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Volumn 22, Issue 5, 2016, Pages 563-567

Activation of Bacteroides fragilis toxin by a novel bacterial protease contributes to anaerobic sepsis in mice

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; CYSTEINE PROTEINASE; FRAGILYSIN; FRAGIPAIN; PROTEINASE; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; BACTERIAL TOXIN; METALLOPROTEINASE;

EID: 84964388948     PISSN: 10788956     EISSN: 1546170X     Source Type: Journal    
DOI: 10.1038/nm.4077     Document Type: Article
Times cited : (77)

References (50)
  • 2
    • 63149120571 scopus 로고    scopus 로고
    • Induction of persistent colitis by a human commensal, enterotoxigenic Bacteroides fragilis, in wild-type C57BL/6 mice
    • Rhee, K.J. et al. Induction of persistent colitis by a human commensal, enterotoxigenic Bacteroides fragilis, in wild-type C57BL/6 mice. Infect. Immun. 77, 1708-1718 (2009).
    • (2009) Infect. Immun. , vol.77 , pp. 1708-1718
    • Rhee, K.J.1
  • 3
    • 69949120571 scopus 로고    scopus 로고
    • A human colonic commensal promotes colon tumorigenesis via activation of T helper type 17 T cell responses
    • Wu, S. et al. A human colonic commensal promotes colon tumorigenesis via activation of T helper type 17 T cell responses. Nat. Med. 15, 1016-1022 (2009).
    • (2009) Nat. Med. , vol.15 , pp. 1016-1022
    • Wu, S.1
  • 4
    • 0029853202 scopus 로고    scopus 로고
    • Association of enterotoxigenic Bacteroides fragilis with bacteremia
    • Kato, N., Kato, H., Watanabe, K. & Ueno, K. Association of enterotoxigenic Bacteroides fragilis with bacteremia. Clin. Infect. Dis. 23 (suppl. 1), S83-S86 (1996).
    • (1996) Clin. Infect. Dis. , vol.23 , pp. S83-S86
    • Kato, N.1    Kato, H.2    Watanabe, K.3    Ueno, K.4
  • 5
    • 28844470669 scopus 로고    scopus 로고
    • Characterization of the Bacteroides fragilis pathogenicity island in human blood culture isolates
    • Claros, M.C. et al. Characterization of the Bacteroides fragilis pathogenicity island in human blood culture isolates. Anaerobe 12, 17-22 (2006).
    • (2006) Anaerobe , vol.12 , pp. 17-22
    • Claros, M.C.1
  • 6
    • 0029070855 scopus 로고
    • Attributable mortality of bacteremia associated with the Bacteroides fragilis group
    • Redondo, M.C., Arbo, M.D., Grindlinger, J. & Snydman, D.R. Attributable mortality of bacteremia associated with the Bacteroides fragilis group. Clin. Infect. Dis. 20, 1492-1496 (1995).
    • (1995) Clin. Infect. Dis. , vol.20 , pp. 1492-1496
    • Redondo, M.C.1    Arbo, M.D.2    Grindlinger, J.3    Snydman, D.R.4
  • 7
    • 84873743452 scopus 로고    scopus 로고
    • Population-based assessment of the incidence, risk factors, and outcomes of anaerobic bloodstream infections
    • Ngo, J.T. et al. Population-based assessment of the incidence, risk factors, and outcomes of anaerobic bloodstream infections. Infection 41, 41-48 (2013).
    • (2013) Infection , vol.41 , pp. 41-48
    • Ngo, J.T.1
  • 8
    • 84881318637 scopus 로고    scopus 로고
    • Ferritin-like family proteins in the anaerobe Bacteroides fragilis: When an oxygen storm is coming, take your iron to the shelter
    • Rocha, E.R. & Smith, C.J. Ferritin-like family proteins in the anaerobe Bacteroides fragilis: when an oxygen storm is coming, take your iron to the shelter. Biometals 26, 577-591 (2013).
    • (2013) Biometals , vol.26 , pp. 577-591
    • Rocha, E.R.1    Smith, C.J.2
  • 9
    • 0033850395 scopus 로고    scopus 로고
    • Aerobic and anaerobic microbiology in intra-abdominal infections associated with diverticulitis
    • Brook, I. & Frazier, E.H. Aerobic and anaerobic microbiology in intra-abdominal infections associated with diverticulitis. J. Med. Microbiol. 49, 827-830 (2000).
    • (2000) J. Med. Microbiol. , vol.49 , pp. 827-830
    • Brook, I.1    Frazier, E.H.2
  • 10
    • 84937974735 scopus 로고    scopus 로고
    • Are incidence and epidemiology of anaerobic bacteremia really changing?
    • Vena, A. et al. Are incidence and epidemiology of anaerobic bacteremia really changing? Eur. J. Clin. Microbiol. Infect. Dis. 34, 1621-1629 (2015).
    • (2015) Eur. J. Clin. Microbiol. Infect. Dis. , vol.34 , pp. 1621-1629
    • Vena, A.1
  • 11
    • 84925683536 scopus 로고    scopus 로고
    • Variations in organism-specific severe sepsis mortality in the United States: 1999-2008
    • Ani, C., Farshidpanah, S., Bellinghausen Stewart, A. & Nguyen, H.B. Variations in organism-specific severe sepsis mortality in the United States: 1999-2008. Crit. Care Med. 43, 65-77 (2015).
    • (2015) Crit. Care Med. , vol.43 , pp. 65-77
    • Ani, C.1    Farshidpanah, S.2    Bellinghausen Stewart, A.3    Nguyen, H.B.4
  • 12
    • 84944355387 scopus 로고    scopus 로고
    • A comparison of outcomes of emergent, urgent, and elective surgical treatment of diverticulitis
    • Moghadamyeghaneh, Z. et al. A comparison of outcomes of emergent, urgent, and elective surgical treatment of diverticulitis. Am. J. Surg. 210, 838-845 (2015).
    • (2015) Am. J. Surg. , vol.210 , pp. 838-845
    • Moghadamyeghaneh, Z.1
  • 13
    • 75749143053 scopus 로고    scopus 로고
    • Lessons learned from the anaerobe survey: Historical perspective and review of the most recent data (2005-2007)
    • Snydman, D.R. et al. Lessons learned from the anaerobe survey: historical perspective and review of the most recent data (2005-2007). Clin. Infect. Dis. 50 (suppl. 1), S26-S33 (2010).
    • (2010) Clin. Infect. Dis. , vol.50 , pp. S26-S33
    • Snydman, D.R.1
  • 14
    • 0018688946 scopus 로고
    • Protective efficacy of immunization with capsular antigen against experimental infection with Bacteroides fragilis
    • Kasper, D.L., Onderdonk, A.B., Crabb, J. & Bartlett, J.G. Protective efficacy of immunization with capsular antigen against experimental infection with Bacteroides fragilis. J. Infect. Dis. 140, 724-731 (1979).
    • (1979) J. Infect. Dis. , vol.140 , pp. 724-731
    • Kasper, D.L.1    Onderdonk, A.B.2    Crabb, J.3    Bartlett, J.G.4
  • 15
    • 84869462415 scopus 로고    scopus 로고
    • Multidrug-resistant Bacteroides fragilis group on the rise in Europe?
    • Hartmeyer, G.N., Sóki, J., Nagy, E. & Justesen, U.S. Multidrug-resistant Bacteroides fragilis group on the rise in Europe? J. Med. Microbiol. 61, 1784-1788 (2012).
    • (2012) J. Med. Microbiol. , vol.61 , pp. 1784-1788
    • Hartmeyer, G.N.1    Sóki, J.2    Nagy, E.3    Justesen, U.S.4
  • 16
    • 84911007673 scopus 로고    scopus 로고
    • Trends in the susceptibility of commonly encountered clinically significant anaerobes and susceptibilities of blood isolates of anaerobes to 16 antimicrobial agents, including fidaxomicin and rifaximin, 2008-2012, northern Taiwan
    • Wang, F.D., Liao, C.H., Lin, Y.T., Sheng, W.H. & Hsueh, P.R. Trends in the susceptibility of commonly encountered clinically significant anaerobes and susceptibilities of blood isolates of anaerobes to 16 antimicrobial agents, including fidaxomicin and rifaximin, 2008-2012, northern Taiwan. Eur. J. Clin. Microbiol. Infect. Dis. 33, 2041-2052 (2014).
    • (2014) Eur. J. Clin. Microbiol. Infect. Dis. , vol.33 , pp. 2041-2052
    • Wang, F.D.1    Liao, C.H.2    Lin, Y.T.3    Sheng, W.H.4    Hsueh, P.R.5
  • 17
    • 0032703884 scopus 로고    scopus 로고
    • Molecular evolution of the pathogenicity island of enterotoxigenic Bacteroides fragilis strains
    • Franco, A.A. et al. Molecular evolution of the pathogenicity island of enterotoxigenic Bacteroides fragilis strains. J. Bacteriol. 181, 6623-6633 (1999).
    • (1999) J. Bacteriol. , vol.181 , pp. 6623-6633
    • Franco, A.A.1
  • 18
    • 0028893229 scopus 로고
    • The enterotoxin of Bacteroides fragilis is a metalloprotease
    • Moncrief, J.S. et al. The enterotoxin of Bacteroides fragilis is a metalloprotease. Infect. Immun. 63, 175-181 (1995).
    • (1995) Infect. Immun. , vol.63 , pp. 175-181
    • Moncrief, J.S.1
  • 19
    • 0031027277 scopus 로고    scopus 로고
    • Cloning and characterization of the Bacteroides fragilis metalloprotease toxin gene
    • Franco, A.A. et al. Cloning and characterization of the Bacteroides fragilis metalloprotease toxin gene. Infect. Immun. 65, 1007-1013 (1997).
    • (1997) Infect. Immun. , vol.65 , pp. 1007-1013
    • Franco, A.A.1
  • 20
    • 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, 14979-14984 (1998).
    • (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
  • 21
    • 79952133561 scopus 로고    scopus 로고
    • Structure, function and latency regulation of a bacterial enterotoxin potentially derived from a mammalian adamalysin/ADAM xenolog
    • Goulas, T., Arolas, J.L. & Gomis-Rüth, F.X. Structure, function and latency regulation of a bacterial enterotoxin potentially derived from a mammalian adamalysin/ADAM xenolog. Proc. Natl. Acad. Sci. USA 108, 1856-1861 (2011).
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 1856-1861
    • Goulas, T.1    Arolas, J.L.2    Gomis-Rüth, F.X.3
  • 22
    • 0036378394 scopus 로고    scopus 로고
    • Nuclear factor-κB activation pathway in intestinal epithelial cells is a major regulator of chemokine gene expression and neutrophil migration induced by Bacteroides fragilis enterotoxin
    • Kim, J.M. et al. Nuclear factor-κB activation pathway in intestinal epithelial cells is a major regulator of chemokine gene expression and neutrophil migration induced by Bacteroides fragilis enterotoxin. Clin. Exp. Immunol. 130, 59-66 (2002).
    • (2002) Clin. Exp. Immunol. , vol.130 , pp. 59-66
    • Kim, J.M.1
  • 23
    • 84863922855 scopus 로고    scopus 로고
    • ADAM10 mediates vascular injury induced by Staphylococcus aureus α-hemolysin
    • Powers, M.E., Kim, H.K., Wang, Y. & Bubeck Wardenburg, J. ADAM10 mediates vascular injury induced by Staphylococcus aureus α-hemolysin. J. Infect. Dis. 206, 352-356 (2012).
    • (2012) J. Infect. Dis. , vol.206 , pp. 352-356
    • Powers, M.E.1    Kim, H.K.2    Wang, Y.3    Bubeck Wardenburg, J.4
  • 24
    • 80053971276 scopus 로고    scopus 로고
    • A Staphylococcus aureus pore-forming toxin subverts the activity of ADAM10 to cause lethal infection in mice
    • Inoshima, I. et al. A Staphylococcus aureus pore-forming toxin subverts the activity of ADAM10 to cause lethal infection in mice. Nat. Med. 17, 1310-1314 (2011).
    • (2011) Nat. Med. , vol.17 , pp. 1310-1314
    • Inoshima, I.1
  • 25
    • 84983488777 scopus 로고    scopus 로고
    • Synergistic action of Staphylococcus aureus α-toxin on platelets and myeloid lineage cells contributes to lethal sepsis
    • Powers, M.E., Becker, R.E., Sailer, A., Turner, J.R. & Bubeck Wardenburg, J. Synergistic action of Staphylococcus aureus α-toxin on platelets and myeloid lineage cells contributes to lethal sepsis. Cell Host Microbe 17, 775-787 (2015).
    • (2015) Cell Host Microbe , vol.17 , pp. 775-787
    • Powers, M.E.1    Becker, R.E.2    Sailer, A.3    Turner, J.R.4    Bubeck Wardenburg, J.5
  • 26
    • 23344446430 scopus 로고    scopus 로고
    • Mutation of the zinc-binding metalloprotease motif affects Bacteroides fragilis toxin activity but does not affect propeptide processing
    • Franco, A.A., Buckwold, S.L., Shin, J.W., Ascon, M. & Sears, C.L. Mutation of the zinc-binding metalloprotease motif affects Bacteroides fragilis toxin activity but does not affect propeptide processing. Infect. Immun. 73, 5273-5277 (2005).
    • (2005) Infect. Immun. , vol.73 , pp. 5273-5277
    • Franco, A.A.1    Buckwold, S.L.2    Shin, J.W.3    Ascon, M.4    Sears, C.L.5
  • 27
    • 0026504428 scopus 로고
    • Purification and characterization of an enterotoxin from Bacteroides fragilis
    • Van Tassell, R.L., Lyerly, D.M. & Wilkins, T.D. Purification and characterization of an enterotoxin from Bacteroides fragilis. Infect. Immun. 60, 1343-1350 (1992).
    • (1992) Infect. Immun. , vol.60 , pp. 1343-1350
    • Van Tassell, R.L.1    Lyerly, D.M.2    Wilkins, T.D.3
  • 28
    • 1542314750 scopus 로고    scopus 로고
    • The structure-function relationship in the clostripain family of peptidases
    • Labrou, N.E. & Rigden, D.J. The structure-function relationship in the clostripain family of peptidases. Eur. J. Biochem. 271, 983-992 (2004).
    • (2004) Eur. J. Biochem. , vol.271 , pp. 983-992
    • Labrou, N.E.1    Rigden, D.J.2
  • 29
    • 84923233758 scopus 로고    scopus 로고
    • Comparative structural analysis of the caspase family with other clan CD cysteine peptidases
    • McLuskey, K. & Mottram, J.C. Comparative structural analysis of the caspase family with other clan CD cysteine peptidases. Biochem. J. 466, 219-232 (2015).
    • (2015) Biochem. J , vol.466 , pp. 219-232
    • McLuskey, K.1    Mottram, J.C.2
  • 30
    • 0027244427 scopus 로고
    • The heterodimeric protease clostripain from Clostridium histolyticum is encoded by a single gene
    • Dargatz, H., Diefenthal, T., Witte, V., Reipen, G. & von Wettstein, D. The heterodimeric protease clostripain from Clostridium histolyticum is encoded by a single gene. Mol. Gen. Genet. 240, 140-145 (1993).
    • (1993) Mol. Gen. Genet. , vol.240 , pp. 140-145
    • Dargatz, H.1    Diefenthal, T.2    Witte, V.3    Reipen, G.4    Von Wettstein, D.5
  • 31
    • 70450211370 scopus 로고    scopus 로고
    • Challenging a paradigm: Theoretical calculations of the protonation state of the Cys25-His159 catalytic diad in free papain
    • Shokhen, M., Khazanov, N. & Albeck, A. Challenging a paradigm: theoretical calculations of the protonation state of the Cys25-His159 catalytic diad in free papain. Proteins 77, 916-926 (2009).
    • (2009) Proteins , vol.77 , pp. 916-926
    • Shokhen, M.1    Khazanov, N.2    Albeck, A.3
  • 32
    • 30044442427 scopus 로고    scopus 로고
    • A papain-like enzyme at work: Native and acylenzyme intermediate structures in phytochelatin synthesis
    • Vivares, D., Arnoux, P. & Pignol, D. A papain-like enzyme at work: native and acylenzyme intermediate structures in phytochelatin synthesis. Proc. Natl. Acad. Sci. USA 102, 18848-18853 (2005).
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 18848-18853
    • Vivares, D.1    Arnoux, P.2    Pignol, D.3
  • 33
    • 84881061241 scopus 로고    scopus 로고
    • Reaction pathway and free energy profile for papain-catalyzed hydrolysis of N-acetyl-Phe-Gly 4-nitroanilide
    • Wei, D., Huang, X., Liu, J., Tang, M. & Zhan, C.G. Reaction pathway and free energy profile for papain-catalyzed hydrolysis of N-acetyl-Phe-Gly 4-nitroanilide. Biochemistry 52, 5145-5154 (2013).
    • (2013) Biochemistry , vol.52 , pp. 5145-5154
    • Wei, D.1    Huang, X.2    Liu, J.3    Tang, M.4    Zhan, C.G.5
  • 34
    • 84883076264 scopus 로고    scopus 로고
    • Severe sepsis and septic shock
    • Angus, D.C. & van der Poll, T. Severe sepsis and septic shock. N. Engl. J. Med. 369, 840-851 (2013).
    • (2013) N. Engl. J. Med. , vol.369 , pp. 840-851
    • Angus, D.C.1    Van Der Poll, T.2
  • 35
    • 79952075868 scopus 로고    scopus 로고
    • Multiple roles of Staphylococcus aureus enterotoxins: Pathogenicity, superantigenic activity, and correlation to antibiotic resistance
    • Ortega, E., Abriouel, H., Lucas, R. & Gálvez, A. Multiple roles of Staphylococcus aureus enterotoxins: pathogenicity, superantigenic activity, and correlation to antibiotic resistance. Toxins (Basel) 2, 2117-2131 (2010).
    • (2010) Toxins (Basel) , vol.2 , pp. 2117-2131
    • Ortega, E.1    Abriouel, H.2    Lucas, R.3    Gálvez, A.4
  • 36
    • 84870500590 scopus 로고    scopus 로고
    • Shiga toxins and the pathophysiology of hemolytic uremic syndrome in humans and animals
    • Mayer, C.L., Leibowitz, C.S., Kurosawa, S. & Stearns-Kurosawa, D.J. Shiga toxins and the pathophysiology of hemolytic uremic syndrome in humans and animals. Toxins (Basel) 4, 1261-1287 (2012).
    • (2012) Toxins (Basel) , vol.4 , pp. 1261-1287
    • Mayer, C.L.1    Leibowitz, C.S.2    Kurosawa, S.3    Stearns-Kurosawa, D.J.4
  • 37
    • 84862804469 scopus 로고    scopus 로고
    • Genetic requirement for ADAM10 in severe Staphylococcus aureus skin infection
    • Inoshima, N., Wang, Y. & Bubeck Wardenburg, J. Genetic requirement for ADAM10 in severe Staphylococcus aureus skin infection. J. Invest. Dermatol. 132, 1513-1516 (2012).
    • (2012) J. Invest. Dermatol. , vol.132 , pp. 1513-1516
    • Inoshima, N.1    Wang, Y.2    Bubeck Wardenburg, J.3
  • 38
    • 84925357894 scopus 로고    scopus 로고
    • An ADAM10 promoter polymorphism is a functional variant in severe sepsis patients and confers susceptibility to the development of sepsis
    • Cui, L. et al. An ADAM10 promoter polymorphism is a functional variant in severe sepsis patients and confers susceptibility to the development of sepsis. Crit. Care 19, 73 (2015).
    • (2015) Crit. Care , vol.19 , pp. 73
    • Cui, L.1
  • 39
    • 84859426282 scopus 로고    scopus 로고
    • MEROPS: The database of proteolytic enzymes, their substrates and inhibitors
    • Rawlings, N.D., Barrett, A.J. & Bateman, A. MEROPS: the database of proteolytic enzymes, their substrates and inhibitors. Nucleic Acids Res. 40, D343-D350 (2012).
    • (2012) Nucleic Acids Res. , vol.40 , pp. D343-D350
    • Rawlings, N.D.1    Barrett, A.J.2    Bateman, A.3
  • 40
    • 0033004266 scopus 로고    scopus 로고
    • Analysis of a capsular polysaccharide biosynthesis locus of Bacteroides fragilis
    • Comstock, L.E. et al. Analysis of a capsular polysaccharide biosynthesis locus of Bacteroides fragilis. Infect. Immun. 67, 3525-3532 (1999).
    • (1999) Infect. Immun. , vol.67 , pp. 3525-3532
    • Comstock, L.E.1
  • 41
    • 0029874043 scopus 로고    scopus 로고
    • Activation of Shiga-like toxins by mouse and human intestinal mucus correlates with virulence of enterohemorrhagic Escherichia coli O91:H21 isolates in orally infected, streptomycin-treated mice
    • Melton-Celsa, A.R., Darnell, S.C. & O'Brien, A.D. Activation of Shiga-like toxins by mouse and human intestinal mucus correlates with virulence of enterohemorrhagic Escherichia coli O91:H21 isolates in orally infected, streptomycin-treated mice. Infect. Immun. 64, 1569-1576 (1996).
    • (1996) Infect. Immun. , vol.64 , pp. 1569-1576
    • Melton-Celsa, A.R.1    Darnell, S.C.2    O'Brien, A.D.3
  • 42
    • 69949123813 scopus 로고    scopus 로고
    • Identifying genetic determinants needed to establish a human gut symbiont in its habitat
    • Goodman, A.L. et al. Identifying genetic determinants needed to establish a human gut symbiont in its habitat. Cell Host Microbe 6, 279-289 (2009).
    • (2009) Cell Host Microbe , vol.6 , pp. 279-289
    • Goodman, A.L.1
  • 43
    • 46049115447 scopus 로고    scopus 로고
    • Starch catabolism by a prominent human gut symbiont is directed by the recognition of amylose helices
    • Koropatkin, N.M., Martens, E.C., Gordon, J.I. & Smith, T.J. Starch catabolism by a prominent human gut symbiont is directed by the recognition of amylose helices. Structure 16, 1105-1115 (2008).
    • (2008) Structure , vol.16 , pp. 1105-1115
    • Koropatkin, N.M.1    Martens, E.C.2    Gordon, J.I.3    Smith, T.J.4
  • 44
    • 75649151032 scopus 로고    scopus 로고
    • Xia2: An expert system for macromolecular crystallography data reduction
    • Winter, G. xia2: an expert system for macromolecular crystallography data reduction. J. Appl. Cryst. 43, 186-190 (2010).
    • (2010) J. Appl. Cryst , vol.43 , pp. 186-190
    • Winter, G.1
  • 47
    • 84884682632 scopus 로고    scopus 로고
    • Collaboration gets the most out of software
    • Morin, A. et al. Collaboration gets the most out of software. eLife 2, e01456 (2013).
    • (2013) ELife , vol.2
    • Morin, A.1
  • 48
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams, P.D. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D Biol. Crystallogr. 66, 213-221 (2010).
    • (2010) Acta Crystallogr. D Biol. Crystallogr , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 49
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: A web-based environment for protein structure homology modelling
    • Arnold, K., Bordoli, L., Kopp, J. & Schwede, T. The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling. Bioinformatics 22, 195-201 (2006).
    • (2006) Bioinformatics , vol.22 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4


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