Res. 56, 449-463.
    • (2004) Pediatr. Res. , vol.56 , pp. 449-463
    • Persaud-Sawin, D.-A.1    McNamara II, J.O.2    Rylova, S.3    Vandongen, A.4    Boustany, R.-M.N.5
  • 5
    • 4143064622 scopus 로고    scopus 로고
    • The combinatorial extension method reveals a sphingolipid binding domain on pancreatic bile salt-dependent lipase: Role in secretion
    • Aubert-Jousset, E., Garmy, N., Sbarra, V., Fantini, J., Sadoulet, M. O., and Lombardo, D. (2004) The combinatorial extension method reveals a sphingolipid binding domain on pancreatic bile salt-dependent lipase: role in secretion, Structure 12, 1437-1447.
    • (2004) Structure , vol.12 , pp. 1437-1447
    • Aubert-Jousset, E.1    Garmy, N.2    Sbarra, V.3    Fantini, J.4    Sadoulet, M.O.5    Lombardo, D.6
  • 6
    • 0038386467 scopus 로고    scopus 로고
    • How sphingolipids bind and shape proteins: Molecular basis of lipid-protein interactions in lipid shells, rafts and related biomembrane domains
    • Fantini, J. (2003) How sphingolipids bind and shape proteins: molecular basis of lipid-protein interactions in lipid shells, rafts and related biomembrane domains, Cell. Mol. Life Sci. 60, 1027-1032.
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 1027-1032
    • Fantini, J.1
  • 7
    • 0024339704 scopus 로고
    • Animal glycosphingolipids as membrane attachment sites for bacteria
    • Karlsson, K. A. (1989) Animal glycosphingolipids as membrane attachment sites for bacteria, Annu. Rev. Biochem. 58, 309-350.
    • (1989) Annu. Rev. Biochem. , vol.58 , pp. 309-350
    • Karlsson, K.A.1
  • 8
    • 0031217027 scopus 로고    scopus 로고
    • Epidemiology of Helicobacter pylori infection with special reference to professional risk
    • Matysiak-Budnik, T., and Megraud, F. (1997) Epidemiology of Helicobacter pylori infection with special reference to professional risk, J. Physiol. Pharmacol. 48 (Suppl. 4), 3-17.
    • (1997) J. Physiol. Pharmacol. , vol.48 , Issue.SUPPL. 4 , pp. 3-17
    • Matysiak-Budnik, T.1    Megraud, F.2
  • 9
    • 0029911619 scopus 로고    scopus 로고
    • Relationship between Helicobacter pylori eradication and reduced duodenal and gastric ulcer recurrence: A review
    • Hopkins, R. J., Gilardi, L. S., and Turney, E. A. (1996) Relationship between Helicobacter pylori eradication and reduced duodenal and gastric ulcer recurrence: a review, Gastroenterology 110, 1244-1252.
    • (1996) Gastroenterology , vol.110 , pp. 1244-1252
    • Hopkins, R.J.1    Gilardi, L.S.2    Turney, E.A.3
  • 10
    • 0034063957 scopus 로고    scopus 로고
    • Helicobacter pylori infection is the primary cause of gastric cancer
    • Graham, D. Y. (2000) Helicobacter pylori infection is the primary cause of gastric cancer, J. Gastroenterol. 35 (Suppl. 12), 90-97.
    • (2000) J. Gastroenterol. , vol.35 , Issue.SUPPL. 12 , pp. 90-97
    • Graham, D.Y.1
  • 12
    • 0027513390 scopus 로고
    • Cloning, nucleotide sequence, and expression of a gene encoding an adhesin subunit protein of Helicobacter pylori
    • Evans, D. J., Karjalainen, T. K., Evans, D. J., Jr., Graham, D. Y., and Lee, C.-H. (1993) Cloning, nucleotide sequence, and expression of a gene encoding an adhesin subunit protein of Helicobacter pylori, J. Bacterial. 175, 674-683.
    • (1993) J. Bacterial. , vol.175 , pp. 674-683
    • Evans, D.J.1    Karjalainen, T.K.2    Evans Jr., D.J.3    Graham, D.Y.4    Lee, C.-H.5
  • 13
    • 0031037910 scopus 로고    scopus 로고
    • Inhibition of Helicobacter pylori binding to gastrointestinal epithelial cells by sialic acid-containing oligosaccharides
    • Simon, P. M., Goode, P. L., Mobasseri, A., and Zopf, D. (1997) Inhibition of Helicobacter pylori binding to gastrointestinal epithelial cells by sialic acid-containing oligosaccharides, Infect. Immun. 65, 750-757.
    • (1997) Infect. Immun. , vol.65 , pp. 750-757
    • Simon, P.M.1    Goode, P.L.2    Mobasseri, A.3    Zopf, D.4
  • 14
    • 0028875018 scopus 로고
    • The putative neuraminyllactose-binding hemagglutinin HpaA of Helicobacter pylori CCUG 17874 is a lipoprotein
    • O'Toole, P. W., Janzon, L., Doig, P., Huang, J., Kostrzynska, M., and Trust, T. J. (1995) The putative neuraminyllactose-binding hemagglutinin HpaA of Helicobacter pylori CCUG 17874 is a lipoprotein, J. Bacteriol 177, 6049-6057.
    • (1995) J. Bacteriol. , vol.177 , pp. 6049-6057
    • O'Toole, P.W.1    Janzon, L.2    Doig, P.3    Huang, J.4    Kostrzynska, M.5    Trust, T.J.6
  • 15
    • 0037542606 scopus 로고    scopus 로고
    • Recombinant HpaA purified from Escherichia coli has biological properties similar to those of native Helicobacter pylori HpaA
    • Lundström, A. M., Bölin, I., Byström, M., and Nyström, S. (2003) Recombinant HpaA purified from Escherichia coli has biological properties similar to those of native Helicobacter pylori HpaA, APMIS 111, 389-397.
    • (2003) APMIS , vol.111 , pp. 389-397
    • Lundström, A.M.1    Bölin, I.2    Byström, M.3    Nyström, S.4
  • 16
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex, N., and Peitsch, M. C. (1997) SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling, Electrophoresis 18, 2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 18
    • 0003505803 scopus 로고    scopus 로고
    • Specific interactions in protein structures
    • (Nishio, M., Hirota, M., and Umezawa, Y., Eds.), Wiley-VCH, New York
    • Nishio, M., Hirota, M., and Umezawa, Y. (1998) Specific interactions in protein structures, in The CH/π Interaction, Evidence, Nature, and Consequences (Nishio, M., Hirota, M., and Umezawa, Y., Eds.) pp 175-202, Wiley-VCH, New York.
    • (1998) The CH/π Interaction, Evidence, Nature, and Consequences , pp. 175-202
    • Nishio, M.1    Hirota, M.2    Umezawa, Y.3
  • 19
    • 0037609791 scopus 로고    scopus 로고
    • Protein-protein interactions: Structurally conserved residues distinguish between binding sites and exposed protein surfaces
    • Ma, B., Elkayam, T., Wolfson, H., and Nussinov, R. (2003) Protein-protein interactions: structurally conserved residues distinguish between binding sites and exposed protein surfaces, Proc. Natl. Acad. Sci. U.S.A. 100, 5772-5777.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 5772-5777
    • Ma, B.1    Elkayam, T.2    Wolfson, H.3    Nussinov, R.4
  • 20
    • 0033784943 scopus 로고    scopus 로고
    • Reconstitution of sphingolipid-cholesterol plasma membrane microdomains for studies of virus-glycolipid interactions
    • Hammache, D., Pieroni, G., Maresca, M., Ivaldi, S., Yahi, N., and Fantini, J. (2000) Reconstitution of sphingolipid-cholesterol plasma membrane microdomains for studies of virus-glycolipid interactions, Methods Emymol 312, 495-506.
    • (2000) Methods Emymol , vol.312 , pp. 495-506
    • Hammache, D.1    Pieroni, G.2    Maresca, M.3    Ivaldi, S.4    Yahi, N.5    Fantini, J.6
  • 21
    • 0004060046 scopus 로고
    • Peptide-bilayer interactions: Physical measurements related to peptide structure
    • (Bentz, J., Ed.), CRC Press, Boca Raton, FL
    • Lear, J. D., and Rafalski, M. (1993) Peptide-Bilayer Interactions: Physical Measurements Related to Peptide Structure, in Viral Fusion Mechanisms (Bentz, J., Ed.) pp 55-66, CRC Press, Boca Raton, FL.
    • (1993) Viral Fusion Mechanisms , pp. 55-66
    • Lear, J.D.1    Rafalski, M.2
  • 22
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons, K., and Ikonen, E. (1997) Functional rafts in cell membranes, Nature 387, 569-572.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 23
    • 22744441951 scopus 로고    scopus 로고
    • Apical uptake and transepithelial transport of sphingosine monomers through intact human intestinal epithelial cells: Physicochemical and molecular modeling studies
    • Garmy, N., Taïeb, N., Yahi, N., and Fantini, J. (2005) Apical uptake and transepithelial transport of sphingosine monomers through intact human intestinal epithelial cells: physicochemical and molecular modeling studies, Arch. Biochem. Biophys. 440, 91-100.
    • (2005) Arch. Biochem. Biophys. , vol.440 , pp. 91-100
    • Garmy, N.1    Taïeb, N.2    Yahi, N.3    Fantini, J.4
  • 24
    • 0029952519 scopus 로고    scopus 로고
    • Structural basis of lectin-carbohydrate recognition
    • Weis, W. I., and Drickamer, K. (1996) Structural basis of lectin-carbohydrate recognition, Annu. Rev. Biochem. 65, 441-473.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 441-473
    • Weis, W.I.1    Drickamer, K.2
  • 25
    • 18844471722 scopus 로고    scopus 로고
    • Rafts and related glycosphingolipid-enriched microdomains in the intestinal epithelium: Bacterial targets linked to nutrient absorption
    • Taïeb, N., Yahi, N., and Fantini, J. (2004) Rafts and related glycosphingolipid-enriched microdomains in the intestinal epithelium: bacterial targets linked to nutrient absorption, Adv. Drug Deliv. Rev. 56, 779-794.
    • (2004) Adv. Drug Deliv. Rev. , vol.56 , pp. 779-794
    • Taïeb, N.1    Yahi, N.2    Fantini, J.3
  • 26
    • 0029117927 scopus 로고
    • The CH/Pi interaction: Significance in molecular recognition
    • Nishio, M., Umezawa, Y., Hirota, M., and Takeuchi, Y. (1995) The CH/Pi interaction: significance in molecular recognition, Tetrahedron 51, 8665-8701.
    • (1995) Tetrahedron , vol.51 , pp. 8665-8701
    • Nishio, M.1    Umezawa, Y.2    Hirota, M.3    Takeuchi, Y.4
  • 27
    • 1442300119 scopus 로고    scopus 로고
    • Identification of common structural features of binding sites in galactose-specific proteins
    • Sujatha, M. S., and Balajy, P. V. (2004) Identification of common structural features of binding sites in galactose-specific proteins, Proteins 55, 44-65.
    • (2004) Proteins , vol.55 , pp. 44-65
    • Sujatha, M.S.1    Balajy, P.V.2
  • 28
    • 4344662387 scopus 로고    scopus 로고
    • Energetics of galactose- and glucose-aromatic amino acid interactions: Implications for binding in galactose-specific proteins. Identification of common structural features of binding sites in galactose-specific proteins
    • Sujatha, M. S., Sasidhar, Y. U., and Balajy, P. V. (2004) Energetics of galactose- and glucose-aromatic amino acid interactions: implications for binding in galactose-specific proteins. Identification of common structural features of binding sites in galactose-specific proteins, Protein Sci. 13, 2502-2514.
    • (2004) Protein Sci. , vol.13 , pp. 2502-2514
    • Sujatha, M.S.1    Sasidhar, Y.U.2    Balajy, P.V.3
  • 29
    • 85012573093 scopus 로고
    • Glycosphingolipids
    • (Wiegandt, H., Ed.), Elsevier, Amsterdam
    • Makita, A., and Taniguchi, N. (1985) Glycosphingolipids, in Glycolipids (Wiegandt, H., Ed.) pp 1-99, Elsevier, Amsterdam.
    • (1985) Glycolipids , pp. 1-99
    • Makita, A.1    Taniguchi, N.2
  • 30
    • 4444261821 scopus 로고    scopus 로고
    • Role of CH/pi interactions in substrate binding by Escherichia coli beta-galactosidase
    • Spiwok, V., Lipovova, P., Skalova, T., Buchtelova, E., Hasek, J., and Kralova, B. (2004) Role of CH/pi interactions in substrate binding by Escherichia coli beta-galactosidase, Carbohydr. Res. 339, 2275-2280.
    • (2004) Carbohydr. Res. , vol.339 , pp. 2275-2280
    • Spiwok, V.1    Lipovova, P.2    Skalova, T.3    Buchtelova, E.4    Hasek, J.5    Kralova, B.6
  • 32
    • 0035707754 scopus 로고    scopus 로고
    • Inhibition of Helicobacter pylori adherence by a peptide derived from neuraminyl lactose binding adhesin
    • Chaturvedi, G., Tewari, R., Agnihotri, N., Vishwakarma, R. A., and Ganguly, N. K. (2001) Inhibition of Helicobacter pylori adherence by a peptide derived from neuraminyl lactose binding adhesin, Mol. Cell. Biochem. 228, 83-89.
    • (2001) Mol. Cell. Biochem. , vol.228 , pp. 83-89
    • Chaturvedi, G.1    Tewari, R.2    Agnihotri, N.3    Vishwakarma, R.A.4    Ganguly, N.K.5
  • 33
    • 0035182770 scopus 로고    scopus 로고
    • In vitro binding of Helicobacter pylori to monohexosylceramides
    • Abul-Milh, M., Barnette Foster, D., and Lingwood, C. A. (2001) In vitro binding of Helicobacter pylori to monohexosylceramides, Clycoconjugate J. 18, 253-260.
    • (2001) Clycoconjugate J. , vol.18 , pp. 253-260
    • Abul-Milh, M.1    Barnette Foster, D.2    Lingwood, C.A.3
  • 34
    • 0035687226 scopus 로고    scopus 로고
    • Helicobacter pylori-binding gangliosides of human gastric adenocarcinoma
    • Roche, N., Larsson, T., Ångstrom, J., and Teneberg, S. (2001) Helicobacter pylori-binding gangliosides of human gastric adenocarcinoma, Glycobiology 11, 935-944.
    • (2001) Glycobiology , vol.11 , pp. 935-944
    • Roche, N.1    Larsson, T.2    Ångstrom, J.3    Teneberg, S.4
  • 35
    • 0037036135 scopus 로고    scopus 로고
    • A role for lipid shells in targeting proteins to caveolae, rafts, and other lipid domains
    • Anderson, R. G., and Jacobson, K. (2002) A role for lipid shells in targeting proteins to caveolae, rafts, and other lipid domains, Science 296, 1821-1825.
    • (2002) Science , vol.296 , pp. 1821-1825
    • Anderson, R.G.1    Jacobson, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.