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Volumn 2, Issue 1, 2000, Pages 91-98

Microbial metalloproteases and pathogenesis

Author keywords

Exotoxin; Metalloprotease; Metalloproteinase

Indexed keywords

METALLOPROTEINASE;

EID: 0033973889     PISSN: 12864579     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1286-4579(00)00280-X     Document Type: Review
Times cited : (296)

References (50)
  • 2
    • 0020857013 scopus 로고
    • Pseudomonas aeruginosa elastase and its role in pseudomonas infections
    • Wretlind B., Pavlovskis O.R. Pseudomonas aeruginosa elastase and its role in pseudomonas infections. Rev. Infect. Dis. 5 S:1983;998-1004.
    • (1983) Rev. Infect. Dis. , vol.5 , pp. 998-1004
    • Wretlind, B.1    Pavlovskis, O.R.2
  • 3
    • 0028082122 scopus 로고
    • The effect on enterotoxicity of protease purified from Vibrio cholerae O1
    • Ichinose Y., Ehara M., Honda T., Miwatani T. The effect on enterotoxicity of protease purified from Vibrio cholerae O1. FEMS Microbiol. Lett. 115:1994;265-271.
    • (1994) FEMS Microbiol. Lett. , vol.115 , pp. 265-271
    • Ichinose, Y.1    Ehara, M.2    Honda, T.3    Miwatani, T.4
  • 4
    • 0028903373 scopus 로고
    • Structure and function of Clostridium botulinum toxins
    • Oguma K., Fujinaga Y., Inoue K. Structure and function of Clostridium botulinum toxins. Microbiol. Immunol. 39:1995;161-168.
    • (1995) Microbiol. Immunol. , vol.39 , pp. 161-168
    • Oguma, K.1    Fujinaga, Y.2    Inoue, K.3
  • 6
    • 0028088404 scopus 로고
    • Anthrax toxin lethal factor contains a zinc metalloprotease consensus sequence which is required for lethal toxin activity
    • Klimpel K.R., Arora N., Leppla S.H. Anthrax toxin lethal factor contains a zinc metalloprotease consensus sequence which is required for lethal toxin activity. Mol. Microbiol. 13:1994;1093-1100.
    • (1994) Mol. Microbiol. , vol.13 , pp. 1093-1100
    • Klimpel, K.R.1    Arora, N.2    Leppla, S.H.3
  • 7
    • 33845280830 scopus 로고
    • Structural basis of the action of thermolysin and related zinc peptidases
    • Matthews B.W. Structural basis of the action of thermolysin and related zinc peptidases. Acc. Chem. Res. 21:1988;333-340.
    • (1988) Acc. Chem. Res. , vol.21 , pp. 333-340
    • Matthews, B.W.1
  • 8
    • 0025906404 scopus 로고
    • Three-dimensional structure of the elastase of Pseudomonas aeruginosa at 1.5-A resolution
    • Thayer M.M., Flaherty K.M., McKay D.B. Three-dimensional structure of the elastase of Pseudomonas aeruginosa at 1.5-A resolution. J. Biol. Chem. 266:1991;2864-2871.
    • (1991) J. Biol. Chem. , vol.266 , pp. 2864-2871
    • Thayer, M.M.1    Flaherty, K.M.2    McKay, D.B.3
  • 9
    • 0021168136 scopus 로고
    • Pathogenesis of serratial infection: Activation of the Hageman factor-prekallikrein cascade by serratial protease
    • Matsumoto K., Yamamoto T., Kamata R., Maeda H. Pathogenesis of serratial infection: activation of the Hageman factor-prekallikrein cascade by serratial protease. J. Biochem. 96:1984;739-749.
    • (1984) J. Biochem. , vol.96 , pp. 739-749
    • Matsumoto, K.1    Yamamoto, T.2    Kamata, R.3    Maeda, H.4
  • 11
    • 0031946979 scopus 로고    scopus 로고
    • Lethal factor active-site mutations affect catalytic activity in vitro
    • Hammond S.E., Hanna P.C. Lethal factor active-site mutations affect catalytic activity in vitro. Infect. Immun. 66:1998;2374-2378.
    • (1998) Infect. Immun. , vol.66 , pp. 2374-2378
    • Hammond, S.E.1    Hanna, P.C.2
  • 12
    • 0031781189 scopus 로고    scopus 로고
    • Secretion of elastolytic enzymes and their propeptides by Pseudomonas aeruginosa
    • Braun P., Degroot A., Bitter W., Tommassen J. Secretion of elastolytic enzymes and their propeptides by Pseudomonas aeruginosa. J. Bacteriol. 173:1998;3467-3469.
    • (1998) J. Bacteriol. , vol.173 , pp. 3467-3469
    • Braun, P.1    Degroot, A.2    Bitter, W.3    Tommassen, J.4
  • 13
    • 0030704251 scopus 로고    scopus 로고
    • Functional domains of a zinc metalloprotease from Vibrio vulnificus
    • Miyoshi S., Wakae H., Tomochika K., Shinoda S. Functional domains of a zinc metalloprotease from Vibrio vulnificus. Infect. Immun. 179:1997;7606-7609.
    • (1997) Infect. Immun. , vol.179 , pp. 7606-7609
    • Miyoshi, S.1    Wakae, H.2    Tomochika, K.3    Shinoda, S.4
  • 14
    • 0026475721 scopus 로고
    • Sequence of a cluster of genes controlling synthesis and secretion of alkaline proteinase in Pseudomonas aeruginosa: Relationships to other secretory pathways
    • Duong F., Lazdunski A., Cami B., Murgier M. Sequence of a cluster of genes controlling synthesis and secretion of alkaline proteinase in Pseudomonas aeruginosa: relationships to other secretory pathways. Gene. 121:1992;47-54.
    • (1992) Gene , vol.121 , pp. 47-54
    • Duong, F.1    Lazdunski, A.2    Cami, B.3    Murgier, M.4
  • 15
    • 0026088819 scopus 로고
    • The secretion genes of Pseudomonas aeruginosa alkaline protease are functionally related to those of Erwinia chrysanthemi protease and Escherichia coli α-hemolysin
    • Guzzo J., Duong F., Wandersman C., Murgier M., Lazdunski A. The secretion genes of Pseudomonas aeruginosa alkaline protease are functionally related to those of Erwinia chrysanthemi protease and Escherichia coli α-hemolysin. Mol. Micrbiol. 5:1991;447-453.
    • (1991) Mol. Micrbiol. , vol.5 , pp. 447-453
    • Guzzo, J.1    Duong, F.2    Wandersman, C.3    Murgier, M.4    Lazdunski, A.5
  • 16
    • 0027535307 scopus 로고
    • LasR of Pseudomonas aeruginosa is a transcriptional activator of the alkaline protease gene (apr) and an enhancer of exotoxin A expression
    • Gambello M.J., Kaye S., Iglewski B.H. LasR of Pseudomonas aeruginosa is a transcriptional activator of the alkaline protease gene (apr) and an enhancer of exotoxin A expression. Infect. Immun. 61:1993;1180-1184.
    • (1993) Infect. Immun. , vol.61 , pp. 1180-1184
    • Gambello, M.J.1    Kaye, S.2    Iglewski, B.H.3
  • 17
    • 0028849833 scopus 로고
    • Synthesis of multiple exoproducts in Pseudomonas aeruginosa is under the control of RhlR-RhlI, another set of regulators in strain PAO1 with homology to the antoinducer-responsive LuxR-LuxI family
    • Brint J.M., Ohman D.E. Synthesis of multiple exoproducts in Pseudomonas aeruginosa is under the control of RhlR-RhlI, another set of regulators in strain PAO1 with homology to the antoinducer-responsive LuxR-LuxI family. J. Bacteriol. 177:1995;7155-7163.
    • (1995) J. Bacteriol. , vol.177 , pp. 7155-7163
    • Brint, J.M.1    Ohman, D.E.2
  • 19
    • 0029858955 scopus 로고    scopus 로고
    • In vitro proteolytic processing and activation of the recombinant precursor of El Tol cytolysin/hemolysin (pro-HlyA) of Vibrio cholerae by soluble hemagglutinin/protease of V. cholerae, trypsin, and other proteases
    • Nagamune K., Yamamoto K., Naka A., Matsuyama J., Miwatani T., Honda T. In vitro proteolytic processing and activation of the recombinant precursor of El Tol cytolysin/hemolysin (pro-HlyA) of Vibrio cholerae by soluble hemagglutinin/protease of V. cholerae, trypsin, and other proteases. Infect. Immun. 64:1996;4655-4658.
    • (1996) Infect. Immun. , vol.64 , pp. 4655-4658
    • Nagamune, K.1    Yamamoto, K.2    Naka, A.3    Matsuyama, J.4    Miwatani, T.5    Honda, T.6
  • 20
    • 0029083327 scopus 로고
    • Proteolytic activity of Bacteroides fragilis enterotoxin causes fluid secretion and intestinal damage in vivo
    • Obiso R.J., Lyerly D.M., VanTassell R.L., Wilkins T.D. Proteolytic activity of Bacteroides fragilis enterotoxin causes fluid secretion and intestinal damage in vivo. Infect. Immun. 63:1995;3820-3826.
    • (1995) Infect. Immun. , vol.63 , pp. 3820-3826
    • Obiso, R.J.1    Lyerly, D.M.2    Vantassell, R.L.3    Wilkins, T.D.4
  • 21
    • 0032440487 scopus 로고    scopus 로고
    • Bacteroides fragilis enterotoxin cleaves the zonula adherens protein, E-cadherin
    • Wu S., Lim K.C., Huang J., Saidi R.F., Sears C.L. Bacteroides fragilis enterotoxin cleaves the zonula adherens protein, E-cadherin. Proc. Natl. Acad. Sci. USA. 95:1998;14979-14984.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 14979-14984
    • Wu, S.1    Lim, K.C.2    Huang, J.3    Saidi, R.F.4    Sears, C.L.5
  • 22
    • 0023109713 scopus 로고
    • Enhancement of vascular permeability due to histamine-releasing effect of Vibrio vulnificus protease
    • Miyoshi S., Sugiyama K., Suzuki Y., Furuta H., Miyoshi N., Shinoda S. Enhancement of vascular permeability due to histamine-releasing effect of Vibrio vulnificus protease. FEMS Microbiol. Lett. 40:1987;95-98.
    • (1987) FEMS Microbiol. Lett. , vol.40 , pp. 95-98
    • Miyoshi, S.1    Sugiyama, K.2    Suzuki, Y.3    Furuta, H.4    Miyoshi, N.5    Shinoda, S.6
  • 25
    • 0026764605 scopus 로고
    • Activation mechanism of human Hageman factor-plasma kallikrein-kinin system by Vibrio vulnificus metalloprotease
    • Miyoshi S., Shinoda S. Activation mechanism of human Hageman factor-plasma kallikrein-kinin system by Vibrio vulnificus metalloprotease. FEBS Lett. 308:1992;315-319.
    • (1992) FEBS Lett. , vol.308 , pp. 315-319
    • Miyoshi, S.1    Shinoda, S.2
  • 26
    • 0029595242 scopus 로고
    • Actions of Vibrio vulnificus metalloprotease on human plasma proteinase-proteinase inhibitor systems: A comparative study of native protease with its derivative modified by polyethylene glycol
    • Miyoshi S., Narukawa H., Tomochika K., Shinoda S. Actions of Vibrio vulnificus metalloprotease on human plasma proteinase-proteinase inhibitor systems: a comparative study of native protease with its derivative modified by polyethylene glycol. Microbiol. Immunol. 39:1995;959-966.
    • (1995) Microbiol. Immunol. , vol.39 , pp. 959-966
    • Miyoshi, S.1    Narukawa, H.2    Tomochika, K.3    Shinoda, S.4
  • 27
    • 0029907110 scopus 로고    scopus 로고
    • Role of microbial proteases in pathogenesis
    • Maeda H. Role of microbial proteases in pathogenesis. Microbiol. Immunol. 40:1996;685-699.
    • (1996) Microbiol. Immunol. , vol.40 , pp. 685-699
    • Maeda, H.1
  • 28
    • 0017817596 scopus 로고
    • Purification of Pseudomonas aeruginosa proteases and microscopic characterization of pseudomonal protease-induced rabbit corneal damage
    • Kreger A.S., Gray L.D. Purification of Pseudomonas aeruginosa proteases and microscopic characterization of pseudomonal protease-induced rabbit corneal damage. Infect. Immun. 19:1978;630-648.
    • (1978) Infect. Immun. , vol.19 , pp. 630-648
    • Kreger, A.S.1    Gray, L.D.2
  • 29
    • 0019487621 scopus 로고
    • Characterization of rabbit corneal damage produced by Serratia keratitis and by a serratia protease
    • Lyerly D., Gray L., Kreger A. Characterization of rabbit corneal damage produced by Serratia keratitis and by a serratia protease. Infect. Immun. 33:1981;927-932.
    • (1981) Infect. Immun. , vol.33 , pp. 927-932
    • Lyerly, D.1    Gray, L.2    Kreger, A.3
  • 30
    • 0031686026 scopus 로고    scopus 로고
    • Characterization of the hemorrhagic reaction caused by Vibrio vulnificus metalloprotease, a member of the thermolysin family
    • Miyoshi S., Nakazawa H., Tomochika K., Shinoda S. Characterization of the hemorrhagic reaction caused by Vibrio vulnificus metalloprotease, a member of the thermolysin family. Infect. Immun. 66:1998;4851-4855.
    • (1998) Infect. Immun. , vol.66 , pp. 4851-4855
    • Miyoshi, S.1    Nakazawa, H.2    Tomochika, K.3    Shinoda, S.4
  • 31
    • 0029047842 scopus 로고
    • Protease-cleaved iron-transferrin augments oxidant-mediated endothelial cell injury via hydroxyl radical formation
    • Miller R.A., Britigan B.E. Protease-cleaved iron-transferrin augments oxidant-mediated endothelial cell injury via hydroxyl radical formation. J. Clin. Invest. 95:1995;2491-2500.
    • (1995) J. Clin. Invest. , vol.95 , pp. 2491-2500
    • Miller, R.A.1    Britigan, B.E.2
  • 32
    • 0023243153 scopus 로고
    • 2-macroglobulin and chicken egg white ovomacroglobulin
    • 2-macroglobulin and chicken egg white ovomacroglobulin. J. Biochem. 101:1987;199-205.
    • (1987) J. Biochem. , vol.101 , pp. 199-205
    • Molla, A.1    Oda, T.2    Maeda, H.3
  • 33
    • 0023655730 scopus 로고
    • 2-macroglobulin and regeneration of protease activity and cytotoxicity
    • 2-macroglobulin and regeneration of protease activity and cytotoxicity. J. Biol. Chem. 262:1987;10946-10950.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10946-10950
    • Maeda, H.1    Molla, A.2    Oda, T.3    Katsuki, T.4
  • 34
    • 0024532987 scopus 로고
    • Characterization of a Legionella pneumophila extracellular protease exhibiting hemolytic and cytotoxic activities
    • Keen M.G., Hoffman P.S. Characterization of a Legionella pneumophila extracellular protease exhibiting hemolytic and cytotoxic activities. Infect. Immun. 57:1989;732-738.
    • (1989) Infect. Immun. , vol.57 , pp. 732-738
    • Keen, M.G.1    Hoffman, P.S.2
  • 36
    • 0032581369 scopus 로고    scopus 로고
    • Anthrax lethal factor cleaves the N-terminus of MAPKKs and induces tyrosine/threonine phosphorylation of MAPKs in cultured macrophages
    • Vitale G., Pellizzari R., Recchi C., Napolitani G., Mock M., Montecucco C. Anthrax lethal factor cleaves the N-terminus of MAPKKs and induces tyrosine/threonine phosphorylation of MAPKs in cultured macrophages. Biochem. Biophys. Res. Commun. 248:1998;706-711.
    • (1998) Biochem. Biophys. Res. Commun. , vol.248 , pp. 706-711
    • Vitale, G.1    Pellizzari, R.2    Recchi, C.3    Napolitani, G.4    Mock, M.5    Montecucco, C.6
  • 37
    • 0018411654 scopus 로고
    • Assessment of protease (elastase) as a Pseudomonas aeruginosa virulence factor in experimental mouse burn infection
    • Pavlovskis O.R., Wretlind B. Assessment of protease (elastase) as a Pseudomonas aeruginosa virulence factor in experimental mouse burn infection. Infect. Immun. 24:1979;181-187.
    • (1979) Infect. Immun. , vol.24 , pp. 181-187
    • Pavlovskis, O.R.1    Wretlind, B.2
  • 38
    • 0029943570 scopus 로고    scopus 로고
    • Bradykinin generation triggered by Pseudomonas proteases facilitates invasion of the systemic circulation by Pseudomonas aeruginosa
    • Sakata Y., Akaike T., Suga M., Ijiri S., Ando M., Maeda H. Bradykinin generation triggered by Pseudomonas proteases facilitates invasion of the systemic circulation by Pseudomonas aeruginosa. Microbiol. Immunol. 40:1996;415-423.
    • (1996) Microbiol. Immunol. , vol.40 , pp. 415-423
    • Sakata, Y.1    Akaike, T.2    Suga, M.3    Ijiri, S.4    Ando, M.5    Maeda, H.6
  • 40
    • 0027155975 scopus 로고
    • A bacterial protease perturbs the paracellular barrier function of transporting epithelial monolayers in culture
    • Azghani A.O., Gray L.D., Johnson A.R. A bacterial protease perturbs the paracellular barrier function of transporting epithelial monolayers in culture. Infect. Immun. 61:1993;2681-2686.
    • (1993) Infect. Immun. , vol.61 , pp. 2681-2686
    • Azghani, A.O.1    Gray, L.D.2    Johnson, A.R.3
  • 41
    • 0026734829 scopus 로고
    • Significant role of an exocellular protease in utilization of heme by Vibrio vulnificus
    • Nishina Y., Miyoshi S., Nagase A., Shinoda S. Significant role of an exocellular protease in utilization of heme by Vibrio vulnificus. Infect. Immun. 60:1992;2128-2132.
    • (1992) Infect. Immun. , vol.60 , pp. 2128-2132
    • Nishina, Y.1    Miyoshi, S.2    Nagase, A.3    Shinoda, S.4
  • 42
    • 0029787281 scopus 로고    scopus 로고
    • Involvement of vulnibactin and exocellular protease in utilization of transferrin- And lactoferrin-bound iron by Vibrio vulnificus
    • Okujo N., Akiyama T., Miyoshi S., Shinoda S., Yamamoto S. Involvement of vulnibactin and exocellular protease in utilization of transferrin- and lactoferrin-bound iron by Vibrio vulnificus. Microbiol. Immunol. 40:1996;595-598.
    • (1996) Microbiol. Immunol. , vol.40 , pp. 595-598
    • Okujo, N.1    Akiyama, T.2    Miyoshi, S.3    Shinoda, S.4    Yamamoto, S.5
  • 43
    • 0025275204 scopus 로고
    • Inactivation of chemotactic activity of C5a by the serratial 56-kilodalton protease
    • Oda T., Kojima Y., Akaike T., Ijiri S., Molla A., Maeda H. Inactivation of chemotactic activity of C5a by the serratial 56-kilodalton protease. Infect. Immun. 58:1990;1269-1272.
    • (1990) Infect. Immun. , vol.58 , pp. 1269-1272
    • Oda, T.1    Kojima, Y.2    Akaike, T.3    Ijiri, S.4    Molla, A.5    Maeda, H.6
  • 44
    • 0025170582 scopus 로고
    • Proteolytic inactivation of cytokines by Pseudomonas aeruginosa
    • Parmely M., Gale A., Clabaugh M., Horvat R., Zhou W.W. Proteolytic inactivation of cytokines by Pseudomonas aeruginosa. Infect. Immun. 58:1990;3009-3014.
    • (1990) Infect. Immun. , vol.58 , pp. 3009-3014
    • Parmely, M.1    Gale, A.2    Clabaugh, M.3    Horvat, R.4    Zhou, W.W.5
  • 45
    • 0027288424 scopus 로고
    • Legionella pneumophila protease inactivates interleukin-2 and cleaves CD4 on human T cells
    • Mintz C.S., Miller R.D., Gutgsell N.S., Malek T. Legionella pneumophila protease inactivates interleukin-2 and cleaves CD4 on human T cells. Infect. Immun. 61:1993;3416-3421.
    • (1993) Infect. Immun. , vol.61 , pp. 3416-3421
    • Mintz, C.S.1    Miller, R.D.2    Gutgsell, N.S.3    Malek, T.4
  • 46
    • 0029736417 scopus 로고    scopus 로고
    • Novel pathogenic mechanism of microbial metalloproteinases: Liberation of membrane-anchored molecules in biologically active form exemplified by studies with the human interleukin-6 receptor
    • Vollmer P., Walev I., Rose-John S., Bhakdi S. Novel pathogenic mechanism of microbial metalloproteinases: liberation of membrane-anchored molecules in biologically active form exemplified by studies with the human interleukin-6 receptor. Infect. Immun. 64:1996;3646-3651.
    • (1996) Infect. Immun. , vol.64 , pp. 3646-3651
    • Vollmer, P.1    Walev, I.2    Rose-John, S.3    Bhakdi, S.4
  • 47
    • 0027197079 scopus 로고
    • Role of Hageman factor/kallikrein-kinin system in pseudomonal elastase-induced shock model
    • Khan M.M.H., Yamamoto T., Araki H., Shibuya Y., Kambara T. Role of Hageman factor/kallikrein-kinin system in pseudomonal elastase-induced shock model. Biochim. Biophys. Acta. 1157:1993;119-126.
    • (1993) Biochim. Biophys. Acta , vol.1157 , pp. 119-126
    • Khan, M.M.H.1    Yamamoto, T.2    Araki, H.3    Shibuya, Y.4    Kambara, T.5
  • 48
    • 0028340071 scopus 로고
    • Purification and characterization of an elastinolytic metalloprotease from Aspergillus fumigatus and immunoelectron microscopic evidence of secretion of this enzyme by the fungus invading the murine lung
    • Markaryan A., Morozova I., Yu H., Kolattukudy P.E. Purification and characterization of an elastinolytic metalloprotease from Aspergillus fumigatus and immunoelectron microscopic evidence of secretion of this enzyme by the fungus invading the murine lung. Infect. Immun. 62:1994;2149-2157.
    • (1994) Infect. Immun. , vol.62 , pp. 2149-2157
    • Markaryan, A.1    Morozova, I.2    Yu, H.3    Kolattukudy, P.E.4
  • 50


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