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Volumn 71, Issue 5, 2014, Pages 745-770

Bacterial serine proteases secreted by the autotransporter pathway: Classification, specificity, and role in virulence

Author keywords

Autotransporter; Cytotoxin; Glycoprotein; Immune evasion; SPATE

Indexed keywords

AMINO ACID SEQUENCE; BACTERIAL SECRETION SYSTEMS; ENTEROBACTERIACEAE; EVOLUTION, MOLECULAR; GENETIC VARIATION; IMMUNE EVASION; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PHYLOGENY; PROTEIN CONFORMATION; SEQUENCE ALIGNMENT; SERINE PROTEASES; SPECIES SPECIFICITY; SUBSTRATE SPECIFICITY; VIRULENCE;

EID: 84893841370     PISSN: 1420682X     EISSN: 14209071     Source Type: Journal    
DOI: 10.1007/s00018-013-1355-8     Document Type: Review
Times cited : (118)

References (167)
  • 2
    • 0032169654 scopus 로고    scopus 로고
    • The great escape: Structure and function of the autotransporter proteins
    • Henderson IR, Navarro-Garcia F, Nataro JP (1998) The great escape: structure and function of the autotransporter proteins. Trends Microbiol 6(9):370-378
    • (1998) Trends Microbiol , vol.6 , Issue.9 , pp. 370-378
    • Henderson, I.R.1    Navarro-Garcia, F.2    Nataro, J.P.3
  • 3
    • 0035035580 scopus 로고    scopus 로고
    • Two-partner secretion in Gram-negative bacteria: A thrifty, specific pathway for large virulence proteins
    • Jacob-Dubuisson F, Locht C, Antoine R (2001) Two-partner secretion in Gram-negative bacteria: a thrifty, specific pathway for large virulence proteins. Mol Microbiol 40(2):306-313
    • (2001) Mol Microbiol , vol.40 , Issue.2 , pp. 306-313
    • Jacob-Dubuisson, F.1    Locht, C.2    Antoine, R.3
  • 4
    • 33744728321 scopus 로고    scopus 로고
    • Trimeric autotransporter adhesins: Variable structure, common function
    • Linke D et al (2006) Trimeric autotransporter adhesins: variable structure, common function. Trends Microbiol 14(6):264-270
    • (2006) Trends Microbiol , vol.14 , Issue.6 , pp. 264-270
    • Linke, D.1
  • 5
    • 77957956351 scopus 로고    scopus 로고
    • The Pseudomonas aeruginosa patatinlike protein PlpD is the archetype of a novel Type V secretion system
    • Salacha R et al (2010) The Pseudomonas aeruginosa patatinlike protein PlpD is the archetype of a novel Type V secretion system. Environ Microbiol 12(6):1498-1512
    • (2010) Environ Microbiol , vol.12 , Issue.6 , pp. 1498-1512
    • Salacha, R.1
  • 6
    • 84867325507 scopus 로고    scopus 로고
    • Intimin and invasin export their C-terminus to the bacterial cell surface using an inverse mechanism compared to classical autotransport
    • Oberhettinger P et al (2012) Intimin and invasin export their C-terminus to the bacterial cell surface using an inverse mechanism compared to classical autotransport. PLoS ONE 7(10):e47069
    • (2012) PLoS ONE , vol.7 , Issue.10
    • Oberhettinger, P.1
  • 8
    • 48149101623 scopus 로고    scopus 로고
    • Common themes and variations in serine protease autotransporters
    • Yen YT et al (2008) Common themes and variations in serine protease autotransporters. Trends Microbiol 16(8):370-379
    • (2008) Trends Microbiol , vol.16 , Issue.8 , pp. 370-379
    • Yen, Y.T.1
  • 9
    • 63549137674 scopus 로고    scopus 로고
    • Secretion and subcellular localizations of bacterial proteins: A semantic awareness issue
    • Desvaux M et al (2009) Secretion and subcellular localizations of bacterial proteins: a semantic awareness issue. Trends Microbiol 17(4):139-145
    • (2009) Trends Microbiol , vol.17 , Issue.4 , pp. 139-145
    • Desvaux, M.1
  • 10
    • 0034547870 scopus 로고    scopus 로고
    • Autotransporter proteins, evolution and redefining protein secretion: Response
    • Henderson IR, Cappello R, Nataro JP (2000) Autotransporter proteins, evolution and redefining protein secretion: response. Trends Microbiol 8(12):534-535
    • (2000) Trends Microbiol , vol.8 , Issue.12 , pp. 534-535
    • Henderson, I.R.1    Cappello, R.2    Nataro, J.P.3
  • 11
    • 0034255386 scopus 로고    scopus 로고
    • Renaming protein secretion in the gram-negative bacteria
    • Henderson IR et al (2000) Renaming protein secretion in the gram-negative bacteria. Trends Microbiol 8(8):352
    • (2000) Trends Microbiol , vol.8 , Issue.8 , pp. 352
    • Henderson, I.R.1
  • 12
    • 84860719904 scopus 로고    scopus 로고
    • Discovery of an archetypal protein transport system in bacterial outer membranes
    • Selkrig J et al (2012) Discovery of an archetypal protein transport system in bacterial outer membranes. Nat Struct Mol Biol 19(5):506-510
    • (2012) Nat Struct Mol Biol , vol.19 , Issue.5 , pp. 506-510
    • Selkrig, J.1
  • 13
    • 78650039746 scopus 로고    scopus 로고
    • YidC is involved in the biogenesis of the secreted autotransporter hemoglobin protease
    • Jong WS et al (2010) YidC is involved in the biogenesis of the secreted autotransporter hemoglobin protease. J Biol Chem 285(51):39682-39690
    • (2010) J Biol Chem , vol.285 , Issue.51 , pp. 39682-39690
    • Jong, W.S.1
  • 14
    • 70350470007 scopus 로고    scopus 로고
    • Roles of periplasmic chaperone proteins in the biogenesis of serine protease autotransporters of Enterobacteriaceae
    • Ruiz-Perez F et al (2009) Roles of periplasmic chaperone proteins in the biogenesis of serine protease autotransporters of Enterobacteriaceae. J Bacteriol 191(21):6571-6583
    • (2009) J Bacteriol , vol.191 , Issue.21 , pp. 6571-6583
    • Ruiz-Perez, F.1
  • 15
    • 77957678381 scopus 로고    scopus 로고
    • Interaction of FkpA, a peptidyl-prolyl cis/trans isomerase with EspP autotransporter protein
    • Ruiz-Perez F, Henderson IR, Nataro JP (2010) Interaction of FkpA, a peptidyl-prolyl cis/trans isomerase with EspP autotransporter protein. Gut Microbes 1(5):339-344
    • (2010) Gut Microbes , vol.1 , Issue.5 , pp. 339-344
    • Ruiz-Perez, F.1    Henderson, I.R.2    Nataro, J.P.3
  • 16
    • 34547643207 scopus 로고    scopus 로고
    • IcsA surface presentation in Shigella flexneri requires the periplasmic chaperones DegP, Skp, and SurA
    • Purdy GE, Fisher CR, Payne SM (2007) IcsA surface presentation in Shigella flexneri requires the periplasmic chaperones DegP, Skp, and SurA. J Bacteriol 189(15):5566-5573
    • (2007) J Bacteriol , vol.189 , Issue.15 , pp. 5566-5573
    • Purdy, G.E.1    Fisher, C.R.2    Payne, S.M.3
  • 17
    • 73149118024 scopus 로고    scopus 로고
    • Interaction of an autotransporter passenger domain with BamA during its translocation across the bacterial outer membrane
    • Ieva R, Bernstein HD (2009) Interaction of an autotransporter passenger domain with BamA during its translocation across the bacterial outer membrane. Proc Natl Acad Sci USA 106(45):19120-19125
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.45 , pp. 19120-19125
    • Ieva, R.1    Bernstein, H.D.2
  • 18
    • 71449127822 scopus 로고    scopus 로고
    • The Bam (Omp85) complex is involved in secretion of the autotransporter haemoglobin protease
    • Sauri A et al (2009) The Bam (Omp85) complex is involved in secretion of the autotransporter haemoglobin protease. Microbiology 155 (Pt 12):3982-3991
    • (2009) Microbiology , vol.155 , Issue.PART 12 , pp. 3982-3991
    • Sauri, A.1
  • 19
    • 79961225871 scopus 로고    scopus 로고
    • Sequential and spatially restricted interactions of assembly factors with an autotransporter beta domain
    • Ieva R et al (2011) Sequential and spatially restricted interactions of assembly factors with an autotransporter beta domain. Proc Natl Acad Sci USA 108(31):E383-E391
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.31
    • Ieva, R.1
  • 20
    • 34447529326 scopus 로고    scopus 로고
    • Requirement for YaeT in the outer membrane assembly of autotransporter proteins
    • Jain S, Goldberg MB (2007) Requirement for YaeT in the outer membrane assembly of autotransporter proteins. J Bacteriol 189(14):5393-5398
    • (2007) J Bacteriol , vol.189 , Issue.14 , pp. 5393-5398
    • Jain, S.1    Goldberg, M.B.2
  • 21
    • 79961138396 scopus 로고    scopus 로고
    • The essential beta-barrel assembly machinery complex components BamD and BamA are required for autotransporter biogenesis
    • Rossiter AE et al (2011) The essential beta-barrel assembly machinery complex components BamD and BamA are required for autotransporter biogenesis. J Bacteriol 193(16):4250-4253
    • (2011) J Bacteriol , vol.193 , Issue.16 , pp. 4250-4253
    • Rossiter, A.E.1
  • 22
    • 0023128808 scopus 로고
    • Gene structure and extracellular secretion of Neisseria gonorrhoeae IgA protease
    • Pohlner J et al (1987) Gene structure and extracellular secretion of Neisseria gonorrhoeae IgA protease. Nature 325(6103):458-462
    • (1987) Nature , vol.325 , Issue.6103 , pp. 458-462
    • Pohlner, J.1
  • 23
    • 0027136213 scopus 로고
    • Characterization of the Neisseria Iga beta-core. The essential unit for outer membrane targeting and extracellular protein secretion
    • Klauser T et al (1993) Characterization of the Neisseria Iga beta-core. The essential unit for outer membrane targeting and extracellular protein secretion. J Mol Biol 234(3):579-593
    • (1993) J Mol Biol , vol.234 , Issue.3 , pp. 579-593
    • Klauser, T.1
  • 24
    • 35648988968 scopus 로고    scopus 로고
    • Are bacterial 'autotransporters' really transporters?
    • Bernstein HD (2007) Are bacterial 'autotransporters' really transporters? Trends Microbiol 15(10):441-447
    • (2007) Trends Microbiol , vol.15 , Issue.10 , pp. 441-447
    • Bernstein, H.D.1
  • 25
    • 8844235655 scopus 로고    scopus 로고
    • Protein secretion through autotransporter and two-partner pathways
    • Jacob-Dubuisson F, Fernandez R, Coutte L (2004) Protein secretion through autotransporter and two-partner pathways. Biochim Biophys Acta 1694 (1-3):235-257
    • (2004) Biochim Biophys Acta , vol.1694 , Issue.1-3 , pp. 235-257
    • Jacob-Dubuisson, F.1    Fernandez, R.2    Coutte, L.3
  • 26
    • 35848952765 scopus 로고    scopus 로고
    • Protein secretion in gram-negative bacteria via the autotransporter pathway
    • Dautin N, Bernstein HD (2007) Protein secretion in gram-negative bacteria via the autotransporter pathway. Annu Rev Microbiol 61:89-112
    • (2007) Annu Rev Microbiol , vol.61 , pp. 89-112
    • Dautin, N.1    Bernstein, H.D.2
  • 27
    • 84857148914 scopus 로고    scopus 로고
    • From self sufficiency to dependence: Mechanisms and factors important for autotransporter biogenesis
    • Leyton DL, Rossiter AE, Henderson IR (2012) From self sufficiency to dependence: mechanisms and factors important for autotransporter biogenesis. Nat Rev Microbiol 10(3):213-225
    • (2012) Nat Rev Microbiol , vol.10 , Issue.3 , pp. 213-225
    • Leyton, D.L.1    Rossiter, A.E.2    Henderson, I.R.3
  • 28
    • 84858226936 scopus 로고    scopus 로고
    • Type V secretion: Mechanism (s) of autotransport through the bacterial outer membrane
    • Leo JC, Grin I, Linke D (2012) Type V secretion: mechanism (s) of autotransport through the bacterial outer membrane. Philos Trans R Soc Lond B 367(1592):1088-1101
    • (2012) Philos Trans R Soc Lond B , vol.367 , Issue.1592 , pp. 1088-1101
    • Leo, J.C.1    Grin, I.2    Linke, D.3
  • 29
    • 0037799238 scopus 로고    scopus 로고
    • Signal recognition particle (SRP)-mediated targeting and Sec-dependent translocation of an extracellular Escherichia coli protein
    • Sijbrandi R et al (2003) Signal recognition particle (SRP)-mediated targeting and Sec-dependent translocation of an extracellular Escherichia coli protein. J Biol Chem 278(7):4654-4659
    • (2003) J Biol Chem , vol.278 , Issue.7 , pp. 4654-4659
    • Sijbrandi, R.1
  • 30
    • 11844280919 scopus 로고    scopus 로고
    • An unusual signal peptide facilitates late steps in the biogenesis of a bacterial autotransporter
    • Szabady RL et al (2005) An unusual signal peptide facilitates late steps in the biogenesis of a bacterial autotransporter. Proc Natl Acad Sci USA 102(1):221-226
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.1 , pp. 221-226
    • Szabady, R.L.1
  • 31
    • 60649098853 scopus 로고    scopus 로고
    • Vectorial transport and folding of an autotransporter virulence protein during outer membrane secretion
    • Junker M, Besingi RN, Clark PL (2009) Vectorial transport and folding of an autotransporter virulence protein during outer membrane secretion. Mol Microbiol 71(5):1323-1332
    • (2009) Mol Microbiol , vol.71 , Issue.5 , pp. 1323-1332
    • Junker, M.1    Besingi, R.N.2    Clark, P.L.3
  • 32
    • 78049313288 scopus 로고    scopus 로고
    • Secretion of a bacterial virulence factor is driven by the folding of a C-terminal segment
    • Peterson JH et al (2010) Secretion of a bacterial virulence factor is driven by the folding of a C-terminal segment. Proc Natl Acad Sci USA 107(41):17739-17744
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.41 , pp. 17739-17744
    • Peterson, J.H.1
  • 33
    • 84857175966 scopus 로고    scopus 로고
    • ATP-independent control of autotransporter virulence protein transport via the folding properties of the secreted protein
    • Renn JP et al (2012) ATP-independent control of autotransporter virulence protein transport via the folding properties of the secreted protein. Chem Biol 19(2):287-296
    • (2012) Chem Biol , vol.19 , Issue.2 , pp. 287-296
    • Renn, J.P.1
  • 34
    • 33645525759 scopus 로고    scopus 로고
    • Pertactin beta-helix folding mechanism suggests common themes for the secretion and folding of autotransporter proteins
    • Junker M et al (2006) Pertactin beta-helix folding mechanism suggests common themes for the secretion and folding of autotransporter proteins. Proc Natl Acad Sci USA 103(13):4918-4923
    • (2006) Proc Natl Acad Sci USA , vol.103 , Issue.13 , pp. 4918-4923
    • Junker, M.1
  • 35
    • 42249109450 scopus 로고    scopus 로고
    • Serine peptidases: Classification, structure and function
    • Page MJ, Di Cera E (2008) Serine peptidases: classification, structure and function. Cell Mol Life Sci 65 (7-8):1220-1236
    • (2008) Cell Mol Life Sci , vol.65 , Issue.7-8 , pp. 1220-1236
    • Page, M.J.1    Di Cera, E.2
  • 36
    • 84859426282 scopus 로고    scopus 로고
    • MEROPS: The database of proteolytic enzymes, their substrates and inhibitors
    • Database issue
    • Rawlings ND, Barrett AJ, Bateman A (2012) MEROPS: the database of proteolytic enzymes, their substrates and inhibitors. Nucleic Acids Res 40 (Database issue):D343-D350
    • (2012) Nucleic Acids Res , vol.40
    • Rawlings, N.D.1    Barrett, A.J.2    Bateman, A.3
  • 38
    • 78649888930 scopus 로고    scopus 로고
    • Serine protease autotransporters of Enterobacteriaceae (SPATEs): Biogenesis and function
    • Dautin N (2010) Serine protease autotransporters of Enterobacteriaceae (SPATEs): biogenesis and function. Toxins (Basel) 2(6):1179-1206
    • (2010) Toxins (Basel) , vol.2 , Issue.6 , pp. 1179-1206
    • Dautin, N.1
  • 39
    • 34548481341 scopus 로고    scopus 로고
    • Contribution of a novel gene, rpeA, encoding a putative autotransporter adhesin to intestinal colonization by rabbit-specific enteropathogenic Escherichia coli
    • Leyton DL et al (2007) Contribution of a novel gene, rpeA, encoding a putative autotransporter adhesin to intestinal colonization by rabbit-specific enteropathogenic Escherichia coli. Infect Immun 75(9):4664-4669
    • (2007) Infect Immun , vol.75 , Issue.9 , pp. 4664-4669
    • Leyton, D.L.1
  • 40
    • 34247238897 scopus 로고    scopus 로고
    • Cleavage of a bacterial autotransporter by an evolutionarily convergent autocatalytic mechanism
    • Dautin N et al (2007) Cleavage of a bacterial autotransporter by an evolutionarily convergent autocatalytic mechanism. EMBO J 26(7):1942-1952
    • (2007) EMBO J , vol.26 , Issue.7 , pp. 1942-1952
    • Dautin, N.1
  • 41
    • 84855287863 scopus 로고    scopus 로고
    • Molecular basis for the activation of a catalytic asparagine residue in a self-cleaving bacterial autotransporter
    • Barnard TJ et al (2012) Molecular basis for the activation of a catalytic asparagine residue in a self-cleaving bacterial autotransporter. J Mol Biol 415(1):128-142
    • (2012) J Mol Biol , vol.415 , Issue.1 , pp. 128-142
    • Barnard, T.J.1
  • 42
    • 77956916073 scopus 로고    scopus 로고
    • A novel intein-like autoproteolytic mechanism in autotransporter proteins
    • Tajima N et al (2010) A novel intein-like autoproteolytic mechanism in autotransporter proteins. J Mol Biol 402(4):645-656
    • (2010) J Mol Biol , vol.402 , Issue.4 , pp. 645-656
    • Tajima, N.1
  • 43
    • 20444435483 scopus 로고    scopus 로고
    • Crystal structure of hemoglobin protease, a heme binding autotransporter protein from pathogenic Escherichia coli
    • Otto BR et al (2005) Crystal structure of hemoglobin protease, a heme binding autotransporter protein from pathogenic Escherichia coli. J Biol Chem 280(17):17339-17345
    • (2005) J Biol Chem , vol.280 , Issue.17 , pp. 17339-17345
    • Otto, B.R.1
  • 44
    • 0029988488 scopus 로고    scopus 로고
    • Structure of Bordetella pertussis virulence factor P.69 pertactin
    • Emsley P et al (1996) Structure of Bordetella pertussis virulence factor P.69 pertactin. Nature 381(6577):90-92
    • (1996) Nature , vol.381 , Issue.6577 , pp. 90-92
    • Emsley, P.1
  • 45
    • 65649092581 scopus 로고    scopus 로고
    • Active-site gating regulates substrate selectivity in a chymotrypsin-like serine protease the structure of Haemophilus influenzae immunoglobulin A1 protease
    • Johnson TA et al (2009) Active-site gating regulates substrate selectivity in a chymotrypsin-like serine protease the structure of Haemophilus influenzae immunoglobulin A1 protease. J Mol Biol 389(3):559-574
    • (2009) J Mol Biol , vol.389 , Issue.3 , pp. 559-574
    • Johnson, T.A.1
  • 46
    • 80052722849 scopus 로고    scopus 로고
    • Crystal structure of the Haemophilus influenzae Hap adhesin reveals an intercellular oligomerization mechanism for bacterial aggregation
    • Meng G et al (2011) Crystal structure of the Haemophilus influenzae Hap adhesin reveals an intercellular oligomerization mechanism for bacterial aggregation. EMBO J 30(18):3864-3874
    • (2011) EMBO J , vol.30 , Issue.18 , pp. 3864-3874
    • Meng, G.1
  • 47
    • 36048946721 scopus 로고    scopus 로고
    • Crystal structure of the Helicobacter pylori vacuolating toxin p55 domain
    • Gangwer KA et al (2007) Crystal structure of the Helicobacter pylori vacuolating toxin p55 domain. Proc Natl Acad Sci USA 104(41):16293-16298
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.41 , pp. 16293-16298
    • Gangwer, K.A.1
  • 48
    • 77949323924 scopus 로고    scopus 로고
    • Crystal structure of a full-length autotransporter
    • Van Den Berg B (2010) Crystal structure of a full-length autotransporter. J Mol Biol 396(3):627-633
    • (2010) J Mol Biol , vol.396 , Issue.3 , pp. 627-633
    • Van Den Berg, B.1
  • 49
    • 84865048949 scopus 로고    scopus 로고
    • A bioinformatic strategy for the detection, classification and analysis of bacterial autotransporters
    • Celik N et al (2012) A bioinformatic strategy for the detection, classification and analysis of bacterial autotransporters. PLoS ONE 7(8):e43245
    • (2012) PLoS ONE , vol.7 , Issue.8
    • Celik, N.1
  • 50
    • 0037338681 scopus 로고    scopus 로고
    • A conserved region within the Bordetella pertussis autotransporter BrkA is necessary for folding of its passenger domain
    • Oliver DC et al (2003) A conserved region within the Bordetella pertussis autotransporter BrkA is necessary for folding of its passenger domain. Mol Microbiol 47(5):1367-1383
    • (2003) Mol Microbiol , vol.47 , Issue.5 , pp. 1367-1383
    • Oliver, D.C.1
  • 51
    • 77957121300 scopus 로고    scopus 로고
    • Bacterial macroscopic ropelike fibers with cytopathic and adhesive properties
    • Xicohtencatl-Cortes J et al (2010) Bacterial macroscopic ropelike fibers with cytopathic and adhesive properties. J Biol Chem 285(42):32336-32342
    • (2010) J Biol Chem , vol.285 , Issue.42 , pp. 32336-32342
    • Xicohtencatl-Cortes, J.1
  • 52
    • 33745875356 scopus 로고    scopus 로고
    • Self-associating autotransporters, SAATs: Functional and structural similarities
    • Klemm P, Vejborg RM, Sherlock O (2006) Self-associating autotransporters, SAATs: functional and structural similarities. Int J Med Microbiol 296 (4-5):187-195
    • (2006) Int J Med Microbiol , vol.296 , Issue.4-5 , pp. 187-195
    • Klemm, P.1    Vejborg, R.M.2    Sherlock, O.3
  • 53
    • 78649833347 scopus 로고    scopus 로고
    • Role of domains within the autotransporter Hbp/Tsh
    • Nishimura K et al (2010) Role of domains within the autotransporter Hbp/Tsh. Acta Crystallogr D Biol Crystallogr 66 (Pt 12):1295-1300
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , Issue.PART 12 , pp. 1295-1300
    • Nishimura, K.1
  • 54
    • 80855139532 scopus 로고    scopus 로고
    • Crystal structure of the passenger domain of the Escherichia coli autotransporter EspP
    • Khan S et al (2011) Crystal structure of the passenger domain of the Escherichia coli autotransporter EspP. J Mol Biol 413(5):985-1000
    • (2011) J Mol Biol , vol.413 , Issue.5 , pp. 985-1000
    • Khan, S.1
  • 55
    • 82755163015 scopus 로고    scopus 로고
    • Size and conformation limits to secretion of disulfide-bonded loops in autotransporter proteins
    • Leyton DL et al (2011) Size and conformation limits to secretion of disulfide-bonded loops in autotransporter proteins. J Biol Chem 286(49):42283-42291
    • (2011) J Biol Chem , vol.286 , Issue.49 , pp. 42283-42291
    • Leyton, D.L.1
  • 56
    • 0036893427 scopus 로고    scopus 로고
    • Functional comparison of serine protease autotransporters of enterobacteriaceae
    • Dutta PR et al (2002) Functional comparison of serine protease autotransporters of enterobacteriaceae. Infect Immun 70(12):7105-7113
    • (2002) Infect Immun , vol.70 , Issue.12 , pp. 7105-7113
    • Dutta, P.R.1
  • 57
    • 55849083511 scopus 로고    scopus 로고
    • RegA, an AraC-like protein, is a global transcriptional regulator that controls virulence gene expression in Citrobacter rodentium
    • Hart E et al (2008) RegA, an AraC-like protein, is a global transcriptional regulator that controls virulence gene expression in Citrobacter rodentium. Infect Immun 76(11):5247-5256
    • (2008) Infect Immun , vol.76 , Issue.11 , pp. 5247-5256
    • Hart, E.1
  • 58
    • 0018897472 scopus 로고
    • Species specificity of in vitro Escherichia coli adherence to host intestinal cell membranes and its correlation with in vivo colonization and infectivity
    • Cheney CP et al (1980) Species specificity of in vitro Escherichia coli adherence to host intestinal cell membranes and its correlation with in vivo colonization and infectivity. Infect Immun 28(3):1019-1027
    • (1980) Infect Immun , vol.28 , Issue.3 , pp. 1019-1027
    • Cheney, C.P.1
  • 59
    • 80052517376 scopus 로고    scopus 로고
    • Genome sequence of a porcine extraintestinal pathogenic Escherichia coli strain
    • Tan C et al (2011) Genome sequence of a porcine extraintestinal pathogenic Escherichia coli strain. J Bacteriol 193(18):5038
    • (2011) J Bacteriol , vol.193 , Issue.18 , pp. 5038
    • Tan, C.1
  • 60
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: A webbased environment for protein structure homology modelling
    • Arnold K et al (2006) The SWISS-MODEL workspace: a webbased environment for protein structure homology modelling. Bioinformatics 22(2):195-201
    • (2006) Bioinformatics , vol.22 , Issue.2 , pp. 195-201
    • Arnold, K.1
  • 61
    • 79961216328 scopus 로고    scopus 로고
    • Serine protease autotransporters from Shigella flexneri and pathogenic Escherichia coli target a broad range of leukocyte glycoproteins
    • Ruiz-Perez F et al (2011) Serine protease autotransporters from Shigella flexneri and pathogenic Escherichia coli target a broad range of leukocyte glycoproteins. Proc Natl Acad Sci USA 108(31):12881-12886
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.31 , pp. 12881-12886
    • Ruiz-Perez, F.1
  • 62
    • 0141891157 scopus 로고    scopus 로고
    • Structure-function analysis of the enteroaggregative Escherichia coli plasmid-encoded toxin autotransporter using scanning linker mutagenesis
    • Dutta PR, Sui BQ, Nataro JP (2003) Structure-function analysis of the enteroaggregative Escherichia coli plasmid-encoded toxin autotransporter using scanning linker mutagenesis. J Biol Chem 278(41):39912-39920
    • (2003) J Biol Chem , vol.278 , Issue.41 , pp. 39912-39920
    • Dutta, P.R.1    Sui, B.Q.2    Nataro, J.P.3
  • 63
    • 0032881401 scopus 로고    scopus 로고
    • Involvement of the enteroaggregative Escherichia coli plasmid-encoded toxin in causing human intestinal damage
    • Henderson IR et al (1999) Involvement of the enteroaggregative Escherichia coli plasmid-encoded toxin in causing human intestinal damage. Infect Immun 67(10):5338-5344
    • (1999) Infect Immun , vol.67 , Issue.10 , pp. 5338-5344
    • Henderson, I.R.1
  • 64
    • 77949497864 scopus 로고    scopus 로고
    • The immunogenic SigA enterotoxin of Shigella flexneri 2a binds to HEp-2 cells and induces fodrin redistribution in intoxicated epithelial cells
    • Al-Hasani K et al (2009) The immunogenic SigA enterotoxin of Shigella flexneri 2a binds to HEp-2 cells and induces fodrin redistribution in intoxicated epithelial cells. PLoS ONE 4(12):e8223
    • (2009) PLoS ONE , vol.4 , Issue.12
    • Al-Hasani, K.1
  • 65
    • 2542576380 scopus 로고    scopus 로고
    • The serine protease motif of EspC from enteropathogenic Escherichia coli produces epithelial damage by a mechanism different from that of Pet toxin from enteroaggregative E coli
    • Navarro-Garcia F et al (2004) The serine protease motif of EspC from enteropathogenic Escherichia coli produces epithelial damage by a mechanism different from that of Pet toxin from enteroaggregative E. coli. Infect Immun 72(6):3609-3621
    • (2004) Infect Immun , vol.72 , Issue.6 , pp. 3609-3621
    • Navarro-Garcia, F.1
  • 66
    • 0037678811 scopus 로고    scopus 로고
    • Fodrin CaMbinding domain cleavage by Pet from enteroaggregative Escherichia coli leads to actin cytoskeletal disruption
    • Canizalez-Roman A, Navarro-Garcia F (2003) Fodrin CaMbinding domain cleavage by Pet from enteroaggregative Escherichia coli leads to actin cytoskeletal disruption. Mol Microbiol 48(4):947-958
    • (2003) Mol Microbiol , vol.48 , Issue.4 , pp. 947-958
    • Canizalez-Roman, A.1    Navarro-Garcia, F.2
  • 67
    • 33750475609 scopus 로고    scopus 로고
    • Protease activity, secretion, cell entry, cytotoxicity, and cellular targets of secreted autotransporter toxin of uropathogenic Escherichia coli
    • Maroncle NM et al (2006) Protease activity, secretion, cell entry, cytotoxicity, and cellular targets of secreted autotransporter toxin of uropathogenic Escherichia coli. Infect Immun 74(11):6124-6134
    • (2006) Infect Immun , vol.74 , Issue.11 , pp. 6124-6134
    • Maroncle, N.M.1
  • 68
    • 66549128947 scopus 로고    scopus 로고
    • The Pic protease of enteroaggregative Escherichia coli promotes intestinal colonization and growth in the presence of mucin
    • Harrington SM et al (2009) The Pic protease of enteroaggregative Escherichia coli promotes intestinal colonization and growth in the presence of mucin. Infect Immun 77(6):2465-2473
    • (2009) Infect Immun , vol.77 , Issue.6 , pp. 2465-2473
    • Harrington, S.M.1
  • 69
    • 0032734808 scopus 로고    scopus 로고
    • Characterization of pic, a secreted protease of Shigella flexneri and enteroaggregative Escherichia coli
    • Henderson IR et al (1999) Characterization of pic, a secreted protease of Shigella flexneri and enteroaggregative Escherichia coli. Infect Immun 67(11):5587-5596
    • (1999) Infect Immun , vol.67 , Issue.11 , pp. 5587-5596
    • Henderson, I.R.1
  • 70
    • 0242286559 scopus 로고    scopus 로고
    • Transfer region of pO113 from enterohemorrhagic Escherichia coli: Similarity with R64 and identification of a novel plasmid-encoded autotransporter, EpeA
    • Leyton DL et al (2003) Transfer region of pO113 from enterohemorrhagic Escherichia coli: similarity with R64 and identification of a novel plasmid-encoded autotransporter, EpeA. Infect Immun 71(11):6307-6319
    • (2003) Infect Immun , vol.71 , Issue.11 , pp. 6307-6319
    • Leyton, D.L.1
  • 71
    • 59649109832 scopus 로고    scopus 로고
    • Short report: High prevalence of serine protease autotransporter cytotoxins among strains of enteroaggregative Escherichia coli
    • Boisen N et al (2009) Short report: high prevalence of serine protease autotransporter cytotoxins among strains of enteroaggregative Escherichia coli. Am J Trop Med Hyg 80(2):294-301
    • (2009) Am J Trop Med Hyg , vol.80 , Issue.2 , pp. 294-301
    • Boisen, N.1
  • 72
    • 80052150179 scopus 로고    scopus 로고
    • Origins of the E coli strain causing an outbreak of hemolytic-uremic syndrome in Germany
    • Rasko DA et al (2011) Origins of the E. coli strain causing an outbreak of hemolytic-uremic syndrome in Germany. N Engl J Med 365(8):709-717
    • (2011) N Engl J Med , vol.365 , Issue.8 , pp. 709-717
    • Rasko, D.A.1
  • 73
    • 0347823003 scopus 로고    scopus 로고
    • MatGAT: An application that generates similarity/identity matrices using protein or DNA sequences
    • Campanella JJ, Bitincka L, Smalley J (2003) MatGAT: an application that generates similarity/identity matrices using protein or DNA sequences. BMC Bioinf 4:29
    • (2003) BMC Bioinf , vol.4 , pp. 29
    • Campanella, J.J.1    Bitincka, L.2    Smalley, J.3
  • 74
    • 0030817859 scopus 로고    scopus 로고
    • Use of a novel approach, termed island probing, identifies the Shigella flexneri she pathogenicity island which encodes a homolog of the immunoglobulin A protease-like family of proteins
    • Rajakumar K, Sasakawa C, Adler B (1997) Use of a novel approach, termed island probing, identifies the Shigella flexneri she pathogenicity island which encodes a homolog of the immunoglobulin A protease-like family of proteins. Infect Immun 65(11):4606-4614
    • (1997) Infect Immun , vol.65 , Issue.11 , pp. 4606-4614
    • Rajakumar, K.1    Sasakawa, C.2    Adler, B.3
  • 75
    • 0346492803 scopus 로고    scopus 로고
    • PicU, a second serine protease autotransporter of uropathogenic Escherichia coli
    • Parham NJ et al (2004) PicU, a second serine protease autotransporter of uropathogenic Escherichia coli. FEMS Microbiol Lett 230(1):73-83
    • (2004) FEMS Microbiol Lett , vol.230 , Issue.1 , pp. 73-83
    • Parham, N.J.1
  • 76
    • 0348141893 scopus 로고    scopus 로고
    • Autotransporter genes pic and tsh are associated with Escherichia coli strains that cause acute pyelonephritis and are expressed during urinary tract infection
    • Heimer SR et al (2004) Autotransporter genes pic and tsh are associated with Escherichia coli strains that cause acute pyelonephritis and are expressed during urinary tract infection. Infect Immun 72(1):593-597
    • (2004) Infect Immun , vol.72 , Issue.1 , pp. 593-597
    • Heimer, S.R.1
  • 77
    • 0032919350 scopus 로고    scopus 로고
    • Virulence properties of Escherichia coli 83972, a prototype strain associated with asymptomatic bacteriuria
    • Hull RA et al (1999) Virulence properties of Escherichia coli 83972, a prototype strain associated with asymptomatic bacteriuria. Infect Immun 67(1):429-432
    • (1999) Infect Immun , vol.67 , Issue.1 , pp. 429-432
    • Hull, R.A.1
  • 78
    • 0032915332 scopus 로고    scopus 로고
    • Characterization of the avian pathogenic Escherichia coli hemagglutinin Tsh, a member of the immunoglobulin A protease-type family of autotransporters
    • Stathopoulos C, Provence DL, Curtiss R 3rd (1999) Characterization of the avian pathogenic Escherichia coli hemagglutinin Tsh, a member of the immunoglobulin A protease-type family of autotransporters. Infect Immun 67(2):772-781
    • (1999) Infect Immun , vol.67 , Issue.2 , pp. 772-781
    • Stathopoulos, C.1    Provence, D.L.2    Curtiss III, R.3
  • 79
    • 0032555939 scopus 로고    scopus 로고
    • Characterization of a hemoglobin protease secreted by the pathogenic Escherichia coli strain EB1
    • Otto BR et al (1998) Characterization of a hemoglobin protease secreted by the pathogenic Escherichia coli strain EB1. J Exp Med 188(6):1091-1103
    • (1998) J Exp Med , vol.188 , Issue.6 , pp. 1091-1103
    • Otto, B.R.1
  • 80
    • 0041823436 scopus 로고    scopus 로고
    • A novel pathogenicity island integrated adjacent to the thrW tRNA gene of avian pathogenic Escherichia coli encodes a vacuolating autotransporter toxin
    • Parreira VR, Gyles CL (2003) A novel pathogenicity island integrated adjacent to the thrW tRNA gene of avian pathogenic Escherichia coli encodes a vacuolating autotransporter toxin. Infect Immun 71(9):5087-5096
    • (2003) Infect Immun , vol.71 , Issue.9 , pp. 5087-5096
    • Parreira, V.R.1    Gyles, C.L.2
  • 81
    • 23744456016 scopus 로고    scopus 로고
    • Distribution of the serine protease autotransporters of the Enterobacteriaceae among extraintestinal clinical isolates of Escherichia coli
    • Parham NJ et al (2005) Distribution of the serine protease autotransporters of the Enterobacteriaceae among extraintestinal clinical isolates of Escherichia coli. J Clin Microbiol 43(8):4076-4082
    • (2005) J Clin Microbiol , vol.43 , Issue.8 , pp. 4076-4082
    • Parham, N.J.1
  • 82
    • 77952692819 scopus 로고    scopus 로고
    • Identification of protective and broadly conserved vaccine antigens from the genome of extraintestinal pathogenic Escherichia coli
    • Moriel DG et al (2010) Identification of protective and broadly conserved vaccine antigens from the genome of extraintestinal pathogenic Escherichia coli. Proc Natl Acad Sci USA 107(20):9072-9077
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.20 , pp. 9072-9077
    • Moriel, D.G.1
  • 83
    • 80052337291 scopus 로고    scopus 로고
    • Salmonella bongori provides insights into the evolution of the Salmonellae
    • Fookes M et al (2011) Salmonella bongori provides insights into the evolution of the Salmonellae. PLoS Pathog 7(8):e1002191
    • (2011) PLoS Pathog , vol.7 , Issue.8
    • Fookes, M.1
  • 84
    • 79961163061 scopus 로고    scopus 로고
    • Genome of multidrug-resistant uropathogenic Escherichia coli strain NA114 from India
    • Avasthi TS et al (2011) Genome of multidrug-resistant uropathogenic Escherichia coli strain NA114 from India. J Bacteriol 193(16):4272-4273
    • (2011) J Bacteriol , vol.193 , Issue.16 , pp. 4272-4273
    • Avasthi, T.S.1
  • 85
    • 0034066697 scopus 로고    scopus 로고
    • Four different genes responsible for nonimmune immunoglobulin-binding activities within a single strain of Escherichia coli
    • Sandt CH, Hill CW (2000) Four different genes responsible for nonimmune immunoglobulin-binding activities within a single strain of Escherichia coli. Infect Immun 68(4):2205-2214
    • (2000) Infect Immun , vol.68 , Issue.4 , pp. 2205-2214
    • Sandt, C.H.1    Hill, C.W.2
  • 86
    • 75749094779 scopus 로고    scopus 로고
    • Complete genome sequence of the wild-type commensal Escherichia coli strain SE15, belonging to phylogenetic group B2
    • Toh H et al (2010) Complete genome sequence of the wild-type commensal Escherichia coli strain SE15, belonging to phylogenetic group B2. J Bacteriol 192(4):1165-1166
    • (2010) J Bacteriol , vol.192 , Issue.4 , pp. 1165-1166
    • Toh, H.1
  • 87
    • 1342281315 scopus 로고    scopus 로고
    • Identification and molecular characterization of EatA, an autotransporter protein of enterotoxigenic Escherichia coli
    • Patel SK et al (2004) Identification and molecular characterization of EatA, an autotransporter protein of enterotoxigenic Escherichia coli. Infect Immun 72(3):1786-1794
    • (2004) Infect Immun , vol.72 , Issue.3 , pp. 1786-1794
    • Patel, S.K.1
  • 88
    • 0034778453 scopus 로고    scopus 로고
    • Identification and characterization of a novel genomic island integrated at selC in locus of enterocyte effacement-negative, Shiga toxin-producing Escherichia coli
    • Schmidt H et al (2001) Identification and characterization of a novel genomic island integrated at selC in locus of enterocyte effacement-negative, Shiga toxin-producing Escherichia coli. Infect Immun 69(11):6863-6873
    • (2001) Infect Immun , vol.69 , Issue.11 , pp. 6863-6873
    • Schmidt, H.1
  • 89
    • 0031844794 scopus 로고    scopus 로고
    • Pet, an autotransporter enterotoxin from enteroaggregative Escherichia coli
    • Eslava C et al (1998) Pet, an autotransporter enterotoxin from enteroaggregative Escherichia coli. Infect Immun 66(7):3155-3163
    • (1998) Infect Immun , vol.66 , Issue.7 , pp. 3155-3163
    • Eslava, C.1
  • 90
    • 0034064649 scopus 로고    scopus 로고
    • The sigA gene which is borne on the she pathogenicity island of Shigella flexneri 2a encodes an exported cytopathic protease involved in intestinal fluid accumulation
    • Al-Hasani K et al (2000) The sigA gene which is borne on the she pathogenicity island of Shigella flexneri 2a encodes an exported cytopathic protease involved in intestinal fluid accumulation. Infect Immun 68(5):2457-2463
    • (2000) Infect Immun , vol.68 , Issue.5 , pp. 2457-2463
    • Al-Hasani, K.1
  • 91
    • 0033810425 scopus 로고    scopus 로고
    • Identification of sat, an autotransporter toxin produced by uropathogenic Escherichia coli
    • Guyer DM et al (2000) Identification of sat, an autotransporter toxin produced by uropathogenic Escherichia coli. Mol Microbiol 38(1):53-66
    • (2000) Mol Microbiol , vol.38 , Issue.1 , pp. 53-66
    • Guyer, D.M.1
  • 92
    • 0030917724 scopus 로고    scopus 로고
    • EspP, a novel extracellular serine protease of enterohaemorrhagic Escherichia coli O157:H7 cleaves human coagulation factor V
    • Brunder W, Schmidt H, Karch H (1997) EspP, a novel extracellular serine protease of enterohaemorrhagic Escherichia coli O157:H7 cleaves human coagulation factor V. Mol Microbiol 24(4):767-778
    • (1997) Mol Microbiol , vol.24 , Issue.4 , pp. 767-778
    • Brunder, W.1    Schmidt, H.2    Karch, H.3
  • 93
    • 0030799018 scopus 로고    scopus 로고
    • Characterization of an exported protease from Shiga toxin-producing Escherichia coli
    • Djafari S et al (1997) Characterization of an exported protease from Shiga toxin-producing Escherichia coli. Mol Microbiol 25(4):771-784
    • (1997) Mol Microbiol , vol.25 , Issue.4 , pp. 771-784
    • Djafari, S.1
  • 94
    • 0032948817 scopus 로고    scopus 로고
    • Cytoskeletal effects induced by pet, the serine protease enterotoxin of enteroaggregative Escherichia coli
    • Navarro-Garcia F et al (1999) Cytoskeletal effects induced by pet, the serine protease enterotoxin of enteroaggregative Escherichia coli. Infect Immun 67(5):2184-2192
    • (1999) Infect Immun , vol.67 , Issue.5 , pp. 2184-2192
    • Navarro-Garcia, F.1
  • 95
    • 0035158936 scopus 로고    scopus 로고
    • EspC pathogenicity island of enteropathogenic Escherichia coli encodes an enterotoxin
    • Mellies JL et al (2001) espC pathogenicity island of enteropathogenic Escherichia coli encodes an enterotoxin. Infect Immun 69(1):315-324
    • (2001) Infect Immun , vol.69 , Issue.1 , pp. 315-324
    • Mellies, J.L.1
  • 96
    • 80052335144 scopus 로고    scopus 로고
    • Complete genome sequence of the Crohn's disease-associated adherent-invasive Escherichia coli strain HM605
    • Clarke DJ et al (2011) Complete genome sequence of the Crohn's disease-associated adherent-invasive Escherichia coli strain HM605. J Bacteriol 193(17):4540
    • (2011) J Bacteriol , vol.193 , Issue.17 , pp. 4540
    • Clarke, D.J.1
  • 97
    • 0037012970 scopus 로고    scopus 로고
    • Protein-translocating outer membrane porins of Gram-negative bacteria
    • Yen MR et al (2002) Protein-translocating outer membrane porins of Gram-negative bacteria. Biochim Biophys Acta 1562 (1-2):6-31
    • (2002) Biochim Biophys Acta , vol.1562 , Issue.1-2 , pp. 6-31
    • Yen, M.R.1
  • 98
    • 77649289609 scopus 로고    scopus 로고
    • Complete genome sequence and comparative metabolic profiling of the prototypical enteroaggregative Escherichia coli strain 042
    • Chaudhuri RR et al (2010) Complete genome sequence and comparative metabolic profiling of the prototypical enteroaggregative Escherichia coli strain 042. PLoS ONE 5(1):e8801
    • (2010) PLoS ONE , vol.5 , Issue.1
    • Chaudhuri, R.R.1
  • 99
    • 35448996075 scopus 로고    scopus 로고
    • Subtypes of the plasmid-encoded serine protease EspP in Shiga toxin-producing Escherichia coli: Distribution, secretion, and proteolytic activity
    • Brockmeyer J et al (2007) Subtypes of the plasmid-encoded serine protease EspP in Shiga toxin-producing Escherichia coli: distribution, secretion, and proteolytic activity. Appl Environ Microbiol 73(20):6351-6359
    • (2007) Appl Environ Microbiol , vol.73 , Issue.20 , pp. 6351-6359
    • Brockmeyer, J.1
  • 100
    • 0034947069 scopus 로고    scopus 로고
    • Evolution of an autotransporter: Domain shuffling and lateral transfer from pathogenic Haemophilus to Neisseria
    • Davis J et al (2001) Evolution of an autotransporter: domain shuffling and lateral transfer from pathogenic Haemophilus to Neisseria. J Bacteriol 183(15):4626-4635
    • (2001) J Bacteriol , vol.183 , Issue.15 , pp. 4626-4635
    • Davis, J.1
  • 101
    • 84864096615 scopus 로고    scopus 로고
    • Identification and mechanism of evolution of new alleles coding for the AIDA-I autotransporter of porcine pathogenic Escherichia coli
    • Cote JP et al (2012) Identification and mechanism of evolution of new alleles coding for the AIDA-I autotransporter of porcine pathogenic Escherichia coli. Appl Environ Microbiol 78(13):4597-4605
    • (2012) Appl Environ Microbiol , vol.78 , Issue.13 , pp. 4597-4605
    • Cote, J.P.1
  • 102
    • 79952050309 scopus 로고    scopus 로고
    • Host-toxin interactions involving EspC and Pet, two serine protease autotransporters of the Enterobacteriaceae
    • Navarro-Garcia F, Sonnested M, Teter K (2010) Host-toxin interactions involving EspC and Pet, two serine protease autotransporters of the Enterobacteriaceae. Toxins (Basel) 2(5):1134-1147
    • (2010) Toxins (Basel) , vol.2 , Issue.5 , pp. 1134-1147
    • Navarro-Garcia, F.1    Sonnested, M.2    Teter, K.3
  • 103
    • 23944436431 scopus 로고    scopus 로고
    • Secreted autotransporter toxin produced by a diffusely adhering Escherichia coli strain causes intestinal damage in animal model assays
    • Taddei CR et al (2005) Secreted autotransporter toxin produced by a diffusely adhering Escherichia coli strain causes intestinal damage in animal model assays. FEMS Microbiol Lett 250(2):263-269
    • (2005) FEMS Microbiol Lett , vol.250 , Issue.2 , pp. 263-269
    • Taddei, C.R.1
  • 104
    • 47049125726 scopus 로고    scopus 로고
    • The serine protease motif of Pic mediates a dose-dependent mucolytic activity after binding to sugar constituents of the mucin substrate
    • Gutierrez-Jimenez J, Arciniega I, Navarro-Garcia F (2008) The serine protease motif of Pic mediates a dose-dependent mucolytic activity after binding to sugar constituents of the mucin substrate. Microb Pathog 45(2):115-123
    • (2008) Microb Pathog , vol.45 , Issue.2 , pp. 115-123
    • Gutierrez-Jimenez, J.1    Arciniega, I.2    Navarro-Garcia, F.3
  • 105
    • 63549144223 scopus 로고    scopus 로고
    • Serine protease espP subtype alpha, but not beta or gamma, of Shiga toxin-producing Escherichia coli is associated with highly pathogenic serogroups
    • Khan AB et al (2009) Serine protease espP subtype alpha, but not beta or gamma, of Shiga toxin-producing Escherichia coli is associated with highly pathogenic serogroups. Int J Med Microbiol 299(4):247-254
    • (2009) Int J Med Microbiol , vol.299 , Issue.4 , pp. 247-254
    • Khan, A.B.1
  • 106
    • 84872177985 scopus 로고    scopus 로고
    • Prevalence, biogenesis, and functionality of the serine protease autotransporter EspP
    • Weiss A, Brockmeyer J (2013) Prevalence, biogenesis, and functionality of the serine protease autotransporter EspP. Toxins (Basel) 5(1):25-48
    • (2013) Toxins (Basel) , vol.5 , Issue.1 , pp. 25-48
    • Weiss, A.1    Brockmeyer, J.2
  • 107
    • 84864818874 scopus 로고    scopus 로고
    • VirK is a periplasmic protein required for efficient secretion of plasmid-encoded toxin from enteroaggregative Escherichia coli
    • Tapia-Pastrana G et al (2012) VirK is a periplasmic protein required for efficient secretion of plasmid-encoded toxin from enteroaggregative Escherichia coli. Infect Immun 80(7):2276-2285
    • (2012) Infect Immun , vol.80 , Issue.7 , pp. 2276-2285
    • Tapia-Pastrana, G.1
  • 108
    • 74249112624 scopus 로고    scopus 로고
    • A host-specific factor is necessary for efficient folding of the autotransporter plasmid-encoded toxin
    • Nemec KN et al (2010) A host-specific factor is necessary for efficient folding of the autotransporter plasmid-encoded toxin. Biochimie 92(2):171-177
    • (2010) Biochimie , vol.92 , Issue.2 , pp. 171-177
    • Nemec, K.N.1
  • 109
    • 77957726552 scopus 로고    scopus 로고
    • EspP, a serine protease of enterohemorrhagic Escherichia coli, impairs complement activation by cleaving complement factors C3/C3b and C5
    • Orth D et al (2010) EspP, a serine protease of enterohemorrhagic Escherichia coli, impairs complement activation by cleaving complement factors C3/C3b and C5. Infect Immun 78(10):4294-4301
    • (2010) Infect Immun , vol.78 , Issue.10 , pp. 4294-4301
    • Orth, D.1
  • 110
    • 15544366128 scopus 로고    scopus 로고
    • 26:H-genes required for intestinal colonization in calves
    • 26:H-genes required for intestinal colonization in calves. Infect Immun 73(3):1735-1743
    • (2005) Infect Immun , vol.73 , Issue.3 , pp. 1735-1743
    • Van Diemen, P.M.1
  • 111
    • 77952677567 scopus 로고    scopus 로고
    • Genome-wide transposon mutagenesis reveals a role for pO157 genes in biofilm development in Escherichia coli O157:H7 EDL933
    • Puttamreddy S, Cornick NA, Minion FC (2010) Genome-wide transposon mutagenesis reveals a role for pO157 genes in biofilm development in Escherichia coli O157:H7 EDL933. Infect Immun 78(6):2377-2384
    • (2010) Infect Immun , vol.78 , Issue.6 , pp. 2377-2384
    • Puttamreddy, S.1    Cornick, N.A.2    Minion, F.C.3
  • 112
    • 34249044453 scopus 로고    scopus 로고
    • EspP, a Type V-secreted serine protease of enterohaemorrhagic Escherichia coli O157:H7, influences intestinal colonization of calves and adherence to bovine primary intestinal epithelial cells
    • Dziva F et al (2007) EspP, a Type V-secreted serine protease of enterohaemorrhagic Escherichia coli O157:H7, influences intestinal colonization of calves and adherence to bovine primary intestinal epithelial cells. FEMS Microbiol Lett 271(2):258-264
    • (2007) FEMS Microbiol Lett , vol.271 , Issue.2 , pp. 258-264
    • Dziva, F.1
  • 113
    • 0042825302 scopus 로고    scopus 로고
    • Intracellular expression of the plasmid-encoded toxin from enteroaggregative Escherichia coli
    • Sui BQ, Dutta PR, Nataro JP (2003) Intracellular expression of the plasmid-encoded toxin from enteroaggregative Escherichia coli. Infect Immun 71(9):5364-5370
    • (2003) Infect Immun , vol.71 , Issue.9 , pp. 5364-5370
    • Sui, B.Q.1    Dutta, P.R.2    Nataro, J.P.3
  • 114
    • 0033801659 scopus 로고    scopus 로고
    • Pet toxin from enteroaggregative Escherichia coli produces cellular damage associated with fodrin disruption
    • Villaseca JM et al (2000) Pet toxin from enteroaggregative Escherichia coli produces cellular damage associated with fodrin disruption. Infect Immun 68(10):5920-5927
    • (2000) Infect Immun , vol.68 , Issue.10 , pp. 5920-5927
    • Villaseca, J.M.1
  • 115
    • 79952609941 scopus 로고    scopus 로고
    • Effects of the plasmid-encoded toxin of enteroaggregative Escherichia coli on focal adhesion complexes
    • Cappello RE et al (2011) Effects of the plasmid-encoded toxin of enteroaggregative Escherichia coli on focal adhesion complexes. FEMS Immunol Med Microbiol 61(3):301-314
    • (2011) FEMS Immunol Med Microbiol , vol.61 , Issue.3 , pp. 301-314
    • Cappello, R.E.1
  • 116
    • 34948824901 scopus 로고    scopus 로고
    • Intoxication of epithelial cells by plasmid-encoded toxin requires clathrin-mediated endocytosis
    • Navarro-Garcia F et al (2007) Intoxication of epithelial cells by plasmid-encoded toxin requires clathrin-mediated endocytosis. Microbiology 153 (Pt 9):2828-2838
    • (2007) Microbiology , vol.153 , Issue.PART 9 , pp. 2828-2838
    • Navarro-Garcia, F.1
  • 117
    • 34248393808 scopus 로고    scopus 로고
    • Pet, a non-AB toxin, is transported and translocated into epithelial cells by a retrograde trafficking pathway
    • Navarro-Garcia F et al (2007) Pet, a non-AB toxin, is transported and translocated into epithelial cells by a retrograde trafficking pathway. Infect Immun 75(5):2101-2109
    • (2007) Infect Immun , vol.75 , Issue.5 , pp. 2101-2109
    • Navarro-Garcia, F.1
  • 118
    • 51449093493 scopus 로고    scopus 로고
    • EspC translocation into epithelial cells by enteropathogenic Escherichia coli requires a concerted participation of type V and III secretion systems
    • Vidal JE, Navarro-Garcia F (2008) EspC translocation into epithelial cells by enteropathogenic Escherichia coli requires a concerted participation of type V and III secretion systems. Cell Microbiol 10(10):1975-1986
    • (2008) Cell Microbiol , vol.10 , Issue.10 , pp. 1975-1986
    • Vidal, J.E.1    Navarro-Garcia, F.2
  • 119
    • 33645519983 scopus 로고    scopus 로고
    • Efficient translocation of EspC into epithelial cells depends on enteropathogenic Escherichia coli and host cell contact
    • Vidal JE, Navarro-Garcia F (2006) Efficient translocation of EspC into epithelial cells depends on enteropathogenic Escherichia coli and host cell contact. Infect Immun 74(4):2293-2303
    • (2006) Infect Immun , vol.74 , Issue.4 , pp. 2293-2303
    • Vidal, J.E.1    Navarro-Garcia, F.2
  • 120
    • 33750829147 scopus 로고    scopus 로고
    • EspC, an autotransporter protein secreted by enteropathogenic Escherichia coli (EPEC), displays protease activity on human hemoglobin
    • Drago-Serrano ME, Parra SG, Manjarrez-Hernandez HA (2006) EspC, an autotransporter protein secreted by enteropathogenic Escherichia coli (EPEC), displays protease activity on human hemoglobin. FEMS Microbiol Lett 265(1):35-40
    • (2006) FEMS Microbiol Lett , vol.265 , Issue.1 , pp. 35-40
    • Drago-Serrano, M.E.1    Parra, S.G.2    Manjarrez-Hernandez, H.A.3
  • 121
    • 0029155828 scopus 로고
    • Protein secretion by enteropathogenic Escherichia coli is essential for transducing signals to epithelial cells
    • Kenny B, Finlay BB (1995) Protein secretion by enteropathogenic Escherichia coli is essential for transducing signals to epithelial cells. Proc Natl Acad Sci USA 92(17):7991-7995
    • (1995) Proc Natl Acad Sci USA , vol.92 , Issue.17 , pp. 7991-7995
    • Kenny, B.1    Finlay, B.B.2
  • 122
    • 28044461045 scopus 로고    scopus 로고
    • Citrobacter rodentium of mice and man
    • Mundy R et al (2005) Citrobacter rodentium of mice and man. Cell Microbiol 7(12):1697-1706
    • (2005) Cell Microbiol , vol.7 , Issue.12 , pp. 1697-1706
    • Mundy, R.1
  • 123
    • 0035150963 scopus 로고    scopus 로고
    • Genetic organization of the she pathogenicity island in Shigella flexneri 2a
    • Al-Hasani K et al (2001) Genetic organization of the she pathogenicity island in Shigella flexneri 2a. Microb Pathog 30(1):1-8
    • (2001) Microb Pathog , vol.30 , Issue.1 , pp. 1-8
    • Al-Hasani, K.1
  • 124
    • 0032879806 scopus 로고    scopus 로고
    • Global burden of Shigella infections: Implications for vaccine development and implementation of control strategies
    • Kotloff KL et al (1999) Global burden of Shigella infections: implications for vaccine development and implementation of control strategies. Bull World Health Organ 77(8):651-666
    • (1999) Bull World Health Organ , vol.77 , Issue.8 , pp. 651-666
    • Kotloff, K.L.1
  • 125
    • 34250353445 scopus 로고    scopus 로고
    • Clinical trials of Shigella vaccines: Two steps forward and one step back on a long, hard road
    • Levine MM et al (2007) Clinical trials of Shigella vaccines: two steps forward and one step back on a long, hard road. Nat Rev Microbiol 5(7):540-553
    • (2007) Nat Rev Microbiol , vol.5 , Issue.7 , pp. 540-553
    • Levine, M.M.1
  • 126
    • 80052361387 scopus 로고    scopus 로고
    • Shigella are versatile mucosal pathogens that circumvent the host innate immune system
    • Ashida H et al (2011) Shigella are versatile mucosal pathogens that circumvent the host innate immune system. Curr Opin Immunol 23(4):448-455
    • (2011) Curr Opin Immunol , vol.23 , Issue.4 , pp. 448-455
    • Ashida, H.1
  • 127
    • 3242668923 scopus 로고    scopus 로고
    • Prevalence of the sat, set and sen genes among diverse serotypes of Shigella flexneri strains isolated from patients with acute diarrhoea
    • Niyogi SK, Vargas M, Vila J (2004) Prevalence of the sat, set and sen genes among diverse serotypes of Shigella flexneri strains isolated from patients with acute diarrhoea. Clin Microbiol Infect 10(6):574-576
    • (2004) Clin Microbiol Infect , vol.10 , Issue.6 , pp. 574-576
    • Niyogi, S.K.1    Vargas, M.2    Vila, J.3
  • 128
    • 0242416999 scopus 로고    scopus 로고
    • Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T
    • Wei J et al (2003) Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T. Infect Immun 71(5):2775-2786
    • (2003) Infect Immun , vol.71 , Issue.5 , pp. 2775-2786
    • Wei, J.1
  • 129
    • 28544440091 scopus 로고    scopus 로고
    • Genome dynamics and diversity of Shigella species, the etiologic agents of bacillary dysentery
    • Yang F et al (2005) Genome dynamics and diversity of Shigella species, the etiologic agents of bacillary dysentery. Nucleic Acids Res 33(19):6445-6458
    • (2005) Nucleic Acids Res , vol.33 , Issue.19 , pp. 6445-6458
    • Yang, F.1
  • 130
    • 0036070744 scopus 로고    scopus 로고
    • Sat, the secreted autotransporter toxin of uropathogenic Escherichia coli, is a vacuolating cytotoxin for bladder and kidney epithelial cells
    • Guyer DM et al (2002) Sat, the secreted autotransporter toxin of uropathogenic Escherichia coli, is a vacuolating cytotoxin for bladder and kidney epithelial cells. Infect Immun 70(8):4539-4546
    • (2002) Infect Immun , vol.70 , Issue.8 , pp. 4539-4546
    • Guyer, D.M.1
  • 131
    • 33845422281 scopus 로고    scopus 로고
    • The secreted autotransporter toxin, Sat, functions as a virulence factor in Afa/Dr diffusely adhering Escherichia coli by promoting lesions in tight junction of polarized epithelial cells
    • Guignot J et al (2007) The secreted autotransporter toxin, Sat, functions as a virulence factor in Afa/Dr diffusely adhering Escherichia coli by promoting lesions in tight junction of polarized epithelial cells. Cell Microbiol 9(1):204-221
    • (2007) Cell Microbiol , vol.9 , Issue.1 , pp. 204-221
    • Guignot, J.1
  • 132
    • 79959264076 scopus 로고    scopus 로고
    • Secreted autotransporter toxin (Sat) triggers autophagy in epithelial cells that relies on cell detachment
    • Lievin-Le Moal V et al (2011) Secreted autotransporter toxin (Sat) triggers autophagy in epithelial cells that relies on cell detachment. Cell Microbiol 13(7):992-1013
    • (2011) Cell Microbiol , vol.13 , Issue.7 , pp. 992-1013
    • Lievin-Le Moal, V.1
  • 133
    • 77951214016 scopus 로고    scopus 로고
    • Mammalian autophagy: Core molecular machinery and signaling regulation
    • Yang Z, Klionsky DJ (2010) Mammalian autophagy: core molecular machinery and signaling regulation. Curr Opin Cell Biol 22(2):124-131
    • (2010) Curr Opin Cell Biol , vol.22 , Issue.2 , pp. 124-131
    • Yang, Z.1    Klionsky, D.J.2
  • 134
    • 4644274735 scopus 로고    scopus 로고
    • Functional analysis of the Tsh autotransporter from an avian pathogenic Escherichia coli strain
    • Kostakioti M, Stathopoulos C (2004) Functional analysis of the Tsh autotransporter from an avian pathogenic Escherichia coli strain. Infect Immun 72(10):5548-5554
    • (2004) Infect Immun , vol.72 , Issue.10 , pp. 5548-5554
    • Kostakioti, M.1    Stathopoulos, C.2
  • 135
    • 0028348785 scopus 로고
    • Isolation and characterization of a gene involved in hemagglutination by an avian pathogenic Escherichia coli strain
    • Provence DL, Curtiss R 3rd (1994) Isolation and characterization of a gene involved in hemagglutination by an avian pathogenic Escherichia coli strain. Infect Immun 62(4):1369-1380
    • (1994) Infect Immun , vol.62 , Issue.4 , pp. 1369-1380
    • Provence, D.L.1    Curtiss III, R.2
  • 136
    • 3543013141 scopus 로고    scopus 로고
    • SepA, the 110 kDa protein secreted by Shigella flexneri: Two-domain structure and proteolytic activity
    • Benjelloun-Touimi Z et al (1998) SepA, the 110 kDa protein secreted by Shigella flexneri: two-domain structure and proteolytic activity. Microbiology 144 (Pt 7):1815-1822
    • (1998) Microbiology , vol.144 , Issue.PART 7 , pp. 1815-1822
    • Benjelloun-Touimi, Z.1
  • 137
    • 0036139096 scopus 로고    scopus 로고
    • Escherichia coli hemoglobin protease autotransporter contributes to synergistic abscess formation and heme-dependent growth of Bacteroides fragilis
    • Otto BR et al (2002) Escherichia coli hemoglobin protease autotransporter contributes to synergistic abscess formation and heme-dependent growth of Bacteroides fragilis. Infect Immun 70(1):5-10
    • (2002) Infect Immun , vol.70 , Issue.1 , pp. 5-10
    • Otto, B.R.1
  • 138
    • 0033932231 scopus 로고    scopus 로고
    • Relationship between the Tsh autotransporter and pathogenicity of avian Escherichia coli and localization and analysis of the Tsh genetic region
    • Dozois CM et al (2000) Relationship between the Tsh autotransporter and pathogenicity of avian Escherichia coli and localization and analysis of the Tsh genetic region. Infect Immun 68(7):4145-4154
    • (2000) Infect Immun , vol.68 , Issue.7 , pp. 4145-4154
    • Dozois, C.M.1
  • 139
    • 33947205482 scopus 로고    scopus 로고
    • Autotransporter-encoding sequences are phylogenetically distributed among Escherichia coli clinical isolates and reference strains
    • Restieri C et al (2007) Autotransporter-encoding sequences are phylogenetically distributed among Escherichia coli clinical isolates and reference strains. Appl Environ Microbiol 73(5):1553-1562
    • (2007) Appl Environ Microbiol , vol.73 , Issue.5 , pp. 1553-1562
    • Restieri, C.1
  • 140
    • 0035230160 scopus 로고    scopus 로고
    • Phenotypic and genotypic characterization of virulence factors of Escherichia coli isolated from broiler chickens with simultaneous occurrence of cellulitis and other colibacillosis lesions
    • Gomis SM et al (2001) Phenotypic and genotypic characterization of virulence factors of Escherichia coli isolated from broiler chickens with simultaneous occurrence of cellulitis and other colibacillosis lesions. Can J Vet Res 65(1):1-6
    • (2001) Can J Vet Res , vol.65 , Issue.1 , pp. 1-6
    • Gomis, S.M.1
  • 141
    • 77957747820 scopus 로고    scopus 로고
    • Pic, an autotransporter protein secreted by different pathogens in the Enterobacteriaceae family, is a potent mucus secretagogue
    • Navarro-Garcia F et al (2010) Pic, an autotransporter protein secreted by different pathogens in the Enterobacteriaceae family, is a potent mucus secretagogue. Infect Immun 78(10):4101-4109
    • (2010) Infect Immun , vol.78 , Issue.10 , pp. 4101-4109
    • Navarro-Garcia, F.1
  • 142
    • 77951673268 scopus 로고    scopus 로고
    • TIM genes: A family of cell surface phosphatidylserine receptors that regulate innate and adaptive immunity
    • Freeman GJ et al (2010) TIM genes: a family of cell surface phosphatidylserine receptors that regulate innate and adaptive immunity. Immunol Rev 235(1):172-189
    • (2010) Immunol Rev , vol.235 , Issue.1 , pp. 172-189
    • Freeman, G.J.1
  • 143
    • 67649817705 scopus 로고    scopus 로고
    • PSGL-1 function in immunity and steady state homeostasis
    • Carlow DA et al (2009) PSGL-1 function in immunity and steady state homeostasis. Immunol Rev 230(1):75-96
    • (2009) Immunol Rev , vol.230 , Issue.1 , pp. 75-96
    • Carlow, D.A.1
  • 144
    • 0030966842 scopus 로고    scopus 로고
    • CD44: Structure, function, and association with the malignant process
    • Naor D, Sionov RV, Ish-Shalom D (1997) CD44: structure, function, and association with the malignant process. Adv Cancer Res 71:241-319
    • (1997) Adv Cancer Res , vol.71 , pp. 241-319
    • Naor, D.1    Sionov, R.V.2    Ish-Shalom, D.3
  • 145
    • 0032872724 scopus 로고    scopus 로고
    • Mucin-type O-glycans and leukosialin
    • Fukuda M, Tsuboi S (1999) Mucin-type O-glycans and leukosialin. Biochim Biophys Acta 1455 (2-3):205-217
    • (1999) Biochim Biophys Acta , vol.1455 , Issue.2-3 , pp. 205-217
    • Fukuda, M.1    Tsuboi, S.2
  • 147
    • 8644243987 scopus 로고    scopus 로고
    • Cross-linking of P-selectin glycoprotein ligand-1 induces death of activated T cells
    • Chen SC et al (2004) Cross-linking of P-selectin glycoprotein ligand-1 induces death of activated T cells. Blood 104(10):3233-3242
    • (2004) Blood , vol.104 , Issue.10 , pp. 3233-3242
    • Chen, S.C.1
  • 148
    • 33748939906 scopus 로고    scopus 로고
    • CD44 ligation induces caspase-independent cell death via a novel calpain/AIF pathway in human erythroleukemia cells
    • Artus C et al (2006) CD44 ligation induces caspase-independent cell death via a novel calpain/AIF pathway in human erythroleukemia cells. Oncogene 25(42):5741-5751
    • (2006) Oncogene , vol.25 , Issue.42 , pp. 5741-5751
    • Artus, C.1
  • 149
    • 0029035988 scopus 로고
    • Apoptosis of human hematopoietic progenitor cells induced by crosslinking of surface CD43, the major sialoglycoprotein of leukocytes
    • Bazil V et al (1995) Apoptosis of human hematopoietic progenitor cells induced by crosslinking of surface CD43, the major sialoglycoprotein of leukocytes. Blood 86(2):502-511
    • (1995) Blood , vol.86 , Issue.2 , pp. 502-511
    • Bazil, V.1
  • 150
    • 0030584787 scopus 로고    scopus 로고
    • CD45 ligation induces programmed cell death in T and B lymphocytes
    • Klaus SJ, Sidorenko SP, Clark EA (1996) CD45 ligation induces programmed cell death in T and B lymphocytes. J Immunol 156(8):2743-2753
    • (1996) J Immunol , vol.156 , Issue.8 , pp. 2743-2753
    • Klaus, S.J.1    Sidorenko, S.P.2    Clark, E.A.3
  • 151
    • 77957170681 scopus 로고    scopus 로고
    • Impaired innate immune response and enhanced pathology during Citrobacter rodentium infection in mice lacking functional P-selectin
    • Kum WW et al (2010) Impaired innate immune response and enhanced pathology during Citrobacter rodentium infection in mice lacking functional P-selectin. Cell Microbiol 12(9):1250-1271
    • (2010) Cell Microbiol , vol.12 , Issue.9 , pp. 1250-1271
    • Kum, W.W.1
  • 152
    • 79953715143 scopus 로고    scopus 로고
    • CD34 mediates intestinal inflammation in Salmonella-infected mice
    • Grassl GA et al (2010) CD34 mediates intestinal inflammation in Salmonella-infected mice. Cell Microbiol 12(11):1562-1575
    • (2010) Cell Microbiol , vol.12 , Issue.11 , pp. 1562-1575
    • Grassl, G.A.1
  • 153
    • 12244297799 scopus 로고    scopus 로고
    • CX3CR1-mediated dendritic cell access to the intestinal lumen and bacterial clearance
    • Niess JH et al (2005) CX3CR1-mediated dendritic cell access to the intestinal lumen and bacterial clearance. Science 307(5707):254-258
    • (2005) Science , vol.307 , Issue.5707 , pp. 254-258
    • Niess, J.H.1
  • 154
    • 77952363123 scopus 로고    scopus 로고
    • Lack of functional P-selectin ligand exacerbates Salmonella serovar typhimurium infection
    • Kum WW et al (2009) Lack of functional P-selectin ligand exacerbates Salmonella serovar typhimurium infection. J Immunol 182(10):6550-6561
    • (2009) J Immunol , vol.182 , Issue.10 , pp. 6550-6561
    • Kum, W.W.1
  • 155
    • 84055200171 scopus 로고    scopus 로고
    • CX3CR1 regulates intestinal macrophage homeostasis, bacterial translocation, and colitogenic Th17 responses in mice
    • Medina-Contreras O et al (2011) CX3CR1 regulates intestinal macrophage homeostasis, bacterial translocation, and colitogenic Th17 responses in mice. J Clin Invest 121(12):4787-4795
    • (2011) J Clin Invest , vol.121 , Issue.12 , pp. 4787-4795
    • Medina-Contreras, O.1
  • 156
    • 84856375969 scopus 로고    scopus 로고
    • Outbreak of hemolytic-uremic syndrome linked to Shiga toxin-producing enteroaggregative Escherichia coli O104:H4
    • Nataro JP (2011) Outbreak of hemolytic-uremic syndrome linked to Shiga toxin-producing enteroaggregative Escherichia coli O104:H4. Pediatr Res 70(3):221
    • (2011) Pediatr Res , vol.70 , Issue.3 , pp. 221
    • Nataro, J.P.1
  • 157
    • 0029166295 scopus 로고
    • SepA, the major extracellular protein of Shigella flexneri: Autonomous secretion and involvement in tissue invasion
    • Benjelloun-Touimi Z, Sansonetti PJ, Parsot C (1995) SepA, the major extracellular protein of Shigella flexneri: autonomous secretion and involvement in tissue invasion. Mol Microbiol 17(1):123-135
    • (1995) Mol Microbiol , vol.17 , Issue.1 , pp. 123-135
    • Benjelloun-Touimi, Z.1    Sansonetti, P.J.2    Parsot, C.3
  • 158
    • 84855902172 scopus 로고    scopus 로고
    • Genomic characterization of enteroaggregative Escherichia coli from children in Mali
    • Boisen N et al (2012) Genomic characterization of enteroaggregative Escherichia coli from children in Mali. J Infect Dis 205(3):431-444
    • (2012) J Infect Dis , vol.205 , Issue.3 , pp. 431-444
    • Boisen, N.1
  • 159
    • 66949142240 scopus 로고    scopus 로고
    • Characterisation of early mucosal and neuronal lesions following Shigella flexneri infection in human colon
    • Coron E et al (2009) Characterisation of early mucosal and neuronal lesions following Shigella flexneri infection in human colon. PLoS ONE 4(3):e4713
    • (2009) PLoS ONE , vol.4 , Issue.3
    • Coron, E.1
  • 160
    • 80051940624 scopus 로고    scopus 로고
    • Adhesin degradation accelerates delivery of heat-labile toxin by enterotoxigenic Escherichia coli
    • Roy K et al (2011) Adhesin degradation accelerates delivery of heat-labile toxin by enterotoxigenic Escherichia coli. J Biol Chem 286(34):29771-29779
    • (2011) J Biol Chem , vol.286 , Issue.34 , pp. 29771-29779
    • Roy, K.1
  • 161
    • 17044383351 scopus 로고    scopus 로고
    • A millennium update on pediatric diarrheal illness in the developing world
    • O'Ryan M, Prado V, Pickering LK (2005) A millennium update on pediatric diarrheal illness in the developing world. Semin Pediatr Infect Dis 16(2):125-136
    • (2005) Semin Pediatr Infect Dis , vol.16 , Issue.2 , pp. 125-136
    • O'Ryan, M.1    Prado, V.2    Pickering, L.K.3
  • 162
    • 58149193233 scopus 로고    scopus 로고
    • The SWISS-MODEL Repository and associated resources
    • Kiefer F, et al (2009) The SWISS-MODEL Repository and associated resources. Nucleic Acids Res 37:D387-392
    • (2009) Nucleic Acids Res , vol.37
    • Kiefer, F.1
  • 163
    • 80053345905 scopus 로고    scopus 로고
    • SignalP 4.0: Discriminating signal peptides from transmembrane regions
    • Petersen TN et al (2011) SignalP 4.0: discriminating signal peptides from transmembrane regions. Nat Methods 8(10):785-786
    • (2011) Nat Methods , vol.8 , Issue.10 , pp. 785-786
    • Petersen, T.N.1
  • 164
    • 80054078476 scopus 로고    scopus 로고
    • Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega
    • Sievers F et al (2011) Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega. Mol Syst Biol 7:539
    • (2011) Mol Syst Biol , vol.7 , pp. 539
    • Sievers, F.1
  • 165
    • 48249102000 scopus 로고    scopus 로고
    • Phylogeny.fr: Robust phylogenetic analysis for the non-specialist
    • Dereeper A, et al (2008) Phylogeny.fr: robust phylogenetic analysis for the non-specialist. Nucleic Acids Res 36:W465-W469
    • (2008) Nucleic Acids Res , vol.36
    • Dereeper, A.1
  • 166
    • 77950806408 scopus 로고    scopus 로고
    • New algorithms and methods to estimate maximum-likelihood phylogenies: Assessing the performance of PhyML 3.0
    • Guindon S et al (2010) New algorithms and methods to estimate maximum-likelihood phylogenies: assessing the performance of PhyML 3.0. Syst Biol 59(3):307-321
    • (2010) Syst Biol , vol.59 , Issue.3 , pp. 307-321
    • Guindon, S.1
  • 167
    • 33750314083 scopus 로고    scopus 로고
    • TreeDyn: Towards dynamic graphics and annotations for analyses of trees
    • Chevenet F et al (2006) TreeDyn: towards dynamic graphics and annotations for analyses of trees. BMC Bioinf 7:439
    • (2006) BMC Bioinf , vol.7 , pp. 439
    • Chevenet, F.1


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