메뉴 건너뛰기




Volumn 1, Issue 1, 2010, Pages 17-30

Receptor mimicry as novel therapeutic treatment for biothreat agents

Author keywords

Anti adhesion; Attachment; Biothreat agents; Oligosaccharide; Respiratory tract

Indexed keywords

BOTULINUM TOXIN; CHONDROITIN SULFATE; GALACTOSE; GENTAMICIN; HEPARAN SULFATE; HEPARIN; MANNOSE; N ACETYLNEURAMINIC ACID; OLIGOSACCHARIDE; PROANTHOCYANIDIN; RICIN; SIALIDASE; SIALYL 3' LACTONEOTETRAOSE; SIALYLLACTOSE; STAPHYLOCOCCUS ENTEROTOXIN B; UNCLASSIFIED DRUG;

EID: 77957559971     PISSN: 19491018     EISSN: 19491026     Source Type: Journal    
DOI: 10.4161/bbug.1.1.10049     Document Type: Review
Times cited : (23)

References (151)
  • 1
    • 0036053928 scopus 로고    scopus 로고
    • Bioterrorism: From threat to reality
    • Atlas RM. Bioterrorism: from threat to reality. Annu Rev Microbiol 2002; 56:167-85.
    • (2002) Annu Rev Microbiol , vol.56 , pp. 167-185
    • Atlas, R.M.1
  • 5
    • 0037333208 scopus 로고    scopus 로고
    • "Multivalent" saccharides: Development of new approaches for inhibiting the effects of glycosphingolipid-binding pathogens
    • Schengrund CL. "Multivalent" saccharides: development of new approaches for inhibiting the effects of glycosphingolipid-binding pathogens. Biochem Pharmacol 2003; 65:699-707.
    • (2003) Biochem Pharmacol , vol.65 , pp. 699-707
    • Schengrund, C.L.1
  • 7
    • 0036052918 scopus 로고    scopus 로고
    • Fighting infectious disease with inhibitors of microbial adhesion to host tissues
    • Sharon N, Ofek I. Fighting infectious disease with inhibitors of microbial adhesion to host tissues. Crit Rev Food Sci 2002; 42:267-72.
    • (2002) Crit Rev Food Sci , vol.42 , pp. 267-272
    • Sharon, N.1    Ofek, I.2
  • 8
    • 0029881352 scopus 로고    scopus 로고
    • Oligosaccharide anti-infective agents
    • Zopf D, Roth S. Oligosaccharide anti-infective agents. Lancet 1996; 347:1017-21.
    • (1996) Lancet , vol.347 , pp. 1017-1021
    • Zopf, D.1    Roth, S.2
  • 9
    • 33646103431 scopus 로고    scopus 로고
    • Carbohydrates as future anti-adhesion drugs for infectious diseases
    • Sharon N. Carbohydrates as future anti-adhesion drugs for infectious diseases. Biochim Biophys Acta 2006; 1760:527-37.
    • (2006) Biochim Biophys Acta , vol.1760 , pp. 527-537
    • Sharon, N.1
  • 10
    • 77957586028 scopus 로고    scopus 로고
    • A novel mechanism of carbohydrate recognition by the C-type lectins DC-SIGN and DC-SIGNR
    • Mitchell DA, Fadden AJ, Drickamer K. A novel mechanism of carbohydrate recognition by the C-type lectins DC-SIGN and DC-SIGNR. J Biol Chem 2001; 276:2939-45.
    • (2001) J Biol Chem , vol.276 , pp. 2939-2945
    • Mitchell, D.A.1    Fadden, A.J.2    Drickamer, K.3
  • 11
    • 0041534400 scopus 로고    scopus 로고
    • Collectins and ficolins: Humoral lectins of the innate immune defense
    • Holmskov U, Thiel S, Jensenius JC. Collectins and ficolins: humoral lectins of the innate immune defense. Annu Rev Immunol 2003; 21:547-78.
    • (2003) Annu Rev Immunol , vol.21 , pp. 547-578
    • Holmskov, U.1    Thiel, S.2    Jensenius, J.C.3
  • 12
    • 0036278649 scopus 로고    scopus 로고
    • C-type lectins DC-SIGN and L-SIGN mediate cellular entry by Ebola virus in cis and in trans
    • Alvarez CP, Lasala F, Carrillo J, Muñiz O, Corbí AL, Delgado R. C-type lectins DC-SIGN and L-SIGN mediate cellular entry by Ebola virus in cis and in trans. J Virol 2002; 76:6841-4.
    • (2002) J Virol , vol.76 , pp. 6841-6844
    • Alvarez, C.P.1    Lasala, F.2    Carrillo, J.3    Muñiz, O.4    Corbí, A.L.5    Delgado, R.6
  • 13
    • 0028609712 scopus 로고
    • Receptor specificity of adherence of Streptococcus pneumoniae to human type-II pneumocytes and vascular endothelial cells in vitro
    • Cundell DR, Tuomanen EI. Receptor specificity of adherence of Streptococcus pneumoniae to human type-II pneumocytes and vascular endothelial cells in vitro. Microb Pathog 1994; 17:361-74.
    • (1994) Microb Pathog , vol.17 , pp. 361-374
    • Cundell, D.R.1    Tuomanen, E.I.2
  • 15
    • 0031037910 scopus 로고    scopus 로고
    • Inhibition of Helicobacter pylori binding to gastrointestinal epithelial cells by sialic acid-containing oligosaccharides
    • Simon PM, Goode PL, Mobasseri A, Zopf D. Inhibition of Helicobacter pylori binding to gastrointestinal epithelial cells by sialic acid-containing oligosaccharides. Infect Immun 1997; 65:750-7.
    • (1997) Infect Immun , vol.65 , pp. 750-757
    • Simon, P.M.1    Goode, P.L.2    Mobasseri, A.3    Zopf, D.4
  • 17
    • 0033022734 scopus 로고    scopus 로고
    • The effects of aerosolized dextran in a mouse model of Pseudomonas aeruginosa pulmonary infection
    • Bryan R, Feldman M, Jawetz SC, Rajan S, DiMango E, Tang H, et al. The effects of aerosolized dextran in a mouse model of Pseudomonas aeruginosa pulmonary infection. J Infect Dis 1999; 179:1449-58.
    • (1999) J Infect Dis , vol.179 , pp. 1449-1458
    • Bryan, R.1    Feldman, M.2    Jawetz, S.C.3    Rajan, S.4    Dimango, E.5    Tang, H.6
  • 18
    • 0025976345 scopus 로고
    • Pseudomonas aeruginosa recognizes carbohydrate chains containing type 1 (Galβ1-3GlcNAc) or type 2 (Galβ1-4GlcNAc) disaccharide units
    • Ramphal R, Carnoy C, Fievre S, Michalski J-C, Houdret N, Lamblin G, et al. Pseudomonas aeruginosa recognizes carbohydrate chains containing type 1 (Galβ1-3GlcNAc) or type 2 (Galβ1-4GlcNAc) disaccharide units. Infect Immun 1991; 59:700-4.
    • (1991) Infect Immun , vol.59 , pp. 700-704
    • Ramphal, R.1    Carnoy, C.2    Fievre, S.3    Michalski, J.-C.4    Houdret, N.5    Lamblin, G.6
  • 19
    • 0031809940 scopus 로고    scopus 로고
    • Interaction between the pili of Pseudomonas aeruginosa PAK and its carbohydrate receptor β-DGalNAc(1?4)β-D-Gal analogs
    • Schweizer F, Jiao H, Hindsgaul O, Wong WY, Irvin RT. Interaction between the pili of Pseudomonas aeruginosa PAK and its carbohydrate receptor β-DGalNAc(1?4)β-D-Gal analogs. Can J Microbiol 1997; 44:307-11.
    • (1997) Can J Microbiol , vol.44 , pp. 307-311
    • Schweizer, F.1    Jiao, H.2    Hindsgaul, O.3    Wong, W.Y.4    Irvin, R.T.5
  • 20
    • 0035153078 scopus 로고    scopus 로고
    • Role of heparan sulphate proteoglycans as potential receptors for non-piliated Pseudomonas aeruginosa adherence to non-polarised airway epithelial cells
    • Plotkowski MC, Costa AO, Morandi V, Barbosa HS, Nader HB, de Bentzmann S, et al. Role of heparan sulphate proteoglycans as potential receptors for non-piliated Pseudomonas aeruginosa adherence to non-polarised airway epithelial cells. J Med Microbiol 2001; 50:183-90.
    • (2001) J Med Microbiol , vol.50 , pp. 183-190
    • Plotkowski, M.C.1    Costa, A.O.2    Morandi, V.3    Barbosa, H.S.4    Nader, H.B.5    de Bentzmann, S.6
  • 21
    • 0348109477 scopus 로고    scopus 로고
    • Oligosaccharide receptor mimics inhibit Legionella pneumophila attachment to human respiratory cell lines
    • Thomas RJ, Brooks T. Oligosaccharide receptor mimics inhibit Legionella pneumophila attachment to human respiratory cell lines. Microb Pathog 2004; 36:83-92.
    • (2004) Microb Pathog , vol.36 , pp. 83-92
    • Thomas, R.J.1    Brooks, T.2
  • 22
    • 48149101636 scopus 로고    scopus 로고
    • In vivo effect of adhesion inhibitor heparin on Legionella pneumophila pathogenesis in a murine pneumonia model
    • Ader F, Le Berre R, Fackeure R, Raze D, Menozzi FD, Viget N, et al. In vivo effect of adhesion inhibitor heparin on Legionella pneumophila pathogenesis in a murine pneumonia model. Intensive Care Med 2008; 34:1511-9.
    • (2008) Intensive Care Med , vol.34 , pp. 1511-1519
    • Ader, F.1    le Berre, R.2    Fackeure, R.3    Raze, D.4    Menozzi, F.D.5    Viget, N.6
  • 23
    • 35648960384 scopus 로고    scopus 로고
    • Binding kinetics of influenza viruses to sialic acid-containing carbohydrates
    • Hidari KI, Shimada S, Suzuki Y, Suzuki T. Binding kinetics of influenza viruses to sialic acid-containing carbohydrates. Glycoconj J 2007; 24:583-90.
    • (2007) Glycoconj J , vol.24 , pp. 583-590
    • Hidari, K.I.1    Shimada, S.2    Suzuki, Y.3    Suzuki, T.4
  • 24
    • 0020694752 scopus 로고
    • Characterization of the binding of the TC-83 strain of Venezuelan Equine Encephalitis virus to BW-J-M, a mouse macrophage-like cell line
    • Huggins JW, Jahrling PB, Rill W, Linden CD. Characterization of the binding of the TC-83 strain of Venezuelan Equine Encephalitis virus to BW-J-M, a mouse macrophage-like cell line. J Gen Virol 1983; 64:149-57.
    • (1983) J Gen Virol , vol.64 , pp. 149-157
    • Huggins, J.W.1    Jahrling, P.B.2    Rill, W.3    Linden, C.D.4
  • 25
    • 0023856867 scopus 로고
    • Pseudomonas aeruginosa and Pseudomonas cepacia isolated from Cystic Fibrosis patients bind specifically to gangliotetraosylceramide (Asialo GM1) and gangliotriaosylceramide (Asialo GM2)
    • Krivan HC, Ginsburg V, Roberts DD. Pseudomonas aeruginosa and Pseudomonas cepacia isolated from Cystic Fibrosis patients bind specifically to gangliotetraosylceramide (Asialo GM1) and gangliotriaosylceramide (Asialo GM2). Arch Biochem Biophys 1988; 260:493-6.
    • (1988) Arch Biochem Biophys , vol.260 , pp. 493-496
    • Krivan, H.C.1    Ginsburg, V.2    Roberts, D.D.3
  • 26
    • 0011680902 scopus 로고
    • Many pulmonary pathogenic bacteria bind specifically to the carbohydrate sequence GalNAcβ1-4Gal found in some glycolipids
    • Krivan HC, Roberts DD, Ginsburg V. Many pulmonary pathogenic bacteria bind specifically to the carbohydrate sequence GalNAcβ1-4Gal found in some glycolipids. Proc Nat Acad Sci USA 1988; 85:6157-61.
    • (1988) Proc Nat Acad Sci USA , vol.85 , pp. 6157-6161
    • Krivan, H.C.1    Roberts, D.D.2    Ginsburg, V.3
  • 27
    • 0031301509 scopus 로고    scopus 로고
    • Specific binding of Burkholderia pseudomallei cells and their cell-surface acid phosphatase to gangliotetraosylceramide (asialo GM1) and gangliotriaosylceramide (asialo GM2)
    • Kanai K, Suzuki Y, Kondo E, Maejima Y, Miyamoto D, Suzuki T, Kurata T. Specific binding of Burkholderia pseudomallei cells and their cell-surface acid phosphatase to gangliotetraosylceramide (asialo GM1) and gangliotriaosylceramide (asialo GM2). Southeast Asian J Trop Med Public Health 1997; 28:781-90.
    • (1997) Southeast Asian J Trop Med Public Health , vol.28 , pp. 781-790
    • Kanai, K.1    Suzuki, Y.2    Kondo, E.3    Maejima, Y.4    Miyamoto, D.5    Suzuki, T.6    Kurata, T.7
  • 28
    • 0348041627 scopus 로고    scopus 로고
    • Carbohydrate-protein interactions at interfaces: Comparison of the binding of Ricinus communis lectin to two series of synthetic glycolipids using surface plasmon resonance studies
    • Critchley P, Clarkson GJ. Carbohydrate-protein interactions at interfaces: comparison of the binding of Ricinus communis lectin to two series of synthetic glycolipids using surface plasmon resonance studies. Org Biomol Chem 2003; 1:4148-59.
    • (2003) Org Biomol Chem , vol.1 , pp. 4148-4159
    • Critchley, P.1    Clarkson, G.J.2
  • 29
    • 4544249162 scopus 로고    scopus 로고
    • Common oligosaccharide moieties inhibit the adherence of typical and atypical respiratory pathogens
    • Thomas RJ, Brooks T. Common oligosaccharide moieties inhibit the adherence of typical and atypical respiratory pathogens. J Med Microbiol 2004; 53:833-40.
    • (2004) J Med Microbiol , vol.53 , pp. 833-840
    • Thomas, R.J.1    Brooks, T.2
  • 30
    • 35649003866 scopus 로고    scopus 로고
    • Intervention with bacterial adhesion by multivalent carbohydrates
    • Pieters RJ. Intervention with bacterial adhesion by multivalent carbohydrates. Med Res Rev 2007; 27:796-816.
    • (2007) Med Res Rev , vol.27 , pp. 796-816
    • Pieters, R.J.1
  • 31
    • 0029045189 scopus 로고
    • Particle inhalability curves for humans and small laboratory animals
    • Menache M, Miller F, Raabe O. Particle inhalability curves for humans and small laboratory animals. Ann Occ Hyg 1995; 39:317-28.
    • (1995) Ann Occ Hyg , vol.39 , pp. 317-328
    • Menache, M.1    Miller, F.2    Raabe, O.3
  • 33
    • 0026748190 scopus 로고
    • The broad diversity of neutral and sialylated oligosaccharides derived from human salivary mucins
    • Klein A, Carnoy J, Wieruszeski M, Strecker G, Strang AM, van Halbeek H, et al. The broad diversity of neutral and sialylated oligosaccharides derived from human salivary mucins. Biochem 1992; 31:6152-65.
    • (1992) Biochem , vol.31 , pp. 6152-6165
    • Klein, A.1    Carnoy, J.2    Wieruszeski, M.3    Strecker, G.4    Strang, A.M.5    van Halbeek, H.6
  • 34
    • 0028920643 scopus 로고
    • Cystic fibrosis epithelial cells have a receptor for pathogenic bacteria on their apical surface
    • Imundo L, Barasch J, Prince A, Al-Awqati Q. Cystic fibrosis epithelial cells have a receptor for pathogenic bacteria on their apical surface. Proc Natl Acad Sci USA 1995; 92:3019-23.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 3019-3023
    • Imundo, L.1    Barasch, J.2    Prince, A.3    Al-Awqati, Q.4
  • 35
    • 0029908168 scopus 로고    scopus 로고
    • Receptors in the Pseudomonas aeruginosa adherence to injured and repairing airway epithelium
    • De Bentzmann S, Plotkowski C, Puchelle E. Receptors in the Pseudomonas aeruginosa adherence to injured and repairing airway epithelium. Am J Respir Crit Care Med 1996; 154:155-62.
    • (1996) Am J Respir Crit Care Med , vol.154 , pp. 155-162
    • de Bentzmann, S.1    Plotkowski, C.2    Puchelle, E.3
  • 36
    • 0029767885 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa adherence to remodelling respiratory epithelium
    • De Bentzmann S, Roger P, Puchelle E. Pseudomonas aeruginosa adherence to remodelling respiratory epithelium. Eur Respir J 1996; 9:2145-50.
    • (1996) Eur Respir J , vol.9 , pp. 2145-2150
    • de Bentzmann, S.1    Roger, P.2    Puchelle, E.3
  • 37
    • 0029920335 scopus 로고    scopus 로고
    • Asialo GM1 is a receptor for Pseudomonas aeruginosa adherence to regenerating respiratory epithelial cells
    • De Bentzmann S, Roger P, Dupuit F, Bajolet- Laudinat O, Fuchey C, Plotkowski MC, et al. Asialo GM1 is a receptor for Pseudomonas aeruginosa adherence to regenerating respiratory epithelial cells. Infect Immun 1996; 64:1582-8.
    • (1996) Infect Immun , vol.64 , pp. 1582-1588
    • de Bentzmann, S.1    Roger, P.2    Dupuit, F.3    Bajolet-Laudinat, O.4    Fuchey, C.5    Plotkowski, M.C.6
  • 38
    • 23844546008 scopus 로고    scopus 로고
    • Stopping bacterial adhesion: A novel approach to treating infections
    • Bavington C, Page C. Stopping bacterial adhesion: a novel approach to treating infections. Respir 2005; 72:335-44.
    • (2005) Respir , vol.72 , pp. 335-344
    • Bavington, C.1    Page, C.2
  • 39
    • 33645110204 scopus 로고    scopus 로고
    • Attachment of Yersinia pestis to human respiratory cell lines is inhibited by certain oligosaccharides
    • Thomas RJ, Brooks T. Attachment of Yersinia pestis to human respiratory cell lines is inhibited by certain oligosaccharides. J Med Microbiol 2006; 55:309-15.
    • (2006) J Med Microbiol , vol.55 , pp. 309-315
    • Thomas, R.J.1    Brooks, T.2
  • 40
    • 0023689178 scopus 로고
    • Receptor analogs and monoclonal antibodies that inhibit adherence of Bordetella pertussis to human ciliated epithelial cells
    • Tuomanen E, Towbin H, Rosenfelder G, Braun D, Larson G, Hansson GC, et al. Receptor analogs and monoclonal antibodies that inhibit adherence of Bordetella pertussis to human ciliated epithelial cells. J Exp Med 1988; 168:267-77.
    • (1988) J Exp Med , vol.168 , pp. 267-277
    • Tuomanen, E.1    Towbin, H.2    Rosenfelder, G.3    Braun, D.4    Larson, G.5    Hansson, G.C.6
  • 41
    • 0026094284 scopus 로고
    • Adhesion of Bordetella pertussis to sulfatides and to the GalNAcβ1-4Gal sequence found in glycosphingolipids
    • Brennan MJ, Hannah JH, Leininger E. Adhesion of Bordetella pertussis to sulfatides and to the GalNAcβ1-4Gal sequence found in glycosphingolipids. J Biol Chem 1991; 266:18827-31.
    • (1991) J Biol Chem , vol.266 , pp. 18827-18831
    • Brennan, M.J.1    Hannah, J.H.2    Leininger, E.3
  • 42
    • 0030009996 scopus 로고    scopus 로고
    • The major fimbrial subunit of Bordetella pertussis binds to sulfated sugars
    • Guijen CA, Willems RJ, Mooi FR. The major fimbrial subunit of Bordetella pertussis binds to sulfated sugars. Infect Immun 1996; 64:2657-65.
    • (1996) Infect Immun , vol.64 , pp. 2657-2665
    • Guijen, C.A.1    Willems, R.J.2    Mooi, F.R.3
  • 44
    • 0029972810 scopus 로고    scopus 로고
    • Burkholderia (pseudonym Pseudomonas) cepacia binding to lipid receptors
    • Sylvester FA, Sajjan US, Forstner JF. Burkholderia (pseudonym Pseudomonas) cepacia binding to lipid receptors. Infect Immun 1996; 64:1420-5.
    • (1996) Infect Immun , vol.64 , pp. 1420-1425
    • Sylvester, F.A.1    Sajjan, U.S.2    Forstner, J.F.3
  • 45
    • 0034779118 scopus 로고    scopus 로고
    • Adherence of Burkholderia cepacia to respiratory tract epithelial cells and inhibition with dextrans
    • Chiu CH, Wong S, Hancock RE, Speert DP. Adherence of Burkholderia cepacia to respiratory tract epithelial cells and inhibition with dextrans. Microbiol 2001; 147:2651-8.
    • (2001) Microbiol , vol.147 , pp. 2651-2658
    • Chiu, C.H.1    Wong, S.2    Hancock, R.E.3    Speert, D.P.4
  • 46
    • 0032841852 scopus 로고    scopus 로고
    • Mediation of attachment of Burkholderia pseudomallei to human pharyngeal epithelial cells by the asialoganglioside GM1- GM2 receptor complex
    • Gori AH, Ahmed K, Martinez G, Masaki H, Watanabe K, Nagatake T. Mediation of attachment of Burkholderia pseudomallei to human pharyngeal epithelial cells by the asialoganglioside GM1- GM2 receptor complex. Am J Trop Med Hyg 1999; 61:473-5.
    • (1999) Am J Trop Med Hyg , vol.61 , pp. 473-475
    • Gori, A.H.1    Ahmed, K.2    Martinez, G.3    Masaki, H.4    Watanabe, K.5    Nagatake, T.6
  • 47
    • 0025810013 scopus 로고
    • Chlamydia trachomatis and Chlamydia pneumoniae bind specifically to phosphatidylethanolamine in HeLa cells and to GalNAcβ1-4Galβ1-4Glc sequences found in asialo-GM1 and asialo-GM2
    • Krivan HC, Nilsson B, Lingwood CA, Ryu H. Chlamydia trachomatis and Chlamydia pneumoniae bind specifically to phosphatidylethanolamine in HeLa cells and to GalNAcβ1-4Galβ1-4Glc sequences found in asialo-GM1 and asialo-GM2. Biochem Biophys Res Commun 1991; 175:1082-9.
    • (1991) Biochem Biophys Res Commun , vol.175 , pp. 1082-1089
    • Krivan, H.C.1    Nilsson, B.2    Lingwood, C.A.3    Ryu, H.4
  • 48
    • 0025787889 scopus 로고
    • Blocking of fimbria-mediated adherence of Haemophilus influenzae by sialyl gangliosides
    • van Alphen L, Geelen-van den Broek L, Blaas L, van Ham M, Dankert J. Blocking of fimbria-mediated adherence of Haemophilus influenzae by sialyl gangliosides. Infect Immun 1991; 4473-7.
    • (1991) Infect Immun , pp. 4473-4477
    • van Alphen, L.1    Blaas, L.2    van Ham, M.3    Dankert, J.4
  • 49
    • 0030459932 scopus 로고    scopus 로고
    • Inhibition by dextran of Pseudomonas aeruginosa adherence to epithelial cells
    • Barghouthi S, Guerdoud LM, Speert DP. Inhibition by dextran of Pseudomonas aeruginosa adherence to epithelial cells. Am J Respir Crit Care Med 1996; 154:1788-93.
    • (1996) Am J Respir Crit Care Med , vol.154 , pp. 1788-1793
    • Barghouthi, S.1    Guerdoud, L.M.2    Speert, D.P.3
  • 50
    • 0030998767 scopus 로고    scopus 로고
    • Specific binding of Haemophilus influenzae to minor gangliosides of human respiratory epithelial cells
    • Fakih MG, Murphy TF, Pattoli MA, Berenson CS. Specific binding of Haemophilus influenzae to minor gangliosides of human respiratory epithelial cells. Infect Immun 1997; 65:1695-700.
    • (1997) Infect Immun , vol.65 , pp. 1695-1700
    • Fakih, M.G.1    Murphy, T.F.2    Pattoli, M.A.3    Berenson, C.S.4
  • 53
    • 0023626961 scopus 로고
    • The hemagglutinins of the human influenza viruses A and B recognize different receptor microdomains
    • Suzuki Y, Nagao Y, Kato H, Suzuki T, Matsumoto M, Murayama J. The hemagglutinins of the human influenza viruses A and B recognize different receptor microdomains. Biochim Biophys Acta 1987; 903:417-24.
    • (1987) Biochim Biophys Acta , vol.903 , pp. 417-424
    • Suzuki, Y.1    Nagao, Y.2    Kato, H.3    Suzuki, T.4    Matsumoto, M.5    Murayama, J.6
  • 54
    • 0026039988 scopus 로고
    • Differential inhibitory effects of sulfated polysaccharides and polymers on the replication of various myxoviruses and retroviruses, depending on the composition of the target amino acid sequences of the viral envelope glycoproteins
    • Hosoya M, Balzarini J, Shigeta S, De Clerq E. Differential inhibitory effects of sulfated polysaccharides and polymers on the replication of various myxoviruses and retroviruses, depending on the composition of the target amino acid sequences of the viral envelope glycoproteins. Antimicrob Agents Chemother 1991; 35:2515-20.
    • (1991) Antimicrob Agents Chemother , vol.35 , pp. 2515-2520
    • Hosoya, M.1    Balzarini, J.2    Shigeta, S.3    de Clerq, E.4
  • 55
    • 0023638370 scopus 로고
    • The surface receptor is a major determinant of the cell tropism of influenza C virus
    • Herrler G, Klenk HD. The surface receptor is a major determinant of the cell tropism of influenza C virus. Virol 1987; 159:102-8.
    • (1987) Virol , vol.159 , pp. 102-108
    • Herrler, G.1    Klenk, H.D.2
  • 57
    • 0036250615 scopus 로고    scopus 로고
    • Asialo-GM1 and asialo-GM2 are putative adhesion molecules for Moraxella catarrhalis
    • Ahmed K, Suzuki Y, Miyamoto D, Nagatake T. Asialo-GM1 and asialo-GM2 are putative adhesion molecules for Moraxella catarrhalis. Med Microbiol Immunol 2002; 191:5-10.
    • (2002) Med Microbiol Immunol , vol.191 , pp. 5-10
    • Ahmed, K.1    Suzuki, Y.2    Miyamoto, D.3    Nagatake, T.4
  • 58
    • 0024371541 scopus 로고
    • Sialic acid-dependent adhesion of Mycoplasma pneumoniae to purified glycoproteins
    • Roberts DD, Olson LD, Barile MF, Ginsburg V, Krivan HC. Sialic acid-dependent adhesion of Mycoplasma pneumoniae to purified glycoproteins. J Biol Chem 1989; 264:9289-93.
    • (1989) J Biol Chem , vol.264 , pp. 9289-9293
    • Roberts, D.D.1    Olson, L.D.2    Barile, M.F.3    Ginsburg, V.4    Krivan, H.C.5
  • 59
    • 0024409821 scopus 로고
    • Adhesion of Mycoplasma pneumoniae to sulphated glycolipids and inhibition by dextran sulphate
    • Krivan HC, Olson LD, Barile MF, Ginsburg V, Roberts DD. Adhesion of Mycoplasma pneumoniae to sulphated glycolipids and inhibition by dextran sulphate. J Biol Chem 1989; 264:9283-8.
    • (1989) J Biol Chem , vol.264 , pp. 9283-9288
    • Krivan, H.C.1    Olson, L.D.2    Barile, M.F.3    Ginsburg, V.4    Roberts, D.D.5
  • 60
    • 0032445031 scopus 로고    scopus 로고
    • Glycosphingolipid binding specificities of Neisseria meningitidis and Haemophilus influenzae: Detection, isolation and characterization of a binding-active glycosphingolipid from human oropharyngeal epithelium
    • Hugosson S, Angström J, Olsson BM, Bergström J, Fredlund H, Olcen P, et al. Glycosphingolipid binding specificities of Neisseria meningitidis and Haemophilus influenzae: detection, isolation and characterization of a binding-active glycosphingolipid from human oropharyngeal epithelium. J Biochem 1998; 124:1138-52.
    • (1998) J Biochem , vol.124 , pp. 1138-1152
    • Hugosson, S.1    Angström, J.2    Olsson, B.M.3    Bergström, J.4    Fredlund, H.5    Olcen, P.6
  • 61
    • 0025729230 scopus 로고
    • Glycolipid receptor binding specificity of exoenzyme S from Pseudomonas aeruginosa
    • Lingwood CA, Cheng M, Krivan HC, Woods D. Glycolipid receptor binding specificity of exoenzyme S from Pseudomonas aeruginosa. Biochem Biophys Res Commun 1991; 175:1076-81.
    • (1991) Biochem Biophys Res Commun , vol.175 , pp. 1076-1081
    • Lingwood, C.A.1    Cheng, M.2    Krivan, H.C.3    Woods, D.4
  • 62
    • 0027196740 scopus 로고
    • Heparin inhibits Pseudomonas aeruginosa adherence to soft contact lens
    • Duran JA, Malvar A, Rodriguez-Ares MT, Garcia- Riestra C. Heparin inhibits Pseudomonas aeruginosa adherence to soft contact lens. Eye 1993; 7:152-4.
    • (1993) Eye , vol.7 , pp. 152-154
    • Duran, J.A.1    Malvar, A.2    Rodriguez-Ares, M.T.3    Garcia-Riestra, C.4
  • 64
    • 0032037617 scopus 로고    scopus 로고
    • Adherence of Streptococcus pneumoniae to respiratory epithelial cells is inhibited by sialylated oligosaccharides
    • Barthelson R, Mobasseri A, Zopf D, Simon P. Adherence of Streptococcus pneumoniae to respiratory epithelial cells is inhibited by sialylated oligosaccharides. Infect Immun 1998; 66:1439-44.
    • (1998) Infect Immun , vol.66 , pp. 1439-1444
    • Barthelson, R.1    Mobasseri, A.2    Zopf, D.3    Simon, P.4
  • 65
    • 0031719490 scopus 로고    scopus 로고
    • The pH 6 antigen of Yersinia pestis binds to β1-linked galactosyl residues in glycosphingolipids
    • Payne D, Tatham D, Williamson ED, Titball RW. The pH 6 antigen of Yersinia pestis binds to β1-linked galactosyl residues in glycosphingolipids. Infect Immun 1998; 66:4545-8.
    • (1998) Infect Immun , vol.66 , pp. 4545-4548
    • Payne, D.1    Tatham, D.2    Williamson, E.D.3    Titball, R.W.4
  • 66
    • 0026776010 scopus 로고
    • Adhesive properties conferred by the plasminogen activator of Yersinia pestis
    • Kienle Z, Emody L, Svanborg C, O'Toole PW. Adhesive properties conferred by the plasminogen activator of Yersinia pestis. J Gen Microbiol 1992; 138:1679-87.
    • (1992) J Gen Microbiol , vol.138 , pp. 1679-1687
    • Kienle, Z.1    Emody, L.2    Svanborg, C.3    O'Toole, P.W.4
  • 67
    • 0031771558 scopus 로고    scopus 로고
    • Expression of plasminogen activator Pla of Yersinia pestis enhances bacterial attachment to the mammalian extracellular matrix
    • Lähteenmäki K, Virkola R, Sarén A, Emödy L, Korhonen TK. Expression of plasminogen activator Pla of Yersinia pestis enhances bacterial attachment to the mammalian extracellular matrix. Infect Immun 1998; 66:5755-62.
    • (1998) Infect Immun , vol.66 , pp. 5755-5762
    • Lähteenmäki, K.1    Virkola, R.2    Sarén, A.3    Emödy, L.4    Korhonen, T.K.5
  • 68
    • 0035943478 scopus 로고    scopus 로고
    • The Pla surface protease/adhesin of Yersinia pestis mediates bacterial invasion into human endothelial cells
    • Lähteenmäki K, Kukkonen M, Korhonen TK. The Pla surface protease/adhesin of Yersinia pestis mediates bacterial invasion into human endothelial cells. FEBS Lett 2001; 504:69-72.
    • (2001) FEBS Lett , vol.504 , pp. 69-72
    • Lähteenmäki, K.1    Kukkonen, M.2    Korhonen, T.K.3
  • 69
    • 42149195366 scopus 로고    scopus 로고
    • Recognition of bacterial surface polysaccharides by lectins of the innate immune system and its contribution to defense against infection: The case of pulmonary pathogens
    • Sahly H, Keisari L, Crouch E, Sharon N, Ofek I. Recognition of bacterial surface polysaccharides by lectins of the innate immune system and its contribution to defense against infection: the case of pulmonary pathogens. Infect Immun 2008; 76:1322-32.
    • (2008) Infect Immun , vol.76 , pp. 1322-1332
    • Sahly, H.1    Keisari, L.2    Crouch, E.3    Sharon, N.4    Ofek, I.5
  • 70
    • 0042838105 scopus 로고    scopus 로고
    • Treatment of Helicobacter pylori infection using novel antiadhesion compound (3' sialyllactose sodium salt). A double blind, placebo-controlled clinical study
    • Parente F, Cucino C, Anderloni A, Grandinetti G, Bianchi Porro G. Treatment of Helicobacter pylori infection using novel antiadhesion compound (3' sialyllactose sodium salt). A double blind, placebo-controlled clinical study. Helicobacter 2003; 8:252-6.
    • (2003) Helicobacter , vol.8 , pp. 252-256
    • Parente, F.1    Cucino, C.2    Anderloni, A.3    Grandinetti, G.4    Bianchi Porro, G.5
  • 71
    • 0034699969 scopus 로고    scopus 로고
    • Treatment of acute otitis media with an antiadhesive oligosaccharide: A randomised, double-blind, placebo-controlled trial
    • Ukkonen P, Varis K, Jernfors M, Herva E, Jokinen J, Ruokokoski D, et al. Treatment of acute otitis media with an antiadhesive oligosaccharide: a randomised, double-blind, placebo-controlled trial. Lancet 2000; 356:1398-402.
    • (2000) Lancet , vol.356 , pp. 1398-1402
    • Ukkonen, P.1    Varis, K.2    Jernfors, M.3    Herva, E.4    Jokinen, J.5    Ruokokoski, D.6
  • 72
    • 0030807607 scopus 로고    scopus 로고
    • Oligosaccharides interfere with the establishment and progression of experimental pneumococcal pneumonia
    • Idänpään-Heikkilä I, Simon PM, Zopf D, Vullo T, Cahill P, Sokol H, et al. Oligosaccharides interfere with the establishment and progression of experimental pneumococcal pneumonia. J Infect Dis 1997; 176:704-12.
    • (1997) J Infect Dis , vol.176 , pp. 704-712
    • Idänpään-Heikkilä, I.1    Simon, P.M.2    Zopf, D.3    Vullo, T.4    Cahill, P.5    Sokol, H.6
  • 73
    • 0033105115 scopus 로고    scopus 로고
    • Inhibition of viral adhesion and infection by sialic-acid-conjugated dendritic polymers
    • Reuter JD, Myc A, Hayes MH, Gan Z, Roy R, Qin D, et al. Inhibition of viral adhesion and infection by sialic-acid-conjugated dendritic polymers. Bioconj Chem 1999; 10:271-8.
    • (1999) Bioconj Chem , vol.10 , pp. 271-278
    • Reuter, J.D.1    Myc, A.2    Hayes, M.H.3    Gan, Z.4    Roy, R.5    Qin, D.6
  • 75
    • 58449083093 scopus 로고    scopus 로고
    • Macrophage uptake, intracellular localization, and degradation of poly-?-D-glutamic acid, the capsular antigen of Bacillus anthracis
    • Sutherland MD, Kozel TR. Macrophage uptake, intracellular localization, and degradation of poly-?-D-glutamic acid, the capsular antigen of Bacillus anthracis. Infect Immun 2009; 77:532-8.
    • (2009) Infect Immun , vol.77 , pp. 532-538
    • Sutherland, M.D.1    Kozel, T.R.2
  • 76
    • 41049113518 scopus 로고    scopus 로고
    • BslA, a pXO1-encoded adhesin of Bacillus anthracis
    • Kern JW, Schneewind O. BslA, a pXO1-encoded adhesin of Bacillus anthracis. Mol Microbiol 2008; 68:504-15.
    • (2008) Mol Microbiol , vol.68 , pp. 504-515
    • Kern, J.W.1    Schneewind, O.2
  • 77
    • 0042265058 scopus 로고    scopus 로고
    • Genome-based bioinformatic selection of chromosomal Bacillus anthracis putative vaccine candidates coupled with proteomic identification of surface-associated antigens
    • Ariel N, Zvi A, Makarova KS, Chitlaru T, Elhanany E, Velan B, et al. Genome-based bioinformatic selection of chromosomal Bacillus anthracis putative vaccine candidates coupled with proteomic identification of surface-associated antigens. Infect Immun 2003; 71:4563-79.
    • (2003) Infect Immun , vol.71 , pp. 4563-4579
    • Ariel, N.1    Zvi, A.2    Makarova, K.S.3    Chitlaru, T.4    Elhanany, E.5    Velan, B.6
  • 78
    • 10644269821 scopus 로고    scopus 로고
    • Identification and biochemical characterization of two novel collagen binding MSCRAMMs of Bacillus anthracis
    • Xu Y, Liang X, Chen Y, Koehler TM, Höök M. Identification and biochemical characterization of two novel collagen binding MSCRAMMs of Bacillus anthracis. J Biol Chem 2004; 279:51760-8.
    • (2004) J Biol Chem , vol.279 , pp. 51760-51768
    • Xu, Y.1    Liang, X.2    Chen, Y.3    Koehler, T.M.4    Höök, M.5
  • 79
    • 39449109358 scopus 로고    scopus 로고
    • The integrin Mac-1 (CR3) mediates internalization and directs Bacillus anthracis spores into professional phagocytes
    • Oliva CR, Swiecki MK, Griguer CE, Lisanby MW, Bullard DC, Turnbough CL, et al. The integrin Mac-1 (CR3) mediates internalization and directs Bacillus anthracis spores into professional phagocytes. PNAS 2008; 105:1261-6.
    • (2008) PNAS , vol.105 , pp. 1261-1266
    • Oliva, C.R.1    Swiecki, M.K.2    Griguer, C.E.3    Lisanby, M.W.4    Bullard, D.C.5    Turnbough, C.L.6
  • 80
    • 46449114418 scopus 로고    scopus 로고
    • Type IV pili in Francisella tularensis: Roles of pilF and pilT in fiber assembly, host cell adherence and virulence
    • Chakraborty S, Monfett M, Maier TM, Benach JL, Frank DW, Thanassi DG. Type IV pili in Francisella tularensis: roles of pilF and pilT in fiber assembly, host cell adherence and virulence. Infect Immun 2008; 76:2852-61.
    • (2008) Infect Immun , vol.76 , pp. 2852-2861
    • Chakraborty, S.1    Monfett, M.2    Maier, T.M.3    Benach, J.L.4    Frank, D.W.5    Thanassi, D.G.6
  • 81
    • 69949155661 scopus 로고    scopus 로고
    • Functional analysis of pilin-like proteins from Francisella tularensis: Complementation of type IV pilus phenotypes in Neisseria gonorrhoeae
    • Salomonsson E, Forsberg A, Roos N, Holz C, Maier B, Koomey M, et al. Functional analysis of pilin-like proteins from Francisella tularensis: complementation of type IV pilus phenotypes in Neisseria gonorrhoeae. Microbiol 2009; 155:2546-59.
    • (2009) Microbiol , vol.155 , pp. 2546-2559
    • Salomonsson, E.1    Forsberg, A.2    Roos, N.3    Holz, C.4    Maier, B.5    Koomey, M.6
  • 82
    • 33748480914 scopus 로고    scopus 로고
    • Identification of a Francisella tularensis LVS outer membrane protein that confers adherence to A549 human lung cells
    • Melillo A, Sledjeski DD, Lipski S, Wooton RM, Basrur V, Lafontaine ER. Identification of a Francisella tularensis LVS outer membrane protein that confers adherence to A549 human lung cells. FEMS Microbiol Lett 2006; 263:102-8.
    • (2006) FEMS Microbiol Lett , vol.263 , pp. 102-108
    • Melillo, A.1    Sledjeski, D.D.2    Lipski, S.3    Wooton, R.M.4    Basrur, V.5    Lafontaine, E.R.6
  • 83
    • 33748079800 scopus 로고    scopus 로고
    • Characterization of the receptor-ligand pathways important for entry and survival of Francisella tularensis in human macrophages
    • Balagopal A, MacFarlane A, Mohapatra N, Soni S, Gunn JS, Schlesinger LS. Characterization of the receptor-ligand pathways important for entry and survival of Francisella tularensis in human macrophages. Infect Immun 2006; 74:5114-25.
    • (2006) Infect Immun , vol.74 , pp. 5114-5125
    • Balagopal, A.1    Macfarlane, A.2    Mohapatra, N.3    Soni, S.4    Gunn, J.S.5    Schlesinger, L.S.6
  • 84
    • 33751501420 scopus 로고    scopus 로고
    • Differential infection of mononuclear phagocytes by Francisella tularensis: Role of the macrophage mannose receptor
    • Schulert GS, Allen LH. Differential infection of mononuclear phagocytes by Francisella tularensis: role of the macrophage mannose receptor. J Leuk Biol 2006; 80:563-71.
    • (2006) J Leuk Biol , vol.80 , pp. 563-571
    • Schulert, G.S.1    Allen, L.H.2
  • 85
    • 33751511700 scopus 로고    scopus 로고
    • Critical role for serum opsonins and complement receptors CR3 (CD11b/ CD18) and CR4 (CD11c/CD18) in phagocytosis of Francisella tularensis by human dendritic cells (DC): Uptake of Francisella leads to activation of immature DC and intracellular survival of the bacteria
    • Ben Nasr A, Haithcoat J, Masterson JE, Gunn JS, Eaves-Pyles T, Klimpel JR. Critical role for serum opsonins and complement receptors CR3 (CD11b/ CD18) and CR4 (CD11c/CD18) in phagocytosis of Francisella tularensis by human dendritic cells (DC): uptake of Francisella leads to activation of immature DC and intracellular survival of the bacteria. J Leuk Biol 2006; 80:774-86.
    • (2006) J Leuk Biol , vol.80 , pp. 774-786
    • Ben Nasr, A.1    Haithcoat, J.2    Masterson, J.E.3    Gunn, J.S.4    Eaves-Pyles, T.5    Klimpel, J.R.6
  • 88
    • 0030013729 scopus 로고    scopus 로고
    • A putative receptor for Venezuelan equine encephalitis virus from mosquito cells
    • Ludwig GV, Kondig JP, Smith JF. A putative receptor for Venezuelan equine encephalitis virus from mosquito cells. J Virol 1996; 70:5592-9.
    • (1996) J Virol , vol.70 , pp. 5592-5599
    • Ludwig, G.V.1    Kondig, J.P.2    Smith, J.F.3
  • 89
    • 0037229326 scopus 로고    scopus 로고
    • Glycosaminoglycan binding properties of natural Venezuelan Equine Encephalitis virus isolates
    • Wang E, Brault AC, Powers AM, Kang W, Weaver SC. Glycosaminoglycan binding properties of natural Venezuelan Equine Encephalitis virus isolates. J Virol 2003; 77:1204-10.
    • (2003) J Virol , vol.77 , pp. 1204-1210
    • Wang, E.1    Brault, A.C.2    Powers, A.M.3    Kang, W.4    Weaver, S.C.5
  • 90
    • 56149087275 scopus 로고    scopus 로고
    • Smallpox inhibitor of complement enzymes (SPICE): Regulation of complement activation on cells and mechanism of its cellular attachment
    • Liszewski MK, Bertram P, Leung MK, Hauhart R, Zhang L, Atkinson JP. Smallpox inhibitor of complement enzymes (SPICE): regulation of complement activation on cells and mechanism of its cellular attachment. J Immunol 2008; 181:4199-207.
    • (2008) J Immunol , vol.181 , pp. 4199-4207
    • Liszewski, M.K.1    Bertram, P.2    Leung, M.K.3    Hauhart, R.4    Zhang, L.5    Atkinson, J.P.6
  • 91
    • 0035854387 scopus 로고    scopus 로고
    • Folate receptor-a is a cofactor for cellular entry by Marburg and Ebola viruses
    • Chan SY, Empig CJ, Welte FJ, Speck RF, Schmaljohn A, Kreisberg JF, et al. Folate receptor-a is a cofactor for cellular entry by Marburg and Ebola viruses. Cell 2001; 106:117-26.
    • (2001) Cell , vol.106 , pp. 117-126
    • Chan, S.Y.1    Empig, C.J.2    Welte, F.J.3    Speck, R.F.4    Schmaljohn, A.5    Kreisberg, J.F.6
  • 92
    • 6344261967 scopus 로고    scopus 로고
    • DC-SIGN and DC-SIGNR interact with the glycoprotein of Marburg virus and the S protein of Severe Acute Respiratory Syndrome coronavirus
    • Marzi A, Gramberg T, Simmons G, Möller P, Rennekamp AJ, Krumbiegel M, et al. DC-SIGN and DC-SIGNR interact with the glycoprotein of Marburg virus and the S protein of Severe Acute Respiratory Syndrome coronavirus. J Virol 2004; 78:12090-5.
    • (2004) J Virol , vol.78 , pp. 12090-12095
    • Marzi, A.1    Gramberg, T.2    Simmons, G.3    Möller, P.4    Rennekamp, A.J.5    Krumbiegel, M.6
  • 93
    • 0036182734 scopus 로고    scopus 로고
    • Role of fraction 1 antigen of Yersinia pestis in inhibition of phagocytosis
    • Du Y, Rosqvist R, Forsberg Å. Role of fraction 1 antigen of Yersinia pestis in inhibition of phagocytosis. Infect Immun 2002; 70:1453-60.
    • (2002) Infect Immun , vol.70 , pp. 1453-1460
    • Du, Y.1    Rosqvist, R.2    Forsberg, A.3
  • 94
    • 33749250405 scopus 로고    scopus 로고
    • The effects of PsaA and F1 on the adhesive and invasive interactions of Yersinia pestis with human respiratory tract epithelial cells
    • Liu F, Chen H, Galván EM, Lasaro MA, Schifferli DM. The effects of PsaA and F1 on the adhesive and invasive interactions of Yersinia pestis with human respiratory tract epithelial cells. Infect Immun 2006; 74:5636-44.
    • (2006) Infect Immun , vol.74 , pp. 5636-5644
    • Liu, F.1    Chen, H.2    Galván, E.M.3    Lasaro, M.A.4    Schifferli, D.M.5
  • 95
    • 33747672691 scopus 로고    scopus 로고
    • Adhesive properties of the purified plasminogen activator Pla of Yersinia pestis
    • Lobo LA. Adhesive properties of the purified plasminogen activator Pla of Yersinia pestis. FEMS Microbiol Lett 2006; 262:158-62.
    • (2006) FEMS Microbiol Lett , vol.262 , pp. 158-162
    • Lobo, L.A.1
  • 96
    • 33847707804 scopus 로고    scopus 로고
    • The Psa fimbriae of Yersinia pestis interact with phosphatidylcholine on alveolar epithelial cells and pulmonary surfactant
    • Galván EM, Chen H, Schifferli DM. The Psa fimbriae of Yersinia pestis interact with phosphatidylcholine on alveolar epithelial cells and pulmonary surfactant. Infect Immun 2007; 75:1272-9.
    • (2007) Infect Immun , vol.75 , pp. 1272-1279
    • Galván, E.M.1    Chen, H.2    Schifferli, D.M.3
  • 98
    • 0142091765 scopus 로고    scopus 로고
    • PH 6 antigen of Yersinia pestis interacts with plasma lipoproteins and cell membranes
    • Makoveichuk E, Cherepanov P, Lundberg S, Forsberg A, Olivecrona G. pH 6 antigen of Yersinia pestis interacts with plasma lipoproteins and cell membranes. J Lipid Res 2003; 44:320-30.
    • (2003) J Lipid Res , vol.44 , pp. 320-330
    • Makoveichuk, E.1    Cherepanov, P.2    Lundberg, S.3    Forsberg, A.4    Olivecrona, G.5
  • 100
    • 60549117099 scopus 로고    scopus 로고
    • The Yersinia pestis Ail protein mediates binding and Yop delivery to host cells required for plague virulence
    • Felek S, Krukonis ES. The Yersinia pestis Ail protein mediates binding and Yop delivery to host cells required for plague virulence. Infect Immun 2009; 77:825-36.
    • (2009) Infect Immun , vol.77 , pp. 825-836
    • Felek, S.1    Krukonis, E.S.2
  • 101
    • 42949155298 scopus 로고    scopus 로고
    • Human dendritic cell-specific intercellular adhesion molecule- grabbing nonintegrin (CD209) is a receptor for Yersinia pestis that promotes phagocytosis by dendritic cells
    • Zhang P, Skurnik M, Zhang S-S, Schwartz O, Kalyanasundaram R, Bulgheresi S, et al. Human dendritic cell-specific intercellular adhesion molecule- grabbing nonintegrin (CD209) is a receptor for Yersinia pestis that promotes phagocytosis by dendritic cells. Infect Immun 2008; 76:2070-9.
    • (2008) Infect Immun , vol.76 , pp. 2070-2079
    • Zhang, P.1    Skurnik, M.2    Zhang, S.-S.3    Schwartz, O.4    Kalyanasundaram, R.5    Bulgheresi, S.6
  • 102
    • 48449098069 scopus 로고    scopus 로고
    • The Yersinia pestis autotransporter YapC mediates host cell binding, autoaggregation and biofilm formation
    • Felek S, Lawrenz MB, Krukonis ES. The Yersinia pestis autotransporter YapC mediates host cell binding, autoaggregation and biofilm formation. Microbiol 2008; 154:1802-12.
    • (2008) Microbiol , vol.154 , pp. 1802-1812
    • Felek, S.1    Lawrenz, M.B.2    Krukonis, E.S.3
  • 103
    • 58449124478 scopus 로고    scopus 로고
    • A novel Autotransporter adhesin is required for efficient colonization during bubonic plague
    • Lawrenz MB, Lenz JD, Miller VL. A novel Autotransporter adhesin is required for efficient colonization during bubonic plague. Infect Immun 2009; 77:317-26.
    • (2009) Infect Immun , vol.77 , pp. 317-326
    • Lawrenz, M.B.1    Lenz, J.D.2    Miller, V.L.3
  • 104
    • 0033758854 scopus 로고    scopus 로고
    • Nonspecific adherence by Actinobacillus actinomycetemcomitans requires genes widespread in Bacteria and Archaea
    • Kachlany SC, Planet PJ, Bhattacharjee MK, Kollia E, DeSalle R, Fine DH, et al. Nonspecific adherence by Actinobacillus actinomycetemcomitans requires genes widespread in Bacteria and Archaea. J Bacteriol 2000; 182:6169-76.
    • (2000) J Bacteriol , vol.182 , pp. 6169-6176
    • Kachlany, S.C.1    Planet, P.J.2    Bhattacharjee, M.K.3    Kollia, E.4    Desalle, R.5    Fine, D.H.6
  • 105
    • 0036791036 scopus 로고    scopus 로고
    • HecA, a member of a class of adhesins produced by diverse pathogenic bacteria, contributes to the attachment, aggregation, epidermal cell killing, and virulence phenotypes of Erwinia chrysanthemi EC16 on Nicotiana clevelandii seedlings
    • Rojas CM, Ham JH, Deng W-L, Doyle JJ, Colimer A. HecA, a member of a class of adhesins produced by diverse pathogenic bacteria, contributes to the attachment, aggregation, epidermal cell killing, and virulence phenotypes of Erwinia chrysanthemi EC16 on Nicotiana clevelandii seedlings. PNAS 2002; 99:13142-7.
    • (2002) PNAS , vol.99 , pp. 13142-13147
    • Rojas, C.M.1    Ham, J.H.2    Deng, W.-L.3    Doyle, J.J.4    Colimer, A.5
  • 106
    • 0031663156 scopus 로고    scopus 로고
    • Ganglioside GT1b as a complementary receptor component for Clostridium botulinum neurotoxins
    • Kozaki S, Kamata Y, Watarai S, Nishiki T, Mochida S. Ganglioside GT1b as a complementary receptor component for Clostridium botulinum neurotoxins. Microb Pathog 1998; 25:91-9.
    • (1998) Microb Pathog , vol.25 , pp. 91-99
    • Kozaki, S.1    Kamata, Y.2    Watarai, S.3    Nishiki, T.4    Mochida, S.5
  • 107
    • 0018867612 scopus 로고
    • Interaction between Clostridium botulinum neurotoxin and gangliosides
    • Kitamura M, Iwamori M, Nagai Y. Interaction between Clostridium botulinum neurotoxin and gangliosides. Biochim Biophys Acta 1980; 628:328-35.
    • (1980) Biochim Biophys Acta , vol.628 , pp. 328-335
    • Kitamura, M.1    Iwamori, M.2    Nagai, Y.3
  • 108
    • 0022547513 scopus 로고
    • TLC immunostaining characterization of Clostridium botulinum type A neurotoxin binding to gangliosides and free fatty acids
    • Takamizawa K, Iwamori M, Kozaki S, Sakaguchi G, Tanaka R, Takayama H, et al. TLC immunostaining characterization of Clostridium botulinum type A neurotoxin binding to gangliosides and free fatty acids. FEBS Lett 1986; 201:229-32.
    • (1986) FEBS Lett , vol.201 , pp. 229-232
    • Takamizawa, K.1    Iwamori, M.2    Kozaki, S.3    Sakaguchi, G.4    Tanaka, R.5    Takayama, H.6
  • 109
    • 0037031826 scopus 로고    scopus 로고
    • Botulinum neurotoxin A activity is dependent upon the presence of specific gangliosides in neuroblastoma cells expressing synaptotagmin I
    • Yowler BC, Kensinger RD, Schengrund CL. Botulinum neurotoxin A activity is dependent upon the presence of specific gangliosides in neuroblastoma cells expressing synaptotagmin I. J Biol Chem 2002; 277:32815-9.
    • (2002) J Biol Chem , vol.277 , pp. 32815-32819
    • Yowler, B.C.1    Kensinger, R.D.2    Schengrund, C.L.3
  • 110
    • 0022648666 scopus 로고
    • Binding of Clostridium botulinum neurotoxin to gangliosides
    • Ochanda JO, Syuto B, Ohishi J, Naiki M, Kubo S. Binding of Clostridium botulinum neurotoxin to gangliosides. J Biochem 1986; 100:27-33.
    • (1986) J Biochem , vol.100 , pp. 27-33
    • Ochanda, J.O.1    Syuto, B.2    Ohishi, J.3    Naiki, M.4    Kubo, S.5
  • 111
    • 27444433349 scopus 로고    scopus 로고
    • Binding of Clostridium botulinum type C and D neurotoxins to ganglioside and phospholipid. Novel insights into the receptor for clostridial neurotoxins
    • Tsukamoto K, Kohda T, Mukamoto M, Takeuchi K, Ihara H, Saito M, et al. Binding of Clostridium botulinum type C and D neurotoxins to ganglioside and phospholipid. Novel insights into the receptor for clostridial neurotoxins. J Biol Chem 2005; 280:35164-71.
    • (2005) J Biol Chem , vol.280 , pp. 35164-35171
    • Tsukamoto, K.1    Kohda, T.2    Mukamoto, M.3    Takeuchi, K.4    Ihara, H.5    Saito, M.6
  • 112
    • 0023008947 scopus 로고
    • Evidence for direct binding of Clostridium botulinum type E derivative toxin and its fragments to gangliosides and free fatty acids
    • Kamata Y, Kozaki S, Sakaguchi G, Iwamori M, Nagai Y. Evidence for direct binding of Clostridium botulinum type E derivative toxin and its fragments to gangliosides and free fatty acids. Biochem Biophys Res Commun 1986; 140:1015-9.
    • (1986) Biochem Biophys Res Commun , vol.140 , pp. 1015-1019
    • Kamata, Y.1    Kozaki, S.2    Sakaguchi, G.3    Iwamori, M.4    Nagai, Y.5
  • 113
    • 3142735021 scopus 로고    scopus 로고
    • Synaptotagmins I and II act as nerve cell receptors for botulinum neurotoxin G
    • Rummel A, Karnath T, Henke T, Bigalke H, Binz T. Synaptotagmins I and II act as nerve cell receptors for botulinum neurotoxin G. J Biol Chem 2004; 279:30865-70.
    • (2004) J Biol Chem , vol.279 , pp. 30865-30870
    • Rummel, A.1    Karnath, T.2    Henke, T.3    Bigalke, H.4    Binz, T.5
  • 114
    • 0029034518 scopus 로고
    • Digalactosylceramide is the receptor for staphylococcal enterotoxin- B in human kidney proximal tubular cells
    • Chatterjee S, Khullar M, Shi WY. Digalactosylceramide is the receptor for staphylococcal enterotoxin- B in human kidney proximal tubular cells. Glycobiology 1995; 5:327-33.
    • (1995) Glycobiology , vol.5 , pp. 327-333
    • Chatterjee, S.1    Khullar, M.2    Shi, W.Y.3
  • 116
    • 38449083835 scopus 로고    scopus 로고
    • Systematic comparison of oligosaccharide specificity of Ricinus communis agglutinin I and Erythrina lectins: A search by frontal affinity chromatography
    • Itakura Y, Nakamura-Tsuruta S, Kominami J, Sharon N, Kasai K, Hirabayashi J. Systematic comparison of oligosaccharide specificity of Ricinus communis agglutinin I and Erythrina lectins: a search by frontal affinity chromatography. J Biochem 2007; 142:459.
    • (2007) J Biochem , vol.142 , pp. 459
    • Itakura, Y.1    Nakamura-Tsuruta, S.2    Kominami, J.3    Sharon, N.4    Kasai, K.5    Hirabayashi, J.6
  • 117
    • 43849089490 scopus 로고    scopus 로고
    • Multivalent binding of ricin to bovine serum albumin-based neoglycoconjugates
    • Blome MC, Schengrund CL. Multivalent binding of ricin to bovine serum albumin-based neoglycoconjugates. Toxicon 2008; 51:1214-24.
    • (2008) Toxicon , vol.51 , pp. 1214-1224
    • Blome, M.C.1    Schengrund, C.L.2
  • 119
    • 0036042515 scopus 로고    scopus 로고
    • A collagen-like surface glycoprotein is a structural component of the Bacillus anthracis exosporium
    • Sylvestre P, Coutre-Tosi E, Mock M. A collagen-like surface glycoprotein is a structural component of the Bacillus anthracis exosporium. Mol Microbiol 2002; 45:169-78.
    • (2002) Mol Microbiol , vol.45 , pp. 169-178
    • Sylvestre, P.1    Coutre-Tosi, E.2    Mock, M.3
  • 120
    • 0038054122 scopus 로고    scopus 로고
    • Carbohydrates and glycoproteins of Bacillus anthracis and related bacilli: Targets for biodetection
    • Fox A, Stewart GC, Waller LN, Fox KF, Harley WM, Price RL. Carbohydrates and glycoproteins of Bacillus anthracis and related bacilli: targets for biodetection. J Microbiol Methods 2003; 54:143-52.
    • (2003) J Microbiol Methods , vol.54 , pp. 143-152
    • Fox, A.1    Stewart, G.C.2    Waller, L.N.3    Fox, K.F.4    Harley, W.M.5    Price, R.L.6
  • 121
    • 2642549692 scopus 로고    scopus 로고
    • Ruthenium red staining for ultrastructural visualization of a glycoprotein layer surrounding the spore of Bacillus anthracis and Bacillus subtilis
    • Waller LN, Fox N, Fox KF, Fox A, Price RL. Ruthenium red staining for ultrastructural visualization of a glycoprotein layer surrounding the spore of Bacillus anthracis and Bacillus subtilis. J Microbiol Methods 2004; 58:23-30.
    • (2004) J Microbiol Methods , vol.58 , pp. 23-30
    • Waller, L.N.1    Fox, N.2    Fox, K.F.3    Fox, A.4    Price, R.L.5
  • 122
    • 23844550737 scopus 로고    scopus 로고
    • Mannose-binding lectin binds to Ebola and Marburg envelope glycoproteins, resulting in blocking of virus interaction with DC-SIGN and complement-mediated virus neutralization
    • Ji X, Olinger GG, Aris S, Chen Y, Gewurz H, Spear GT. Mannose-binding lectin binds to Ebola and Marburg envelope glycoproteins, resulting in blocking of virus interaction with DC-SIGN and complement-mediated virus neutralization. J Gen Virol 2005; 86:2535-42.
    • (2005) J Gen Virol , vol.86 , pp. 2535-2542
    • Ji, X.1    Olinger, G.G.2    Aris, S.3    Chen, Y.4    Gewurz, H.5    Spear, G.T.6
  • 123
    • 0344011988 scopus 로고    scopus 로고
    • Mannosyl glycodendritic structure inhibits DC-SIGN-mediated Ebola virus infection in cis and in trans
    • Lasala F, Arce E, Otero JR, Rojo J, Delgado R. Mannosyl glycodendritic structure inhibits DC-SIGN-mediated Ebola virus infection in cis and in trans. Antimicrob Ag Chemother 2003; 47:3970-2.
    • (2003) Antimicrob Ag Chemother , vol.47 , pp. 3970-3972
    • Lasala, F.1    Arce, E.2    Otero, J.R.3    Rojo, J.4    Delgado, R.5
  • 125
    • 33947236208 scopus 로고    scopus 로고
    • Structural modification of a base disaccharide alters antiadhesion properties towards Yersinia pestis
    • Thomas RJ, Hacking A, Brooks TJG. Structural modification of a base disaccharide alters antiadhesion properties towards Yersinia pestis. FEMS Immunol Med Microbiol 2007; 49:410-4.
    • (2007) FEMS Immunol Med Microbiol , vol.49 , pp. 410-414
    • Thomas, R.J.1    Hacking, A.2    Brooks, T.J.G.3
  • 126
    • 4444348990 scopus 로고    scopus 로고
    • The interaction of Pseudomonas aeruginosa PAK with human and animal respiratory cell lines
    • Hambrook J, Titball R, Lindsay C. The interaction of Pseudomonas aeruginosa PAK with human and animal respiratory cell lines. FEMS Microbiol Lett 2004; 238:49-55.
    • (2004) FEMS Microbiol Lett , vol.238 , pp. 49-55
    • Hambrook, J.1    Titball, R.2    Lindsay, C.3
  • 127
    • 9244230605 scopus 로고    scopus 로고
    • The pH 6 antigen is an antiphagocytic factor produced by Yersinia pestis independent of Yersinia outer proteins and capsule antigen
    • Huang X-Z, Lindler LE. The pH 6 antigen is an antiphagocytic factor produced by Yersinia pestis independent of Yersinia outer proteins and capsule antigen. Infect Immun 2004; 72:7212-9.
    • (2004) Infect Immun , vol.72 , pp. 7212-7219
    • Huang, X.-Z.1    Lindler, L.E.2
  • 128
    • 0036156103 scopus 로고    scopus 로고
    • Adherence of Burkholderia pseudomallei cells to cultured human epithelial cell lines is regulated by growth temperature
    • Brown NF, Boddey JA, Flegg CA, Beacham IR. Adherence of Burkholderia pseudomallei cells to cultured human epithelial cell lines is regulated by growth temperature. Infect Immun 2002; 70:974-80.
    • (2002) Infect Immun , vol.70 , pp. 974-980
    • Brown, N.F.1    Boddey, J.A.2    Flegg, C.A.3    Beacham, I.R.4
  • 129
    • 0032898814 scopus 로고    scopus 로고
    • Attachment of Burkholderia pseudomallei to pharyngeal epithelial cells: A highly pathogenic bacteria with low attachment ability
    • Ahmed K, Encisco HDR, Masaki H, Tao M, Omori A, Tharavichikul P, et al. Attachment of Burkholderia pseudomallei to pharyngeal epithelial cells: a highly pathogenic bacteria with low attachment ability. Am J Trop Med Hyg 1999; 60:90-3.
    • (1999) Am J Trop Med Hyg , vol.60 , pp. 90-93
    • Ahmed, K.1    Encisco, H.D.R.2    Masaki, H.3    Tao, M.4    Omori, A.5    Tharavichikul, P.6
  • 130
    • 19944433259 scopus 로고    scopus 로고
    • A type IV pilin, PilA, contributes to adherence of Burkholderia pseudomallei and virulence in vivo
    • Essex-Lopresti AE, Boddey JA, Thomas R, Smith MP, Hartley MG, Atkins T, et al. A type IV pilin, PilA, contributes to adherence of Burkholderia pseudomallei and virulence in vivo. Infect Immun 2005; 73:1260-4.
    • (2005) Infect Immun , vol.73 , pp. 1260-1264
    • Essex-Lopresti, A.E.1    Boddey, J.A.2    Thomas, R.3    Smith, M.P.4    Hartley, M.G.5    Atkins, T.6
  • 131
    • 33748068125 scopus 로고    scopus 로고
    • Temperature-regulated microcolony formation by Burkholderia pseudomallei requires pilA and enhances association with cultured human cells
    • Boddey JA, Flegg CA, Day CJ, Beacham IR, Peak IR. Temperature-regulated microcolony formation by Burkholderia pseudomallei requires pilA and enhances association with cultured human cells. Infect Immun 2006; 74:5374-81.
    • (2006) Infect Immun , vol.74 , pp. 5374-5381
    • Boddey, J.A.1    Flegg, C.A.2    Day, C.J.3    Beacham, I.R.4    Peak, I.R.5
  • 132
    • 0021324093 scopus 로고
    • Inhibitory effect of Ganglioside GT1b on the activities of Clostridium botulinum toxins
    • Kozaki S, Sakaguchi G, Nishimura M, Iwamori M, Nagai Y. Inhibitory effect of Ganglioside GT1b on the activities of Clostridium botulinum toxins. FEMS Microbiol Lett 1984; 212:219-23.
    • (1984) FEMS Microbiol Lett , vol.212 , pp. 219-223
    • Kozaki, S.1    Sakaguchi, G.2    Nishimura, M.3    Iwamori, M.4    Nagai, Y.5
  • 133
    • 0026354658 scopus 로고
    • An immunotoxin prepared with blocked ricin: A natural plant toxin adapted for therapeutic use
    • Lambert JM, Goldmacher VS, Collinson AR, Nadler LM, Blattler WA. An immunotoxin prepared with blocked ricin: a natural plant toxin adapted for therapeutic use. Cancer Res 1991; 51:6236-42.
    • (1991) Cancer Res , vol.51 , pp. 6236-6242
    • Lambert, J.M.1    Goldmacher, V.S.2    Collinson, A.R.3    Nadler, L.M.4    Blattler, W.A.5
  • 136
    • 33748359338 scopus 로고    scopus 로고
    • Binding diversity of the two binding sites of ricin B lectin
    • Ganguly D, Mukhopadhyay C. Binding diversity of the two binding sites of ricin B lectin. Biopolymers 2006; 83:83-94.
    • (2006) Biopolymers , vol.83 , pp. 83-94
    • Ganguly, D.1    Mukhopadhyay, C.2
  • 137
    • 34447568526 scopus 로고    scopus 로고
    • Extended binding site of ricin B lectin for oligosaccharide recognition
    • Ganguly D, Mukhopadhyay C. Extended binding site of ricin B lectin for oligosaccharide recognition. Biopolymers 2007; 86:311-20.
    • (2007) Biopolymers , vol.86 , pp. 311-320
    • Ganguly, D.1    Mukhopadhyay, C.2
  • 138
    • 33745602817 scopus 로고    scopus 로고
    • Monovalent and polyvalent carbohydrate inhibitors of ricin binding to a model of the cell surface receptor
    • Dawson RM, Alderton MR, Wells D, Hartley PG. Monovalent and polyvalent carbohydrate inhibitors of ricin binding to a model of the cell surface receptor. J Appl Toxicol 2006; 26:247-52.
    • (2006) J Appl Toxicol , vol.26 , pp. 247-252
    • Dawson, R.M.1    Alderton, M.R.2    Wells, D.3    Hartley, P.G.4
  • 139
    • 0026771208 scopus 로고
    • Glycosphingolipids: The putative receptor for Staphylococcus aureus enterotoxin-B in human kidney proximal tubular cells
    • Chatterjee S, Jett M. Glycosphingolipids: the putative receptor for Staphylococcus aureus enterotoxin-B in human kidney proximal tubular cells. Mol Cell Biochem 1992; 113:25-31.
    • (1992) Mol Cell Biochem , vol.113 , pp. 25-31
    • Chatterjee, S.1    Jett, M.2
  • 140
    • 0029022638 scopus 로고
    • Binding of bacterial toxins to glycoproteins in the envelopes of rainbow trout eggs
    • Kudo S, Yazawa S. Binding of bacterial toxins to glycoproteins in the envelopes of rainbow trout eggs. Histochem J 1995; 27:300-8.
    • (1995) Histochem J , vol.27 , pp. 300-308
    • Kudo, S.1    Yazawa, S.2
  • 141
    • 0031824605 scopus 로고    scopus 로고
    • Inhibition of the type 1 fimbriae-mediated adhesion of Escherichia coli to erythrocytes by multiantennary a-mannosyl clusters: The effect of multivalency
    • Lindhorst TK, Kieburg C, Krallmann-Wenzel U. Inhibition of the type 1 fimbriae-mediated adhesion of Escherichia coli to erythrocytes by multiantennary a-mannosyl clusters: the effect of multivalency. Glycoconj J 1998; 15:605-13.
    • (1998) Glycoconj J , vol.15 , pp. 605-613
    • Lindhorst, T.K.1    Kieburg, C.2    Krallmann-Wenzel, U.3
  • 142
    • 0034628502 scopus 로고    scopus 로고
    • Shiga-like toxins are neutralized by tailored multivalent carbohydrate ligands
    • Kitov PI, Sadowska JM, Mulvey G, Armstrong GD, Ling H, Pannu NS, et al. Shiga-like toxins are neutralized by tailored multivalent carbohydrate ligands. Nature 2000; 403:669-72.
    • (2000) Nature , vol.403 , pp. 669-672
    • Kitov, P.I.1    Sadowska, J.M.2    Mulvey, G.3    Armstrong, G.D.4    Ling, H.5    Pannu, N.S.6
  • 143
    • 0346787607 scopus 로고    scopus 로고
    • Adhesion inhibition of F1C-fimbriated Escherichia coli and Pseudomonas aeruginosa PAK and PAO by multivalent carbohydrate ligands
    • Autar R, Salam Khan A, Schad M, Hacker J, Liskamp RMJ, Pieters RJ. Adhesion inhibition of F1C-fimbriated Escherichia coli and Pseudomonas aeruginosa PAK and PAO by multivalent carbohydrate ligands. Chem Bio Chem 2003; 4:1317-25.
    • (2003) Chem Bio Chem , vol.4 , pp. 1317-1325
    • Autar, R.1    Salam Khan, A.2    Schad, M.3    Hacker, J.4    Liskamp, R.M.J.5    Pieters, R.J.6
  • 146
    • 0029090119 scopus 로고
    • Sulfated polyanions block Chlamydia trachomatis infection of cervix-derived human epithelia
    • Zaretsky FR, Pearce-Pratt R, Phillips DM. Sulfated polyanions block Chlamydia trachomatis infection of cervix-derived human epithelia. Infect Immun 1995; 63:3520-6.
    • (1995) Infect Immun , vol.63 , pp. 3520-3526
    • Zaretsky, F.R.1    Pearce-Pratt, R.2    Phillips, D.M.3
  • 147
    • 0034055692 scopus 로고    scopus 로고
    • Contribution of the hydrophobic effect to microbial infection
    • Doyle RJ. Contribution of the hydrophobic effect to microbial infection. Microb Infect 2002; 2:391-400.
    • (2002) Microb Infect , vol.2 , pp. 391-400
    • Doyle, R.J.1
  • 148
    • 0022611522 scopus 로고
    • Inhibitory effect of substituted aromatic hydrocarbons on adherence of Escherichia coli to human epithelial cells
    • Falkowski W, Edwards M, Schaeffer AJ. Inhibitory effect of substituted aromatic hydrocarbons on adherence of Escherichia coli to human epithelial cells. Infect Immun 1986; 52:863-6.
    • (1986) Infect Immun , vol.52 , pp. 863-866
    • Falkowski, W.1    Edwards, M.2    Schaeffer, A.J.3
  • 150
    • 34447530882 scopus 로고    scopus 로고
    • Bioactive compounds in cranberries and their role in prevention of urinary tract infections
    • Howell AB. Bioactive compounds in cranberries and their role in prevention of urinary tract infections. Mol Nutr Food Res 2007; 51:732-7.
    • (2007) Mol Nutr Food Res , vol.51 , pp. 732-737
    • Howell, A.B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.