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Volumn 68, Issue 6, 2000, Pages 3377-3384

Adhesion of Aspergillus species to extracellular matrix proteins: Evidence for involvement of negatively charged carbohydrates on the conidial surface

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; ASPERGILLOSIS; ASPERGILLUS FUMIGATUS; BASEMENT MEMBRANE; BINDING AFFINITY; CARBOHYDRATE ANALYSIS; EXTRACELLULAR MATRIX; HUMAN; HUMAN CELL; MOLECULAR INTERACTION; PRIORITY JOURNAL; SURFACE PROPERTY;

EID: 0034034902     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/IAI.68.6.3377-3384.2000     Document Type: Article
Times cited : (92)

References (49)
  • 1
    • 0025900908 scopus 로고
    • Localization of the major heparin-binding site in fibronectin
    • Barkalow, F. J., and J. E. Schwarzbauer. 1991. Localization of the major heparin-binding site in fibronectin. J. Biol. Chem. 266:7812-7818.
    • (1991) J. Biol. Chem. , vol.266 , pp. 7812-7818
    • Barkalow, F.J.1    Schwarzbauer, J.E.2
  • 2
    • 0343318483 scopus 로고
    • Fluctuations saisonnières des spores d'Aspergillus dans l'air à Bruxelles en 1982
    • Beguin, H., N. Nolard-Tintigner, and B. Claus. 1985. Fluctuations saisonnières des spores d'Aspergillus dans l'air à Bruxelles en 1982. Bull. Soc. Fr. Mycol. Méd. 14:195-200.
    • (1985) Bull. Soc. Fr. Mycol. Méd. , vol.14 , pp. 195-200
    • Beguin, H.1    Nolard-Tintigner, N.2    Claus, B.3
  • 3
    • 0027496555 scopus 로고
    • Distinct mechanisms of epithelial adhesion for Candida albicans and Candida tropicalis. Identification of the participating ligands and development of inhibitory peptides
    • Bendel, C. M., and M. K. Hostetter. 1993. Distinct mechanisms of epithelial adhesion for Candida albicans and Candida tropicalis. Identification of the participating ligands and development of inhibitory peptides. J. Clin. Investig. 92:1840-1849.
    • (1993) J. Clin. Investig. , vol.92 , pp. 1840-1849
    • Bendel, C.M.1    Hostetter, M.K.2
  • 7
    • 0028511746 scopus 로고
    • Mechanisms and implications of the adhesion phenomenon in Aspergillus fumigatus
    • Paris
    • Bouchara, J. P., G. Tronchin, and D. Chabasse. 1994. Mechanisms and implications of the adhesion phenomenon in Aspergillus fumigatus. Pathol. Biol. (Paris) 42:640-646.
    • (1994) Pathol. Biol. , vol.42 , pp. 640-646
    • Bouchara, J.P.1    Tronchin, G.2    Chabasse, D.3
  • 9
    • 0029825546 scopus 로고    scopus 로고
    • Binding of Aspergillus fumigatus spores to lung epithelial cells and basement membrane proteins: Relevance to the asthmatic lung
    • Bromley, I. M., and K. Donaldson. 1996. Binding of Aspergillus fumigatus spores to lung epithelial cells and basement membrane proteins: relevance to the asthmatic lung. Thorax 51:1203-1209.
    • (1996) Thorax , vol.51 , pp. 1203-1209
    • Bromley, I.M.1    Donaldson, K.2
  • 10
    • 0029120352 scopus 로고
    • Heparin binding by fibronectin module III-13 involves six discontinuous basic residues brought together to form a cationic cradle
    • Busby, T. F., W. S. Argraves, S. A. Brew, I. Pechik, G. L. Gilliland, and K. C. Ingham. 1995. Heparin binding by fibronectin module III-13 involves six discontinuous basic residues brought together to form a cationic cradle. J. Biol. Chem. 270:18558-18562.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18558-18562
    • Busby, T.F.1    Argraves, W.S.2    Brew, S.A.3    Pechik, I.4    Gilliland, G.L.5    Ingham, K.C.6
  • 11
    • 0020264236 scopus 로고
    • Fibronectin and fibrin provide a provisional matrix for epidermal cell migration during wound reepithelialization
    • Clark, R. A. F., J. M. Lanigan, P. DellaPelle, E. Manseau, H. F. Dvorak, and R. B. Colvin. 1982. Fibronectin and fibrin provide a provisional matrix for epidermal cell migration during wound reepithelialization. J. Investig. Dermatol. 79:264-269.
    • (1982) J. Investig. Dermatol. , vol.79 , pp. 264-269
    • Clark, R.A.F.1    Lanigan, J.M.2    Dellapelle, P.3    Manseau, E.4    Dvorak, H.F.5    Colvin, R.B.6
  • 12
    • 0031893513 scopus 로고    scopus 로고
    • Invasive aspergillosis
    • Denning, D. W. 1998. Invasive aspergillosis. Clin. Infect. Dis. 26:781-803.
    • (1998) Clin. Infect. Dis. , vol.26 , pp. 781-803
    • Denning, D.W.1
  • 13
    • 0029811772 scopus 로고    scopus 로고
    • Therapeutic outcome in invasive aspergillosis
    • Denning, D. W. 1996. Therapeutic outcome in invasive aspergillosis. Clin. Infect. Dis. 23:608-615.
    • (1996) Clin. Infect. Dis. , vol.23 , pp. 608-615
    • Denning, D.W.1
  • 15
    • 0030041083 scopus 로고    scopus 로고
    • Extracellular matrix biology in the lung
    • Dunsmore, S. E., and D. E. Rannels. 1996. Extracellular matrix biology in the lung. Am. J. Physiol. 270:L3-L27.
    • (1996) Am. J. Physiol. , vol.270
    • Dunsmore, S.E.1    Rannels, D.E.2
  • 16
    • 0030790687 scopus 로고    scopus 로고
    • Common themes in microbial pathogenicity revisited
    • Finlay, B. B., and S. Falkow. 1997. Common themes in microbial pathogenicity revisited. Microbiol. Mol. Biol. Rev. 61:136-169.
    • (1997) Microbiol. Mol. Biol. Rev. , vol.61 , pp. 136-169
    • Finlay, B.B.1    Falkow, S.2
  • 18
    • 0023157625 scopus 로고
    • Primary structure of human plasma fibronectin. Characterization of a 38 kDa domain containing the C-terminal heparin-binding site (Hep III site) and a region of molecular heterogeneity
    • Garcia-Pardo, A., A. Rostagno, and B. Frangione. 1987. Primary structure of human plasma fibronectin. Characterization of a 38 kDa domain containing the C-terminal heparin-binding site (Hep III site) and a region of molecular heterogeneity. Biochem. J. 241:923-928.
    • (1987) Biochem. J. , vol.241 , pp. 923-928
    • Garcia-Pardo, A.1    Rostagno, A.2    Frangione, B.3
  • 21
    • 0032831831 scopus 로고    scopus 로고
    • Recognition of fibronectin by Penicillium marneffei conidia via a sialic acid-dependent process and its relationship to the interaction between conidia and laminin
    • Hamilton, A. J., L. Jeavons, S. Youngchim, and N. Vanittanakom. 1999. Recognition of fibronectin by Penicillium marneffei conidia via a sialic acid-dependent process and its relationship to the interaction between conidia and laminin. Infect. Immun. 67:5200-5205.
    • (1999) Infect. Immun. , vol.67 , pp. 5200-5205
    • Hamilton, A.J.1    Jeavons, L.2    Youngchim, S.3    Vanittanakom, N.4
  • 22
    • 0031741807 scopus 로고    scopus 로고
    • Sialic acid-dependent recognition of laminin by Penicillium mameffei conidia
    • Hamilton, A. J., L. Jeavons, S. Youngchim, N. Vanittanakom, and R. J. Hay. 1998. Sialic acid-dependent recognition of laminin by Penicillium mameffei conidia. Infect. Immun. 66:6024-6026.
    • (1998) Infect. Immun. , vol.66 , pp. 6024-6026
    • Hamilton, A.J.1    Jeavons, L.2    Youngchim, S.3    Vanittanakom, N.4    Hay, R.J.5
  • 23
    • 0028296969 scopus 로고
    • Chemical and immunological analysis of the Aspergillus fumigatus cell wall
    • Hearn, V. M., and J. H. Sietsma. 1994. Chemical and immunological analysis of the Aspergillus fumigatus cell wall. Microbiology 140:789-795.
    • (1994) Microbiology , vol.140 , pp. 789-795
    • Hearn, V.M.1    Sietsma, J.H.2
  • 24
    • 0029894343 scopus 로고    scopus 로고
    • An integrin-like protein in Candida albicans: Implications for pathogenesis
    • Hostetter, M. K. 1996. An integrin-like protein in Candida albicans: implications for pathogenesis. Trends Microbiol. 4:242-246.
    • (1996) Trends Microbiol. , vol.4 , pp. 242-246
    • Hostetter, M.K.1
  • 25
    • 0343318479 scopus 로고
    • Structure of fibronectins
    • A. Rich (ed.), Springer-Verlag, New York, N.Y.
    • Hynes, R. 1990. Structure of fibronectins, p. 113-175. In A. Rich (ed.), Fibronectins. Springer-Verlag, New York, N.Y.
    • (1990) Fibronectins , pp. 113-175
    • Hynes, R.1
  • 26
    • 0025597040 scopus 로고
    • Interaction of heparin with fibronectin and isolated fibronectin domains
    • Ingham, K. C., S. A. Brew, and D. H. Atha. 1990. Interaction of heparin with fibronectin and isolated fibronectin domains. Biochem. J. 272:605-611.
    • (1990) Biochem. J. , vol.272 , pp. 605-611
    • Ingham, K.C.1    Brew, S.A.2    Atha, D.H.3
  • 27
    • 0022978024 scopus 로고
    • A quantitative in vitro assay of polymorphonuclear leukocyte migration through human amnion membrane utilizing 111in-oxine
    • McLaughlin, M. E., R. Kao, I. E. Liener, and J. R. Hoidal. 1971. A quantitative in vitro assay of polymorphonuclear leukocyte migration through human amnion membrane utilizing 111in-oxine. J. Immunol. Methods 95:89-98.
    • (1971) J. Immunol. Methods , vol.95 , pp. 89-98
    • McLaughlin, M.E.1    Kao, R.2    Liener, I.E.3    Hoidal, J.R.4
  • 29
    • 0021886328 scopus 로고
    • Binding of heparin fractions and other polysulfated polysaccharides to plasma fibronectin: Effects of molecular size and degree of sulfation of polysaccharides
    • Ogamo, A., A. Nagai, and K. Nagasawa. 1985. Binding of heparin fractions and other polysulfated polysaccharides to plasma fibronectin: effects of molecular size and degree of sulfation of polysaccharides. Biochim. Biophys. Acta 841:30-41.
    • (1985) Biochim. Biophys. Acta , vol.841 , pp. 30-41
    • Ogamo, A.1    Nagai, A.2    Nagasawa, K.3
  • 31
    • 9244221612 scopus 로고    scopus 로고
    • Binding of human fibronectin to Aspergillus fumigatus conidia
    • Peñalver, M. C., J. E. O'Connor, J. P. Martinez, and M. L. Gil. 1996. Binding of human fibronectin to Aspergillus fumigatus conidia. Infect. Immun. 64: 1146-1153.
    • (1996) Infect. Immun. , vol.64 , pp. 1146-1153
    • Peñalver, M.C.1    O'Connor, J.E.2    Martinez, J.P.3    Gil, M.L.4
  • 32
    • 0019848776 scopus 로고
    • Location of the cell-attachment site in fibronectin with monoclonal antibodies and proteolytic fragments of the molecule
    • Pierschbacher, M. D., E. G. Hayman, and E. Ruoslahti. 1981. Location of the cell-attachment site in fibronectin with monoclonal antibodies and proteolytic fragments of the molecule. Cell 26:259-267.
    • (1981) Cell , vol.26 , pp. 259-267
    • Pierschbacher, M.D.1    Hayman, E.G.2    Ruoslahti, E.3
  • 33
    • 0021271957 scopus 로고
    • Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule
    • Pierschbacher, M. D., and E. Ruoslahti. 1984. Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule. Nature 309:30-33.
    • (1984) Nature , vol.309 , pp. 30-33
    • Pierschbacher, M.D.1    Ruoslahti, E.2
  • 34
    • 84907132888 scopus 로고
    • The current role of Aspergillus and Penicillium in human and animal health
    • Pitt, J. I. 1994. The current role of Aspergillus and Penicillium in human and animal health. J. Med. Vet. Mycol. 32:17-32.
    • (1994) J. Med. Vet. Mycol. , vol.32 , pp. 17-32
    • Pitt, J.I.1
  • 36
    • 0030840333 scopus 로고    scopus 로고
    • Identification of N-acetylneuraminic acid and its 9-0 acetylated derivative on the cell surface of Cryptococcus neoformans: Influence of fungal phagocytosis
    • Rodrigues, M. L., S. Rozental, J. N. S. S. Couceiro, J. Angluster, C. S. Alviano, and L. R. Travassos. 1997. Identification of N-acetylneuraminic acid and its 9-0 acetylated derivative on the cell surface of Cryptococcus neoformans: influence of fungal phagocytosis. Infect. Immun. 65:4937-4942.
    • (1997) Infect. Immun. , vol.65 , pp. 4937-4942
    • Rodrigues, M.L.1    Rozental, S.2    Couceiro, J.N.S.S.3    Angluster, J.4    Alviano, C.S.5    Travassos, L.R.6
  • 37
    • 0030055076 scopus 로고    scopus 로고
    • Extracellular matrix and lung inflammation
    • Roman, J. 1996. Extracellular matrix and lung inflammation. Immunol. Res. 15:163-178.
    • (1996) Immunol. Res. , vol.15 , pp. 163-178
    • Roman, J.1
  • 38
    • 0002937537 scopus 로고    scopus 로고
    • Fibronectins and fibronectin receptors in lung development, injury and repair
    • R. G. Crystal and J. B. West (ed.), Lippincott-Raven, Philadelphia, Pa.
    • Roman, J., and J. A. McDonald. 1997. Fibronectins and fibronectin receptors in lung development, injury and repair, p. 737-755. In R. G. Crystal and J. B. West (ed.), The lung: scientific foundations. Lippincott-Raven, Philadelphia, Pa.
    • (1997) The Lung: Scientific Foundations , pp. 737-755
    • Roman, J.1    McDonald, J.A.2
  • 40
    • 0021223036 scopus 로고
    • Histochemical localization of sialoglycoconjugates with a sialic acid-specific lectin from the slug Limax flavus
    • Schulte, B. A., S. S. Spicer, and R. L. Miller. 1984. Histochemical localization of sialoglycoconjugates with a sialic acid-specific lectin from the slug Limax flavus. Histochem. J. 16:1125-1132.
    • (1984) Histochem. J. , vol.16 , pp. 1125-1132
    • Schulte, B.A.1    Spicer, S.S.2    Miller, R.L.3
  • 41
    • 0033559259 scopus 로고    scopus 로고
    • Crystal structure of a heparin- And integrin-binding segment of human fibronectin
    • Sharma, A., J. A. Askari, M. J. Humphries, E. Y. Jones, and D. I. Stuart. 1999. Crystal structure of a heparin- and integrin-binding segment of human fibronectin. EMBO J. 18:1468-1479.
    • (1999) EMBO J. , vol.18 , pp. 1468-1479
    • Sharma, A.1    Askari, J.A.2    Humphries, M.J.3    Jones, E.Y.4    Stuart, D.I.5
  • 42
    • 0022461275 scopus 로고
    • Purification and complete primary structures of the heparin-, cell-, and DNA-binding domains of bovine plasma fibronectin
    • Skorstengaard, K., M. S. Jensen, T. E. Petersen, and S. Magnusson. 1986. Purification and complete primary structures of the heparin-, cell-, and DNA-binding domains of bovine plasma fibronectin. Eur. J. Biochem. 154: 15-29.
    • (1986) Eur. J. Biochem. , vol.154 , pp. 15-29
    • Skorstengaard, K.1    Jensen, M.S.2    Petersen, T.E.3    Magnusson, S.4
  • 43
    • 2642676854 scopus 로고    scopus 로고
    • Anionogenic groups and surface sialoglycoconjugate structures of yeast forms of the human pathogen Paracoccidioides brasiliensis
    • Soares, R. M., F. Costa e Silva-Filho, S. Rozental, J. Angluster, W. de Souza, C. S. Alviano, and L. R. Travassos. 1998. Anionogenic groups and surface sialoglycoconjugate structures of yeast forms of the human pathogen Paracoccidioides brasiliensis. Microbiology 144:309-314.
    • (1998) Microbiology , vol.144 , pp. 309-314
    • Soares, R.M.1    Costa E Silva-Filho, F.2    Rozental, S.3    Angluster, J.4    De Souza, W.5    Alviano, C.S.6    Travassos, L.R.7
  • 44
    • 0021868083 scopus 로고
    • Ultrastructural distribution of fibronectin in normal and fibrotic human lung
    • Torikata, C., B. Villiger, C. Kuhn III, and J. A. McDonald. 1985. Ultrastructural distribution of fibronectin in normal and fibrotic human lung. Lab. Investig. 52:399-408.
    • (1985) Lab. Investig. , vol.52 , pp. 399-408
    • Torikata, C.1    Villiger, B.2    Kuhn C. III3    McDonald, J.A.4
  • 45
    • 0027285494 scopus 로고
    • Interaction between Aspergillus fumigatus and basement membrane laminin: Binding and substrate degradation
    • Tronchìn, G., J. P. Bouchara, G. Larcher, J. C. Lissitzky, and D. Chabasse. 1993. Interaction between Aspergillus fumigatus and basement membrane laminin: binding and substrate degradation. Biol. Cell. 77:201-208.
    • (1993) Biol. Cell. , vol.77 , pp. 201-208
    • Tronchìn, G.1    Bouchara, J.P.2    Larcher, G.3    Lissitzky, J.C.4    Chabasse, D.5
  • 46
    • 0024203350 scopus 로고
    • Heparin type IV collagen interactions: Equilibrium binding and inhibition of type IV collagen self-assembly
    • Tsilibary, E. C., G. G. Koliakos, A. S. Charonis, A. M. Vogel, L. A. Reger, and L. T. Furcht. 1988. Heparin type IV collagen interactions: equilibrium binding and inhibition of type IV collagen self-assembly. J. Biol. Chem. 263: 19112-19118.
    • (1988) J. Biol. Chem. , vol.263 , pp. 19112-19118
    • Tsilibary, E.C.1    Koliakos, G.G.2    Charonis, A.S.3    Vogel, A.M.4    Reger, L.A.5    Furcht, L.T.6
  • 47
    • 0031010201 scopus 로고    scopus 로고
    • Epidemiology of Aspergillus infections in a large cohort of patients undergoing bone marrow transplantation
    • Wald, A., W. Leisenring, J. A. van Burik, and R. A. Bowden. 1997. Epidemiology of Aspergillus infections in a large cohort of patients undergoing bone marrow transplantation. J. Infect. Dis. 175:1459-1466.
    • (1997) J. Infect. Dis. , vol.175 , pp. 1459-1466
    • Wald, A.1    Leisenring, W.2    Van Burik, J.A.3    Bowden, R.A.4
  • 48
    • 0029846488 scopus 로고    scopus 로고
    • Structural domains of heparan sulfate for recognition of the C-terminal domain of human plasma fibronectin (HE-PII)
    • Walker, A., and J. T. Gallagher. 1996. Structural domains of heparan sulfate for recognition of the C-terminal domain of human plasma fibronectin (HE-PII). Biochem. J. 317:871-877.
    • (1996) Biochem. J. , vol.317 , pp. 871-877
    • Walker, A.1    Gallagher, J.T.2
  • 49
    • 0000280766 scopus 로고
    • Fibronectin and other adhesive glycoproteins
    • E. D. Hay (ed.), Plenum Press, New York, N.Y.
    • Yamada, K. M. 1991. Fibronectin and other adhesive glycoproteins, p. 111-146. In E. D. Hay (ed.), Cell biology of extracellular matrix, 2nd ed. Plenum Press, New York, N.Y.
    • (1991) Cell Biology of Extracellular Matrix, 2nd Ed. , pp. 111-146
    • Yamada, K.M.1


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