메뉴 건너뛰기




Volumn 7, Issue 11, 2012, Pages

Structural Basis for Group B Streptococcus Pilus 1 Sortases C Regulation and Specificity

Author keywords

[No Author keywords available]

Indexed keywords

RECOMBINANT ENZYME; RECOMBINANT SORTASE C1; RECOMBINANT SORTASE C2; SORTASE; SORTASE C1; SORTASE C2; TRANSCRIPTION FACTOR AP 1; TRANSCRIPTION FACTOR AP 2; UNCLASSIFIED DRUG;

EID: 84869047387     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0049048     Document Type: Article
Times cited : (24)

References (46)
  • 2
    • 77950173319 scopus 로고    scopus 로고
    • Specific involvement of pilus type 2a in biofilm formation in group B Streptococcus
    • Rinaudo CD, Rosini R, Galeotti CL, Berti F, Necchi F, et al. (2010) Specific involvement of pilus type 2a in biofilm formation in group B Streptococcus. PLoS One 5: e9216.
    • (2010) PLoS One , vol.5
    • Rinaudo, C.D.1    Rosini, R.2    Galeotti, C.L.3    Berti, F.4    Necchi, F.5
  • 3
    • 51749097576 scopus 로고    scopus 로고
    • Pilus backbone contributes to group B Streptococcus paracellular translocation through epithelial cells
    • Pezzicoli A, Santi I, Lauer P, Rosini R, Rinaudo D, et al. (2008) Pilus backbone contributes to group B Streptococcus paracellular translocation through epithelial cells. J Infect Dis 198: 890-898.
    • (2008) J Infect Dis , vol.198 , pp. 890-898
    • Pezzicoli, A.1    Santi, I.2    Lauer, P.3    Rosini, R.4    Rinaudo, D.5
  • 5
    • 37749043209 scopus 로고    scopus 로고
    • Pili in Gram-positive bacteria: assembly, involvement in colonization and biofilm development
    • Mandlik A, Swierczynski A, Das A, Ton-That H, (2008) Pili in Gram-positive bacteria: assembly, involvement in colonization and biofilm development. Trends Microbiol 16: 33-40.
    • (2008) Trends Microbiol , vol.16 , pp. 33-40
    • Mandlik, A.1    Swierczynski, A.2    Das, A.3    Ton-That, H.4
  • 6
    • 67249101935 scopus 로고    scopus 로고
    • Dual role for pilus in adherence to epithelial cells and biofilm formation in Streptococcus agalactiae
    • Konto-Ghiorghi Y, Mairey E, Mallet A, Dumenil G, Caliot E, et al. (2009) Dual role for pilus in adherence to epithelial cells and biofilm formation in Streptococcus agalactiae. PLoS Pathog 5: e1000422.
    • (2009) PLoS Pathog , vol.5
    • Konto-Ghiorghi, Y.1    Mairey, E.2    Mallet, A.3    Dumenil, G.4    Caliot, E.5
  • 7
    • 33846910750 scopus 로고    scopus 로고
    • Group B streptococcal pilus proteins contribute to adherence to and invasion of brain microvascular endothelial cells
    • Maisey HC, Hensler M, Nizet V, Doran KS, (2007) Group B streptococcal pilus proteins contribute to adherence to and invasion of brain microvascular endothelial cells. J Bacteriol 189: 1464-1467.
    • (2007) J Bacteriol , vol.189 , pp. 1464-1467
    • Maisey, H.C.1    Hensler, M.2    Nizet, V.3    Doran, K.S.4
  • 8
    • 58749093047 scopus 로고    scopus 로고
    • Preventing bacterial infections with pilus-based vaccines: the group B streptococcus paradigm
    • Margarit I, Rinaudo CD, Galeotti CL, Maione D, Ghezzo C, et al. (2009) Preventing bacterial infections with pilus-based vaccines: the group B streptococcus paradigm. J Infect Dis 199: 108-115.
    • (2009) J Infect Dis , vol.199 , pp. 108-115
    • Margarit, I.1    Rinaudo, C.D.2    Galeotti, C.L.3    Maione, D.4    Ghezzo, C.5
  • 9
    • 21644481459 scopus 로고    scopus 로고
    • Identification of a Universal Group B Streptococcus Vaccine by Multiple Genome Screen
    • Maione D, Margarit I, Rinaudo CD, Masignani V, Mora M, et al. (2005) Identification of a Universal Group B Streptococcus Vaccine by Multiple Genome Screen. Science 309: 148-150.
    • (2005) Science , vol.309 , pp. 148-150
    • Maione, D.1    Margarit, I.2    Rinaudo, C.D.3    Masignani, V.4    Mora, M.5
  • 12
    • 0345689425 scopus 로고    scopus 로고
    • Assembly of pili on the surface of Corynebacterium diphtheriae
    • Ton-That H, Schneewind O, (2003) Assembly of pili on the surface of Corynebacterium diphtheriae. Mol Microbiol 50: 1429-1438.
    • (2003) Mol Microbiol , vol.50 , pp. 1429-1438
    • Ton-That, H.1    Schneewind, O.2
  • 13
    • 36849072428 scopus 로고    scopus 로고
    • Stabilizing isopeptide bonds revealed in gram-positive bacterial pilus structure
    • Kang HJ, Coulibaly F, Clow F, Proft T, Baker EN, (2007) Stabilizing isopeptide bonds revealed in gram-positive bacterial pilus structure. Science 318: 1625-1628.
    • (2007) Science , vol.318 , pp. 1625-1628
    • Kang, H.J.1    Coulibaly, F.2    Clow, F.3    Proft, T.4    Baker, E.N.5
  • 14
    • 84860894253 scopus 로고    scopus 로고
    • New insights into the role of the glutamic acid of the E-box motif in group B Streptococcus pilus 2a assembly
    • Cozzi R, Nuccitelli A, D'Onofrio M, Necchi F, Rosini R, et al. (2012) New insights into the role of the glutamic acid of the E-box motif in group B Streptococcus pilus 2a assembly. FASEB J.
    • (2012) FASEB J
    • Cozzi, R.1    Nuccitelli, A.2    D'Onofrio, M.3    Necchi, F.4    Rosini, R.5
  • 15
    • 3142559796 scopus 로고    scopus 로고
    • Sortases and pilin elements involved in pilus assembly of Corynebacterium diphtheriae
    • Ton-That H, Marraffini LA, Schneewind O, (2004) Sortases and pilin elements involved in pilus assembly of Corynebacterium diphtheriae. Mol Microbiol 53: 251-261.
    • (2004) Mol Microbiol , vol.53 , pp. 251-261
    • Ton-That, H.1    Marraffini, L.A.2    Schneewind, O.3
  • 16
    • 2042470134 scopus 로고    scopus 로고
    • Assembly of pili in Gram-positive bacteria
    • Ton-That H, Schneewind O, (2004) Assembly of pili in Gram-positive bacteria. Trends Microbiol 12: 228-234.
    • (2004) Trends Microbiol , vol.12 , pp. 228-234
    • Ton-That, H.1    Schneewind, O.2
  • 18
    • 48849099859 scopus 로고    scopus 로고
    • Sortase A utilizes an ancillary protein anchor for efficient cell wall anchoring of pili in Streptococcus agalactiae
    • Nobbs AH, Rosini R, Rinaudo CD, Maione D, Grandi G, et al. (2008) Sortase A utilizes an ancillary protein anchor for efficient cell wall anchoring of pili in Streptococcus agalactiae. Infect Immun 76: 3550-3560.
    • (2008) Infect Immun , vol.76 , pp. 3550-3560
    • Nobbs, A.H.1    Rosini, R.2    Rinaudo, C.D.3    Maione, D.4    Grandi, G.5
  • 19
    • 33745200283 scopus 로고    scopus 로고
    • Identification of novel genomic islands coding for antigenic pilus-like structures in Streptococcus agalactiae
    • Rosini R, Rinaudo CD, Soriani M, Lauer P, Mora M, et al. (2006) Identification of novel genomic islands coding for antigenic pilus-like structures in Streptococcus agalactiae. Mol Microbiol 61: 126-141.
    • (2006) Mol Microbiol , vol.61 , pp. 126-141
    • Rosini, R.1    Rinaudo, C.D.2    Soriani, M.3    Lauer, P.4    Mora, M.5
  • 20
    • 33746328720 scopus 로고    scopus 로고
    • Use of Lactococcus lactis expressing pili from group B Streptococcus as a broad-coverage vaccine against streptococcal disease
    • Buccato S, Maione D, Rinaudo CD, Volpini G, Taddei AR, et al. (2006) Use of Lactococcus lactis expressing pili from group B Streptococcus as a broad-coverage vaccine against streptococcal disease. J Infect Dis 194: 331-340.
    • (2006) J Infect Dis , vol.194 , pp. 331-340
    • Buccato, S.1    Maione, D.2    Rinaudo, C.D.3    Volpini, G.4    Taddei, A.R.5
  • 21
    • 70349975956 scopus 로고    scopus 로고
    • Two crystal structures of pneumococcal pilus sortase C provide novel insights into catalysis and substrate specificity
    • Neiers F, Madhurantakam C, Falker S, Manzano C, Dessen A, et al. (2009) Two crystal structures of pneumococcal pilus sortase C provide novel insights into catalysis and substrate specificity. J Mol Biol 393: 704-716.
    • (2009) J Mol Biol , vol.393 , pp. 704-716
    • Neiers, F.1    Madhurantakam, C.2    Falker, S.3    Manzano, C.4    Dessen, A.5
  • 22
  • 23
    • 79952260321 scopus 로고    scopus 로고
    • Structure of the sortase AcSrtC-1 from Actinomyces oris
    • Persson K, (2011) Structure of the sortase AcSrtC-1 from Actinomyces oris. Acta Crystallogr D Biol Crystallogr 67: 212-217.
    • (2011) Acta Crystallogr D Biol Crystallogr , vol.67 , pp. 212-217
    • Persson, K.1
  • 24
    • 80051574122 scopus 로고    scopus 로고
    • A novel "open-form" structure of sortaseC from Streptococcus suis
    • Lu G, Qi J, Gao F, Yan J, Tang J, et al. (2011) A novel "open-form" structure of sortaseC from Streptococcus suis. Proteins 79: 2764-2769.
    • (2011) Proteins , vol.79 , pp. 2764-2769
    • Lu, G.1    Qi, J.2    Gao, F.3    Yan, J.4    Tang, J.5
  • 25
    • 82555187028 scopus 로고    scopus 로고
    • The crystal structure analysis of group B Streptococcus sortase C1: a model for the "lid" movement upon substrate binding
    • Khare B, Fu ZQ, Huang IH, Ton-That H, Narayana SV, (2011) The crystal structure analysis of group B Streptococcus sortase C1: a model for the "lid" movement upon substrate binding. J Mol Biol 414: 563-577.
    • (2011) J Mol Biol , vol.414 , pp. 563-577
    • Khare, B.1    Fu, Z.Q.2    Huang, I.H.3    Ton-That, H.4    Narayana, S.V.5
  • 26
    • 80052290437 scopus 로고    scopus 로고
    • Structural differences between the Streptococcus agalactiae housekeeping and pilus-specific sortases: SrtA and SrtC1
    • Khare B, Krishnan V, Rajashankar KR, H IH, Xin M, et al. (2011) Structural differences between the Streptococcus agalactiae housekeeping and pilus-specific sortases: SrtA and SrtC1. PLoS One 6: e22995.
    • (2011) PLoS One , vol.6
    • Khare, B.1    Krishnan, V.2    Rajashankar, K.R.3    Xin, M.4
  • 27
    • 79957900908 scopus 로고    scopus 로고
    • Structure analysis and site-directed mutagenesis of defined key residues and motives for pilus-related sortase C1 in group B Streptococcus
    • Cozzi R, Malito E, Nuccitelli A, D'Onofrio M, Martinelli M, et al. (2011) Structure analysis and site-directed mutagenesis of defined key residues and motives for pilus-related sortase C1 in group B Streptococcus. FASEB J 25: 1874-1886.
    • (2011) FASEB J , vol.25 , pp. 1874-1886
    • Cozzi, R.1    Malito, E.2    Nuccitelli, A.3    D'Onofrio, M.4    Martinelli, M.5
  • 28
    • 84861390458 scopus 로고    scopus 로고
    • Structural determinants of Actinomyces sortase SrtC2 required for membrane localization and assembly of type 2 fimbriae for interbacterial coaggregation and oral biofilm formation
    • Wu C, Mishra A, Reardon ME, Huang IH, Counts SC, et al. (2012) Structural determinants of Actinomyces sortase SrtC2 required for membrane localization and assembly of type 2 fimbriae for interbacterial coaggregation and oral biofilm formation. J Bacteriol 194: 2531-2539.
    • (2012) J Bacteriol , vol.194 , pp. 2531-2539
    • Wu, C.1    Mishra, A.2    Reardon, M.E.3    Huang, I.H.4    Counts, S.C.5
  • 29
    • 0035932982 scopus 로고    scopus 로고
    • Structure of sortase, the transpeptidase that anchors proteins to the cell wall of Staphylococcus aureus
    • Ilangovan U, Ton-That H, Iwahara J, Schneewind O, Clubb RT, (2001) Structure of sortase, the transpeptidase that anchors proteins to the cell wall of Staphylococcus aureus. Proc Natl Acad Sci U S A 98: 6056-6061.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 6056-6061
    • Ilangovan, U.1    Ton-That, H.2    Iwahara, J.3    Schneewind, O.4    Clubb, R.T.5
  • 30
    • 69949151708 scopus 로고    scopus 로고
    • The structure of the Staphylococcus aureus sortase-substrate complex reveals how the universally conserved LPXTG sorting signal is recognized
    • Suree N, Liew CK, Villareal VA, Thieu W, Fadeev EA, et al. (2009) The structure of the Staphylococcus aureus sortase-substrate complex reveals how the universally conserved LPXTG sorting signal is recognized. J Biol Chem 284: 24465-24477.
    • (2009) J Biol Chem , vol.284 , pp. 24465-24477
    • Suree, N.1    Liew, C.K.2    Villareal, V.A.3    Thieu, W.4    Fadeev, E.A.5
  • 31
    • 0025046731 scopus 로고
    • Mapping of catalytically important domains in Escherichia coli leader peptidase
    • Bilgin N, Lee JI, Zhu HY, Dalbey R, von Heijne G, (1990) Mapping of catalytically important domains in Escherichia coli leader peptidase. Embo J 9: 2717-2722.
    • (1990) Embo J , vol.9 , pp. 2717-2722
    • Bilgin, N.1    Lee, J.I.2    Zhu, H.Y.3    Dalbey, R.4    von Heijne, G.5
  • 32
    • 0032544580 scopus 로고    scopus 로고
    • The transmembrane domains of ectoapyrase (CD39) affect its enzymatic activity and quaternary structure
    • Wang TF, Ou Y, Guidotti G, (1998) The transmembrane domains of ectoapyrase (CD39) affect its enzymatic activity and quaternary structure. J Biol Chem 273: 24814-24821.
    • (1998) J Biol Chem , vol.273 , pp. 24814-24821
    • Wang, T.F.1    Ou, Y.2    Guidotti, G.3
  • 33
    • 33645137247 scopus 로고    scopus 로고
    • Sortases and the art of anchoring proteins to the envelopes of gram-positive bacteria
    • Marraffini LA, Dedent AC, Schneewind O, (2006) Sortases and the art of anchoring proteins to the envelopes of gram-positive bacteria. Microbiol Mol Biol Rev 70: 192-221.
    • (2006) Microbiol Mol Biol Rev , vol.70 , pp. 192-221
    • Marraffini, L.A.1    Dedent, A.C.2    Schneewind, O.3
  • 34
    • 79952736436 scopus 로고    scopus 로고
    • A model for group B Streptococcus pilus type 1: the structure of a 35-kDa C-terminal fragment of the major pilin GBS80
    • Vengadesan K, Ma X, Dwivedi P, Ton-That H, Narayana SV, (2011) A model for group B Streptococcus pilus type 1: the structure of a 35-kDa C-terminal fragment of the major pilin GBS80. J Mol Biol 407: 731-743.
    • (2011) J Mol Biol , vol.407 , pp. 731-743
    • Vengadesan, K.1    Ma, X.2    Dwivedi, P.3    Ton-That, H.4    Narayana, S.V.5
  • 36
    • 32444439972 scopus 로고    scopus 로고
    • Assembly of distinct pilus structures on the surface of Corynebacterium diphtheriae
    • Gaspar AH, Ton-That H, (2006) Assembly of distinct pilus structures on the surface of Corynebacterium diphtheriae. J Bacteriol 188: 1526-1533.
    • (2006) J Bacteriol , vol.188 , pp. 1526-1533
    • Gaspar, A.H.1    Ton-That, H.2
  • 37
    • 50249189305 scopus 로고    scopus 로고
    • Roles of the sortases of Streptococcus pneumoniae in assembly of the RlrA pilus
    • LeMieux J, Woody S, Camilli A, (2008) Roles of the sortases of Streptococcus pneumoniae in assembly of the RlrA pilus. J Bacteriol 190: 6002-6013.
    • (2008) J Bacteriol , vol.190 , pp. 6002-6013
    • LeMieux, J.1    Woody, S.2    Camilli, A.3
  • 38
    • 82155168216 scopus 로고    scopus 로고
    • Sortase enzymes in Gram-positive bacteria
    • Spirig T, Weiner EM, Clubb RT, (2011) Sortase enzymes in Gram-positive bacteria. Mol Microbiol 82: 1044-1059.
    • (2011) Mol Microbiol , vol.82 , pp. 1044-1059
    • Spirig, T.1    Weiner, E.M.2    Clubb, R.T.3
  • 39
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes
    • Krogh A, Larsson B, von Heijne G, Sonnhammer EL, (2001) Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. J Mol Biol 305: 567-580.
    • (2001) J Mol Biol , vol.305 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    von Heijne, G.3    Sonnhammer, E.L.4
  • 40
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ, (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22: 4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 41
    • 84934438590 scopus 로고    scopus 로고
    • The Polymerase Incomplete Primer Extension (PIPE) method applied to high-throughput cloning and site-directed mutagenesis
    • Klock HE, Lesley SA, (2009) The Polymerase Incomplete Primer Extension (PIPE) method applied to high-throughput cloning and site-directed mutagenesis. Methods Mol Biol 498: 91-103.
    • (2009) Methods Mol Biol , vol.498 , pp. 91-103
    • Klock, H.E.1    Lesley, S.A.2
  • 42
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray Diffraction Data Collected in Oscillation Mode
    • Otwinowski Z, Minor W, (1997) Processing of X-ray Diffraction Data Collected in Oscillation Mode. Methods in Enzymology 276: 307-326.
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 44
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P, Cowtan K, (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60: 2126-2132.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.