메뉴 건너뛰기




Volumn 92, Issue 2, 2010, Pages 171-177

A host-specific factor is necessary for efficient folding of the autotransporter plasmid-encoded toxin

Author keywords

Autotransporter; Circular dichroism; Plasmid encoded toxin; Protein folding

Indexed keywords

AUTOTRANSPORTER; BACTERIAL TOXIN; ESCHERICHIA COLI PROTEIN; UNCLASSIFIED DRUG;

EID: 74249112624     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2009.11.006     Document Type: Article
Times cited : (8)

References (24)
  • 1
    • 35848952765 scopus 로고    scopus 로고
    • Protein secretion in gram-negative bacteria via the autotransporter pathway
    • Dautin N., and Bernstein H.D. Protein secretion in gram-negative bacteria via the autotransporter pathway. Annu. Rev. Microbiol. 61 (2007) 89-112
    • (2007) Annu. Rev. Microbiol. , vol.61 , pp. 89-112
    • Dautin, N.1    Bernstein, H.D.2
  • 4
    • 34447529326 scopus 로고    scopus 로고
    • Requirement for YaeT in the outer membrane assembly of autotransporter proteins
    • Jain S., and Goldberg M.B. Requirement for YaeT in the outer membrane assembly of autotransporter proteins. J. Bacteriol. 189 (2007) 5393-5398
    • (2007) J. Bacteriol. , vol.189 , pp. 5393-5398
    • Jain, S.1    Goldberg, M.B.2
  • 5
    • 0036839640 scopus 로고    scopus 로고
    • Shigella flexneri DegP facilitates IcsA surface expression and is required for efficient intercellular spread
    • Purdy G.E., Hong M., and Payne S.M. Shigella flexneri DegP facilitates IcsA surface expression and is required for efficient intercellular spread. Infect. Immun. 70 (2002) 6355-6364
    • (2002) Infect. Immun. , vol.70 , pp. 6355-6364
    • Purdy, G.E.1    Hong, M.2    Payne, S.M.3
  • 6
    • 34547643207 scopus 로고    scopus 로고
    • IcsA surface presentation in Shigella flexneri requires the periplasmic chaperones DegP, Skp, and SurA
    • Purdy G.E., Fisher C.R., and Payne S.M. IcsA surface presentation in Shigella flexneri requires the periplasmic chaperones DegP, Skp, and SurA. J. Bacteriol. 189 (2007) 5566-5573
    • (2007) J. Bacteriol. , vol.189 , pp. 5566-5573
    • Purdy, G.E.1    Fisher, C.R.2    Payne, S.M.3
  • 7
    • 60649107938 scopus 로고    scopus 로고
    • Contribution of the periplasmic chaperone Skp to efficient presentation of the autotransporter IcsA on the surface of Shigella flexneri
    • Wagner J.K., Heindl J.E., Gray A.N., Jain S., and Goldberg M.B. Contribution of the periplasmic chaperone Skp to efficient presentation of the autotransporter IcsA on the surface of Shigella flexneri. J. Bacteriol. 191 (2009) 815-821
    • (2009) J. Bacteriol. , vol.191 , pp. 815-821
    • Wagner, J.K.1    Heindl, J.E.2    Gray, A.N.3    Jain, S.4    Goldberg, M.B.5
  • 8
    • 70350470007 scopus 로고    scopus 로고
    • Roles of periplasmic chaperone proteins in the biogenesis of serine protease autotransporters of Enterobacteriaceae
    • Ruiz-Perez F., Henderson I.R., Leyton D.L., Rossiter A.E., Zhang Y., and Nataro J.P. Roles of periplasmic chaperone proteins in the biogenesis of serine protease autotransporters of Enterobacteriaceae. J. Bacteriol. 191 (2009) 6571-6583
    • (2009) J. Bacteriol. , vol.191 , pp. 6571-6583
    • Ruiz-Perez, F.1    Henderson, I.R.2    Leyton, D.L.3    Rossiter, A.E.4    Zhang, Y.5    Nataro, J.P.6
  • 9
    • 34948824901 scopus 로고    scopus 로고
    • Intoxication of epithelial cells by plasmid-encoded toxin requires clathrin-mediated endocytosis
    • Navarro-Garcia F., Canizalez-Roman A., Vidal J.E., and Salazar M.I. Intoxication of epithelial cells by plasmid-encoded toxin requires clathrin-mediated endocytosis. Microbiology 153 (2007) 2828-2838
    • (2007) Microbiology , vol.153 , pp. 2828-2838
    • Navarro-Garcia, F.1    Canizalez-Roman, A.2    Vidal, J.E.3    Salazar, M.I.4
  • 10
    • 0037678811 scopus 로고    scopus 로고
    • Fodrin CaM-binding domain cleavage by Pet from enteroaggregative Escherichia coli leads to actin cytoskeletal disruption
    • Canizalez-Roman A., and Navarro-Garcia F. Fodrin CaM-binding domain cleavage by Pet from enteroaggregative Escherichia coli leads to actin cytoskeletal disruption. Mol. Microbiol. 48 (2003) 947-958
    • (2003) Mol. Microbiol. , vol.48 , pp. 947-958
    • Canizalez-Roman, A.1    Navarro-Garcia, F.2
  • 11
    • 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., Canizalez-Roman A., Burlingame K.E., Teter K., and Vidal J.E. Pet, a non-AB toxin, is transported and translocated into epithelial cells by a retrograde trafficking pathway. Infect. Immun. 75 (2007) 2101-2109
    • (2007) Infect. Immun. , vol.75 , pp. 2101-2109
    • Navarro-Garcia, F.1    Canizalez-Roman, A.2    Burlingame, K.E.3    Teter, K.4    Vidal, J.E.5
  • 12
    • 0032881401 scopus 로고    scopus 로고
    • Involvement of the enteroaggregative Escherichia coli plasmid-encoded toxin in causing human intestinal damage
    • Henderson I.R., Hicks S., Navarro-Garcia F., Elias W.P., Philips A.D., and Nataro J.P. Involvement of the enteroaggregative Escherichia coli plasmid-encoded toxin in causing human intestinal damage. Infect. Immun. 67 (1999) 5338-5344
    • (1999) Infect. Immun. , vol.67 , pp. 5338-5344
    • Henderson, I.R.1    Hicks, S.2    Navarro-Garcia, F.3    Elias, W.P.4    Philips, A.D.5    Nataro, J.P.6
  • 14
    • 20444435483 scopus 로고    scopus 로고
    • Crystal structure of hemoglobin protease, a heme binding autotransporter protein from pathogenic Escherichia coli
    • Otto B.R., Sijbrandi R., Luirink J., et al. Crystal structure of hemoglobin protease, a heme binding autotransporter protein from pathogenic Escherichia coli. J. Biol. Chem. 280 (2005) 17339-17345
    • (2005) J. Biol. Chem. , vol.280 , pp. 17339-17345
    • Otto, B.R.1    Sijbrandi, R.2    Luirink, J.3
  • 16
    • 0031842273 scopus 로고    scopus 로고
    • In vitro effects of a high-molecular-weight heat-labile enterotoxin from enteroaggregative Escherichia coli
    • Navarro-Garcia F., Eslava C., Villaseca J.M., et al. In vitro effects of a high-molecular-weight heat-labile enterotoxin from enteroaggregative Escherichia coli. Infect. Immun. 66 (1998) 3149-3154
    • (1998) Infect. Immun. , vol.66 , pp. 3149-3154
    • Navarro-Garcia, F.1    Eslava, C.2    Villaseca, J.M.3
  • 17
    • 0001911969 scopus 로고    scopus 로고
    • Circular dichroism of peptides and proteins
    • Berova N., Nakanishi K., and Woody R.W. (Eds), John Wiley & Sons, Inc., Hoboken
    • Sreerama N., and Woody R.W. Circular dichroism of peptides and proteins. In: Berova N., Nakanishi K., and Woody R.W. (Eds). Circular Dichroism: Principles and Applications (2000), John Wiley & Sons, Inc., Hoboken 601-620
    • (2000) Circular Dichroism: Principles and Applications , pp. 601-620
    • Sreerama, N.1    Woody, R.W.2
  • 18
    • 47749087527 scopus 로고    scopus 로고
    • A conserved stable core structure in the passenger domain beta-helix of autotransporter virulence proteins
    • Renn J.P., and Clark P.L. A conserved stable core structure in the passenger domain beta-helix of autotransporter virulence proteins. Biopolymers 89 (2008) 420-427
    • (2008) Biopolymers , vol.89 , pp. 420-427
    • Renn, J.P.1    Clark, P.L.2
  • 19
    • 51549121332 scopus 로고    scopus 로고
    • Structural characteristics of the plasmid-encoded toxin from enteroaggregative Escherichia coli
    • Scaglione P., Nemec K.N., Burlingame K.E., et al. Structural characteristics of the plasmid-encoded toxin from enteroaggregative Escherichia coli. Biochemistry 47 (2008) 9582-9591
    • (2008) Biochemistry , vol.47 , pp. 9582-9591
    • Scaglione, P.1    Nemec, K.N.2    Burlingame, K.E.3
  • 20
    • 33645525759 scopus 로고    scopus 로고
    • Pertactin beta-helix folding mechanism suggests common themes for the secretion and folding of autotransporter proteins
    • Junker M., Schuster C.C., McDonnell A.V., et al. Pertactin beta-helix folding mechanism suggests common themes for the secretion and folding of autotransporter proteins. Proc. Natl. Acad. Sci. U S A 103 (2006) 4918-4923
    • (2006) Proc. Natl. Acad. Sci. U S A , vol.103 , pp. 4918-4923
    • Junker, M.1    Schuster, C.C.2    McDonnell, A.V.3
  • 21
    • 33747790227 scopus 로고    scopus 로고
    • The turn of the screw: variations of the abundant beta-solenoid motif in passenger domains of type V secretory proteins
    • Kajava A.V., and Steven A.C. The turn of the screw: variations of the abundant beta-solenoid motif in passenger domains of type V secretory proteins. J. Struct. Biol. 155 (2006) 306-315
    • (2006) J. Struct. Biol. , vol.155 , pp. 306-315
    • Kajava, A.V.1    Steven, A.C.2
  • 22
    • 0032734808 scopus 로고    scopus 로고
    • Characterization of pic, a secreted protease of Shigella flexneri and enteroaggregative Escherichia coli
    • Henderson I.R., Czeczulin J., Eslava C., Noriega F., and Nataro J.P. Characterization of pic, a secreted protease of Shigella flexneri and enteroaggregative Escherichia coli. Infect. Immun. 67 (1999) 5587-5596
    • (1999) Infect. Immun. , vol.67 , pp. 5587-5596
    • Henderson, I.R.1    Czeczulin, J.2    Eslava, C.3    Noriega, F.4    Nataro, J.P.5
  • 24
    • 8744267513 scopus 로고    scopus 로고
    • Modulation of human 5-lipoxygenase activity by membrane lipids
    • Pande A.H., Moe D., Nemec K.N., Qin S., Tan S., and Tatulian S.A. Modulation of human 5-lipoxygenase activity by membrane lipids. Biochemistry 43 (2004) 14653-14666
    • (2004) Biochemistry , vol.43 , pp. 14653-14666
    • Pande, A.H.1    Moe, D.2    Nemec, K.N.3    Qin, S.4    Tan, S.5    Tatulian, S.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.