메뉴 건너뛰기




Volumn 379, Issue 1, 2008, Pages 174-187

Structural Analysis of the Saf Pilus by Electron Microscopy and Image Processing

Author keywords

atomic structure fitting; electron microscopy; image processing; pilus; single particle analysis

Indexed keywords

ARTICLE; BACTERIUM PILUS; ELECTRON MICROSCOPY; FIMBRIA; IMAGE PROCESSING; IN VITRO STUDY; NONHUMAN; PRIORITY JOURNAL; SALMONELLA; STRUCTURE ANALYSIS; THREE DIMENSIONAL IMAGING; X RAY CRYSTALLOGRAPHY;

EID: 42749096468     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.03.056     Document Type: Article
Times cited : (28)

References (55)
  • 1
    • 0032035356 scopus 로고    scopus 로고
    • The chaperone/usher pathway: a major terminal branch of the general secretory pathway
    • D.G. Thanassi E.T. Saulino S.J. Hultgren The chaperone/usher pathway: a major terminal branch of the general secretory pathway Curr. Opin. Microbiol. 1 1998 223 231
    • (1998) Curr. Opin. Microbiol. , vol.1 , pp. 223-231
    • Thanassi, D.G.1    Saulino, E.T.2    Hultgren, S.J.3
  • 2
    • 0034051753 scopus 로고    scopus 로고
    • Assembly of complex organelles: pilus biogenesis in gram-negative bacteria as a model system
    • D.G. Thanassi S.J. Hultgren Assembly of complex organelles: pilus biogenesis in gram-negative bacteria as a model system Methods 20 2000 111 126
    • (2000) Methods , vol.20 , pp. 111-126
    • Thanassi, D.G.1    Hultgren, S.J.2
  • 4
    • 34250332241 scopus 로고    scopus 로고
    • FGL chaperone-assembled fimbrial polyadhesins: anti-immune armament of Gram-negative bacterial pathogens
    • A. Zavialov G. Zav'yalova T. Korpela V. Zav'yalov FGL chaperone-assembled fimbrial polyadhesins: anti-immune armament of Gram-negative bacterial pathogens FEMS Microbiol. Rev. 31 2007 478 514
    • (2007) FEMS Microbiol. Rev. , vol.31 , pp. 478-514
    • Zavialov, A.1    Zav'yalova, G.2    Korpela, T.3    Zav'yalov, V.4
  • 6
    • 0033937939 scopus 로고    scopus 로고
    • Multiple pathways allow protein secretion across the bacterial outer membrane
    • D.G. Thanassi S.J. Hultgren Multiple pathways allow protein secretion across the bacterial outer membrane Curr. Opin. Cell Biol. 12 2000 420 430
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 420-430
    • Thanassi, D.G.1    Hultgren, S.J.2
  • 11
    • 0030775342 scopus 로고    scopus 로고
    • The chaperone-assisted membrane release and folding pathway is sensed by two signal transduction systems
    • C.H. Jones P.N. Danese J.S. Pinkner T.J. Silhavey S.J. Hultgren The chaperone-assisted membrane release and folding pathway is sensed by two signal transduction systems EMBO J. 16 1997 6394 6406
    • (1997) EMBO J. , vol.16 , pp. 6394-6406
    • Jones, C.H.1    Danese, P.N.2    Pinkner, J.S.3    Silhavey, T.J.4    Hultgren, S.J.5
  • 13
    • 0034255260 scopus 로고    scopus 로고
    • Snapshots of usher-mediated protein secretion and ordered pilus assembly
    • E.T. Saulino E. Bullitt S.J. Hultgren Snapshots of usher-mediated protein secretion and ordered pilus assembly Proc. Natl. Acad. Sci. USA 97 2000 9240 9245
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 9240-9245
    • Saulino, E.T.1    Bullitt, E.2    Hultgren, S.J.3
  • 16
    • 0037112164 scopus 로고    scopus 로고
    • Chaperone priming of pilus subunits facilitates a topological transition that drives fiber formation
    • F.G. Sauer J.S. Pinkner G. Waksman S.J. Hultgren Chaperone priming of pilus subunits facilitates a topological transition that drives fiber formation Cell 111 2002 543 551
    • (2002) Cell , vol.111 , pp. 543-551
    • Sauer, F.G.1    Pinkner, J.S.2    Waksman, G.3    Hultgren, S.J.4
  • 17
    • 0038820383 scopus 로고    scopus 로고
    • Structure and biogenesis of the capsular F1 antigen from Yersinia pestis: preserved folding energy drives fiber formation
    • A.V. Zavialov J. Berglund A.F. Pudney L.J. Fooks T.M. Ibrahim S. MacIntyre S.D. Knight Structure and biogenesis of the capsular F1 antigen from Yersinia pestis : preserved folding energy drives fiber formation Cell 113 2003 587 596
    • (2003) Cell , vol.113 , pp. 587-596
    • Zavialov, A.V.1    Berglund, J.2    Pudney, A.F.3    Fooks, L.J.4    Ibrahim, T.M.5    MacIntyre, S.6    Knight, S.D.7
  • 18
    • 33745195658 scopus 로고    scopus 로고
    • Donor-strand exchange in chaperone-assisted pilus assembly proceeds through a concerted β strand displacement mechanism
    • H. Remaut R.J. Rose T.J. Hannan S.J. Hultgren S.E. Radford A.E. Ashcroft G. Waksman Donor-strand exchange in chaperone-assisted pilus assembly proceeds through a concerted β strand displacement mechanism Mol. Cell 22 2006 831 842
    • (2006) Mol. Cell , vol.22 , pp. 831-842
    • Remaut, H.1    Rose, R.J.2    Hannan, T.J.3    Hultgren, S.J.4    Radford, S.E.5    Ashcroft, A.E.6    Waksman, G.7
  • 19
    • 0029738256 scopus 로고    scopus 로고
    • Molecular basis of two subfamilies of immunoglobulin-like chaperones
    • D.L. Hung S.D. Knight R.M. Woods J.S. Pinkner S.J. Hultgren Molecular basis of two subfamilies of immunoglobulin-like chaperones EMBO J. 15 1996 3792 3805
    • (1996) EMBO J. , vol.15 , pp. 3792-3805
    • Hung, D.L.1    Knight, S.D.2    Woods, R.M.3    Pinkner, J.S.4    Hultgren, S.J.5
  • 20
    • 0026509588 scopus 로고
    • P pili in uropathogenic E. coli are composite fibres with distinct fibrillar adhesive tips
    • M.J. Kuehn J. Heuser S. Normark S.J. Hultgren P pili in uropathogenic E. coli are composite fibres with distinct fibrillar adhesive tips Nature 356 1992 252 255
    • (1992) Nature , vol.356 , pp. 252-255
    • Kuehn, M.J.1    Heuser, J.2    Normark, S.3    Hultgren, S.J.4
  • 23
    • 0032989015 scopus 로고    scopus 로고
    • Bacterial adhesins: common themes and variations in architecture and assembly
    • G.E. Soto S.J. Hultgren Bacterial adhesins: common themes and variations in architecture and assembly J. Bacteriol. 181 1999 1059 1071
    • (1999) J. Bacteriol. , vol.181 , pp. 1059-1071
    • Soto, G.E.1    Hultgren, S.J.2
  • 24
    • 0027263822 scopus 로고
    • Genetic analysis of the gene cluster encoding nonfimbrial adhesin I from an Escherichia coli uropathogen
    • R. Ahrens M. Ott A. Ritter H. Hoschützky T. Bühler F. Lottspeich Genetic analysis of the gene cluster encoding nonfimbrial adhesin I from an Escherichia coli uropathogen Infect. Immun. 61 1993 2505 2512
    • (1993) Infect. Immun. , vol.61 , pp. 2505-2512
    • Ahrens, R.1    Ott, M.2    Ritter, A.3    Hoschützky, H.4    Bühler, T.5    Lottspeich, F.6
  • 25
    • 0028149058 scopus 로고
    • Nucleotide sequence of the afimbrial-adhesin-encoding afa-3 gene cluster and its translocation via flanking IS1 insertion sequences
    • M.I. Garcia A. Labigne C. LeBouguenec Nucleotide sequence of the afimbrial-adhesin-encoding afa-3 gene cluster and its translocation via flanking IS1 insertion sequences J. Bacteriol. 176 1994 7601 7613
    • (1994) J. Bacteriol. , vol.176 , pp. 7601-7613
    • Garcia, M.I.1    Labigne, A.2    LeBouguenec, C.3
  • 26
    • 0034052364 scopus 로고    scopus 로고
    • Immunocytochemistry of the AfaE adhesin and AfaD invasin produced by pathogenic Escherichia coli strains during interaction of the bacteria with HeLa cells by high-resolution scanning electron microscopy
    • P. Gounon M. Jouve C. Le Bouguénec Immunocytochemistry of the AfaE adhesin and AfaD invasin produced by pathogenic Escherichia coli strains during interaction of the bacteria with HeLa cells by high-resolution scanning electron microscopy Microb. Infect. 2 2000 359 365
    • (2000) Microb. Infect. , vol.2 , pp. 359-365
    • Gounon, P.1    Jouve, M.2    Le Bouguénec, C.3
  • 32
    • 0032791139 scopus 로고    scopus 로고
    • Multiple insertions of fimbrial operons correlate with the evolution of Salmonella serovars responsible for human disease
    • A. Folkesson A. Advani S. Sukupolvi J.D. Pfeifer S. Normark S. Löfdahl Multiple insertions of fimbrial operons correlate with the evolution of Salmonella serovars responsible for human disease Mol. Microbiol. 33 1999 612 622
    • (1999) Mol. Microbiol. , vol.33 , pp. 612-622
    • Folkesson, A.1    Advani, A.2    Sukupolvi, S.3    Pfeifer, J.D.4    Normark, S.5    Löfdahl, S.6
  • 33
    • 1842456935 scopus 로고    scopus 로고
    • Immunogenic properties of the Salmonella atypical fimbriae in BALB/c mice
    • L. Strindelius A. Folkesson S. Normark I. Sjöholm Immunogenic properties of the Salmonella atypical fimbriae in BALB/c mice Vaccine 22 2004 1448 1456
    • (2004) Vaccine , vol.22 , pp. 1448-1456
    • Strindelius, L.1    Folkesson, A.2    Normark, S.3    Sjöholm, I.4
  • 34
    • 0024545752 scopus 로고
    • Isolation and characterization of the alpha-galactosyl-1,4-beta-galactosyl-specific adhesin (P adhesin) from fimbriated Escherichia coli
    • H. Hoschützky F. Lottspeich K. Jann Isolation and characterization of the alpha-galactosyl-1,4-beta-galactosyl-specific adhesin (P adhesin) from fimbriated Escherichia coli Infect. Immun. 57 1989 76 81
    • (1989) Infect. Immun. , vol.57 , pp. 76-81
    • Hoschützky, H.1    Lottspeich, F.2    Jann, K.3
  • 36
    • 0021645447 scopus 로고
    • Multivariate statistical classification of noisy images (randomly oriented biological macromolecules)
    • M. van Heel Multivariate statistical classification of noisy images (randomly oriented biological macromolecules) Ultramicroscopy 13 1984 165 183
    • (1984) Ultramicroscopy , vol.13 , pp. 165-183
    • van Heel, M.1
  • 38
    • 0023102907 scopus 로고
    • Angular reconstitution: a posteriori assignment of projection directions for 3D reconstruction
    • M. van Heel Angular reconstitution: a posteriori assignment of projection directions for 3D reconstruction Ultramicroscopy 21 1987 111 124
    • (1987) Ultramicroscopy , vol.21 , pp. 111-124
    • van Heel, M.1
  • 39
    • 0003845223 scopus 로고    scopus 로고
    • The PyMOL Molecular Graphics System
    • W.L. DeLano The PyMOL Molecular Graphics System 2005 DeLano Scientific LLC South San Francisco, CA
    • (2005)
    • DeLano, W.L.1
  • 41
    • 0034075292 scopus 로고    scopus 로고
    • Recruitment of CD55 and CEACAM5 brush border-associated glycosylphosphatidylinositol-anchored proteins by members of the Afa/Dr diffusely-adhering Escherichia coli family infecting the human polarized intestinal Caco-2/TC7
    • J. Guignot I. Peiffer M.F. Bernet-Camard D. Lublin C. Carnoy S.L. Moseley A.L. Servin Recruitment of CD55 and CEACAM5 brush border-associated glycosylphosphatidylinositol-anchored proteins by members of the Afa/Dr diffusely-adhering Escherichia coli family infecting the human polarized intestinal Caco-2/TC7 Infect. Immun. 68 2000 3554 3563
    • (2000) Infect. Immun. , vol.68 , pp. 3554-3563
    • Guignot, J.1    Peiffer, I.2    Bernet-Camard, M.F.3    Lublin, D.4    Carnoy, C.5    Moseley, S.L.6    Servin, A.L.7
  • 42
    • 0036126951 scopus 로고    scopus 로고
    • The major structural subunits of Dr and F1845 fimbriae are adhesins
    • C.P. Van Loy E.V. Sokurenko S.L. Moseley The major structural subunits of Dr and F1845 fimbriae are adhesins Infect. Immun. 70 2002 1694 1702
    • (2002) Infect. Immun. , vol.70 , pp. 1694-1702
    • Van Loy, C.P.1    Sokurenko, E.V.2    Moseley, S.L.3
  • 43
    • 3142721456 scopus 로고    scopus 로고
    • Differential recognition of members of the carcinoembryonic antigen family by Afa/Dr adhesins of diffusely adhering Escherichia coli (Afa/Dr DAEC)
    • C.N. Berger O. Billker T.F. Meyer A.L. Servin I. Kansau Differential recognition of members of the carcinoembryonic antigen family by Afa/Dr adhesins of diffusely adhering Escherichia coli (Afa/Dr DAEC) Mol. Microbiol. 52 2004 963 983
    • (2004) Mol. Microbiol. , vol.52 , pp. 963-983
    • Berger, C.N.1    Billker, O.2    Meyer, T.F.3    Servin, A.L.4    Kansau, I.5
  • 44
    • 11144281811 scopus 로고    scopus 로고
    • Molecular aspects of biogenesis of Escherichia coli Dr fimbriae: characterization of DraB–DraE complexes
    • R. Piatek B. Zalewska O. Kolaj M. Ferens B. Nowicki J. Kur Molecular aspects of biogenesis of Escherichia coli Dr fimbriae: characterization of DraB–DraE complexes Infect. Immun. 73 2005 135 145
    • (2005) Infect. Immun. , vol.73 , pp. 135-145
    • Piatek, R.1    Zalewska, B.2    Kolaj, O.3    Ferens, M.4    Nowicki, B.5    Kur, J.6
  • 45
    • 0038441501 scopus 로고    scopus 로고
    • Accurate determination of local defocus and specimen tilt in electron microscopy
    • J.A. Mindell N. Grigorieff Accurate determination of local defocus and specimen tilt in electron microscopy J. Struct. Biol. 142 2003 334 347
    • (2003) J. Struct. Biol. , vol.142 , pp. 334-347
    • Mindell, J.A.1    Grigorieff, N.2
  • 48
    • 0000313739 scopus 로고
    • Exact filters for general geometry three-dimensional reconstruction
    • G. Harauz M. van Heel Exact filters for general geometry three-dimensional reconstruction Optik 73 1986 146 156
    • (1986) Optik , vol.73 , pp. 146-156
    • Harauz, G.1    van Heel, M.2
  • 49
    • 0029009159 scopus 로고
    • Structure of Lumbricus terrestris hemoglobin at 30 Å resolution determined using angular reconstitution
    • M. Schatz E.V. Orlova P. Dube J. Jager M. van Heel Structure of Lumbricus terrestris hemoglobin at 30 Å resolution determined using angular reconstitution J. Struct. Biol. 114 1995 28 40
    • (1995) J. Struct. Biol. , vol.114 , pp. 28-40
    • Schatz, M.1    Orlova, E.V.2    Dube, P.3    Jager, J.4    van Heel, M.5
  • 50
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields
    • J. Frank M. Radermacher P. Penczek J. Zhu Y. Li M. Ladjadj A. Leith SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields J. Struct. Biol. 116 1996 190 199
    • (1996) J. Struct. Biol. , vol.116 , pp. 190-199
    • Frank, J.1    Radermacher, M.2    Penczek, P.3    Zhu, J.4    Li, Y.5    Ladjadj, M.6    Leith, A.7
  • 52
    • 84988115618 scopus 로고
    • Validation of the general purpose Tripos 5.2 force field
    • M. Clark R.D. Cramer N. van Opdenbosch Validation of the general purpose Tripos 5.2 force field J. Comput. Chem. 10 1989 982 1012
    • (1989) J. Comput. Chem. , vol.10 , pp. 982-1012
    • Clark, M.1    Cramer, R.D.2    van Opdenbosch, N.3
  • 55
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • E. Krissinel K. Henrick Inference of macromolecular assemblies from crystalline state J. Mol. Biol. 372 2007 774 797
    • (2007) J. Mol. Biol. , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.