메뉴 건너뛰기




Volumn 4, Issue 5, 2013, Pages

An association between peptidoglycan synthesis and organization of the Streptococcus pyogenes ExPortal

Author keywords

[No Author keywords available]

Indexed keywords

GALLIDERMIN; PEPTIDOGLYCAN;

EID: 84887139738     PISSN: 21612129     EISSN: 21507511     Source Type: Journal    
DOI: 10.1128/mBio.00485-13     Document Type: Article
Times cited : (14)

References (48)
  • 1
    • 37349125189 scopus 로고    scopus 로고
    • Sec translocase and sortase A are colocalised in a locus in the cytoplasmic membrane of Streptococcus mutans
    • Hu P, Bian Z, Fan M, Huang M, Zhang P. 2008. Sec translocase and sortase A are colocalised in a locus in the cytoplasmic membrane of Streptococcus mutans. Arch. Oral Biol. 53:150-154.
    • (2008) Arch. Oral Biol , vol.53 , pp. 150-154
    • Hu, P.1    Bian, Z.2    Fan, M.3    Huang, M.4    Zhang, P.5
  • 3
    • 2642540881 scopus 로고    scopus 로고
    • A microdomain for protein secretion in Gram-positive bacteria
    • Rosch J, Caparon M. 2004. A microdomain for protein secretion in Gram-positive bacteria. Science 304:1513-1515.
    • (2004) Science , vol.304 , pp. 1513-1515
    • Rosch, J.1    Caparon, M.2
  • 4
    • 0033939735 scopus 로고    scopus 로고
    • Pathogenesis of group A streptococcal infections
    • Cunningham MW. 2000. Pathogenesis of group A streptococcal infections. Clin. Microbiol. Rev. 13:470-511.
    • (2000) Clin. Microbiol. Rev , vol.13 , pp. 470-511
    • Cunningham, M.W.1
  • 5
    • 34248670671 scopus 로고    scopus 로고
    • How group A Streptococcus circumvents host phagocyte defenses
    • Kwinn LA, Nizet V. 2007. How group A Streptococcus circumvents host phagocyte defenses. Future Microbiol. 2:75-84.
    • (2007) Future Microbiol , vol.2 , pp. 75-84
    • Kwinn, L.A.1    Nizet, V.2
  • 7
    • 0242320522 scopus 로고    scopus 로고
    • The bacterial translocase: A dynamic protein channel complex
    • de Keyzer J, van der Does C, Driessen AJ. 2003. The bacterial translocase: a dynamic protein channel complex. Cell. Mol. Life Sci. 60: 2034-2052.
    • (2003) Cell. Mol. Life Sci , vol.60 , pp. 2034-2052
    • de Keyzer, J.1    van der Does, C.2    Driessen, A.J.3
  • 8
    • 33846603187 scopus 로고    scopus 로고
    • Anionic lipids enriched at the ExPortal of Streptococcus pyogenes
    • Rosch JW, Hsu FF, Caparon MG. 2007. Anionic lipids enriched at the ExPortal of Streptococcus pyogenes. J. Bacteriol. 189:801-806.
    • (2007) J. Bacteriol , vol.189 , pp. 801-806
    • Rosch, J.W.1    Hsu, F.F.2    Caparon, M.G.3
  • 9
    • 57449114045 scopus 로고    scopus 로고
    • Sortase A localizes to distinct foci on the Streptococcus pyogenes membrane
    • Raz A, Fischetti VA. 2008. Sortase A localizes to distinct foci on the Streptococcus pyogenes membrane. Proc. Natl. Acad. Sci. U. S. A. 105: 18549-18554.
    • (2008) Proc. Natl. Acad. Sci. U. S. A , vol.105 , pp. 18549-18554
    • Raz, A.1    Fischetti, V.A.2
  • 11
    • 27944484031 scopus 로고    scopus 로고
    • The ExPortal: An organelle dedicated to the biogenesis of secreted proteins in Streptococcus pyogenes
    • Rosch JW, Caparon MG. 2005. The ExPortal: an organelle dedicated to the biogenesis of secreted proteins in Streptococcus pyogenes. Mol. Microbiol. 58:959-968.
    • (2005) Mol. Microbiol , vol.58 , pp. 959-968
    • Rosch, J.W.1    Caparon, M.G.2
  • 12
    • 84866005675 scopus 로고    scopus 로고
    • Cationic antimicrobial peptides disrupt the Streptococcus pyogenes ExPortal
    • Vega LA, Caparon MG. 2012. Cationic antimicrobial peptides disrupt the Streptococcus pyogenes ExPortal. Mol. Microbiol. 85:1119-1132.
    • (2012) Mol. Microbiol , vol.85 , pp. 1119-1132
    • Vega, L.A.1    Caparon, M.G.2
  • 13
  • 14
    • 37349041697 scopus 로고    scopus 로고
    • Lipid intermediates in the biosynthesis of bacterial peptidoglycan
    • van Heijenoort J. 2007. Lipid intermediates in the biosynthesis of bacterial peptidoglycan. Microbiol. Mol. Biol. Rev. 71:620-635.
    • (2007) Microbiol. Mol. Biol. Rev , vol.71 , pp. 620-635
    • van Heijenoort, J.1
  • 15
    • 84861892432 scopus 로고    scopus 로고
    • Structural perspective of peptidoglycan biosynthesis and assembly
    • Lovering AL, Safadi SS, Strynadka NC. 2012. Structural perspective of peptidoglycan biosynthesis and assembly. Annu. Rev. Biochem. 81: 451-478.
    • (2012) Annu. Rev. Biochem , vol.81 , pp. 451-478
    • Lovering, A.L.1    Safadi, S.S.2    Strynadka, N.C.3
  • 17
    • 33645779735 scopus 로고    scopus 로고
    • Insights into in vivo activities of lantibiotics from gallidermin and epidermin mode-of-action studies
    • Bonelli RR, Schneider T, Sahl HG, Wiedemann I. 2006. Insights into in vivo activities of lantibiotics from gallidermin and epidermin mode-of-action studies. Antimicrob. Agents Chemother. 50:1449-1457.
    • (2006) Antimicrob. Agents Chemother , vol.50 , pp. 1449-1457
    • Bonelli, R.R.1    Schneider, T.2    Sahl, H.G.3    Wiedemann, I.4
  • 20
    • 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
  • 21
    • 34250370517 scopus 로고    scopus 로고
    • Distribution of protein A on the surface of Staphylococcus aureus
    • DeDent AC, McAdow M, Schneewind O. 2007. Distribution of protein A on the surface of Staphylococcus aureus. J. Bacteriol. 189:4473-4484.
    • (2007) J. Bacteriol , vol.189 , pp. 4473-4484
    • Dedent, A.C.1    McAdow, M.2    Schneewind, O.3
  • 26
    • 84871055385 scopus 로고    scopus 로고
    • The helical MreB cytoskeleton in Escherichia coli MC1000/pLE7 is an artifact of the N-terminal YFP tag
    • Swulius MT, Jensen GJ. 2012. The helical MreB cytoskeleton in Escherichia coli MC1000/pLE7 is an artifact of the N-terminal YFP tag. J. Bacteriol. 194:6382-6386.
    • (2012) J. Bacteriol , vol.194 , pp. 6382-6386
    • Swulius, M.T.1    Jensen, G.J.2
  • 27
    • 80455158425 scopus 로고    scopus 로고
    • Dynamic distribution of the SecA and SecY translocase subunits and septal localization of the HtrA surface chaperone/protease during Streptococcus pneumoniae D39 cell division
    • doi:10.1128/ mBio.00202-11
    • Tsui HC, Keen SK, Sham LT, Wayne KJ, Winkler ME. 2011. Dynamic distribution of the SecA and SecY translocase subunits and septal localization of the HtrA surface chaperone/protease during Streptococcus pneumoniae D39 cell division. mBio 2:e00202-00211. doi:10.1128/ mBio.00202-11.
    • (2011) MBio , vol.2
    • Tsui, H.C.1    Keen, S.K.2    Sham, L.T.3    Wayne, K.J.4    Winkler, M.E.5
  • 28
    • 0037494988 scopus 로고    scopus 로고
    • Control of cell morphogenesis in bacteria: Two distinct ways to make a rod-shaped cell
    • Daniel RA, Errington J. 2003. Control of cell morphogenesis in bacteria: two distinct ways to make a rod-shaped cell. Cell 113:767-776.
    • (2003) Cell , vol.113 , pp. 767-776
    • Daniel, R.A.1    Errington, J.2
  • 30
    • 80755143318 scopus 로고    scopus 로고
    • Changes of lipid domains in Bacillus subtilis cells with disrupted cell wall peptidoglycan
    • Muchová K, Wilkinson AJ, Barák I. 2011. Changes of lipid domains in Bacillus subtilis cells with disrupted cell wall peptidoglycan. FEMS Microbiol. Lett. 325:92-98.
    • (2011) FEMS Microbiol. Lett , vol.325 , pp. 92-98
    • Muchová, K.1    Wilkinson, A.J.2    Barák, I.3
  • 32
    • 34548677525 scopus 로고    scopus 로고
    • The cell shape proteins MreB and MreC control cell morphogenesis by positioning cell wall synthetic complexes
    • Divakaruni AV, Baida C, White CL, Gober JW. 2007. The cell shape proteins MreB and MreC control cell morphogenesis by positioning cell wall synthetic complexes. Mol. Microbiol. 66:174-188.
    • (2007) Mol. Microbiol , vol.66 , pp. 174-188
    • Divakaruni, A.V.1    Baida, C.2    White, C.L.3    Gober, J.W.4
  • 35
    • 79960075043 scopus 로고    scopus 로고
    • Coupled, circumferential motions of the cell wall synthesis machinery and MreB filaments in B
    • Garner EC, Bernard R, Wang W, Zhuang X, Rudner DZ, Mitchison T. 2011. Coupled, circumferential motions of the cell wall synthesis machinery and MreB filaments in B. subtilis. Science 333:222-225.
    • (2011) Subtilis. Science , vol.333 , pp. 222-225
    • Garner, E.C.1    Bernard, R.2    Wang, W.3    Zhuang, X.4    Rudner, D.Z.5    Mitchison, T.6
  • 37
    • 0027957715 scopus 로고
    • Genetic and molecular characterization of the Escherichia coli secD operon and its products
    • Pogliano KJ, Beckwith J. 1994. Genetic and molecular characterization of the Escherichia coli secD operon and its products. J. Bacteriol. 176: 804-814.
    • (1994) J. Bacteriol , vol.176 , pp. 804-814
    • Pogliano, K.J.1    Beckwith, J.2
  • 38
    • 0034916176 scopus 로고    scopus 로고
    • Packing characteristics of a model system mimicking cytoplasmic bacterial membranes
    • Lohner K, Latal A, Degovics G, Garidel P. 2001. Packing characteristics of a model system mimicking cytoplasmic bacterial membranes. Chem. Phys. Lipids 111:177-192.
    • (2001) Chem. Phys. Lipids , vol.111 , pp. 177-192
    • Lohner, K.1    Latal, A.2    Degovics, G.3    Garidel, P.4
  • 39
    • 84856774559 scopus 로고    scopus 로고
    • Role of lipids in the interaction of antimicrobial peptides with membranes
    • Teixeira V, Feio MJ, Bastos M. 2012. Role of lipids in the interaction of antimicrobial peptides with membranes. Prog. Lipid Res. 51:149-177.
    • (2012) Prog. Lipid Res , vol.51 , pp. 149-177
    • Teixeira, V.1    Feio, M.J.2    Bastos, M.3
  • 40
    • 77956292192 scopus 로고    scopus 로고
    • Functional microdomains in bacterial membranes
    • López D, Kolter R. 2010. Functional microdomains in bacterial membranes. Genes Dev. 24:1893-1902.
    • (2010) Genes Dev , vol.24 , pp. 1893-1902
    • López, D.1    Kolter, R.2
  • 41
    • 0036375597 scopus 로고    scopus 로고
    • Structure, mechanism and function of prenyltransferases
    • Liang PH, Ko TP, Wang AH. 2002. Structure, mechanism and function of prenyltransferases. Eur. J. Biochem. 269:3339-3354.
    • (2002) Eur. J. Biochem , vol.269 , pp. 3339-3354
    • Liang, P.H.1    Ko, T.P.2    Wang, A.H.3
  • 42
    • 0026469139 scopus 로고
    • Expression of protein F, the fibronectin-binding protein of Streptococcus pyogenes JRS4, in heterologous streptococcal and enterococcal strains promotes their adherence to respiratory epithelial cells
    • Hanski E, Horwitz PA, Caparon MG. 1992. Expression of protein F, the fibronectin-binding protein of Streptococcus pyogenes JRS4, in heterologous streptococcal and enterococcal strains promotes their adherence to respiratory epithelial cells. Infect. Immun. 60:5119-5125.
    • (1992) Infect. Immun , vol.60 , pp. 5119-5125
    • Hanski, E.1    Horwitz, P.A.2    Caparon, M.G.3
  • 43
    • 30744463313 scopus 로고    scopus 로고
    • Regulation of SpeB in Streptococcus pyogenes by pH and NaCl: A model for in vivo gene expression
    • Loughman JA, Caparon M. 2006. Regulation of SpeB in Streptococcus pyogenes by pH and NaCl: a model for in vivo gene expression. J. Bacteriol. 188:399-408.
    • (2006) J. Bacteriol , vol.188 , pp. 399-408
    • Loughman, J.A.1    Caparon, M.2
  • 45
    • 46249119973 scopus 로고    scopus 로고
    • The signal recognition particle pathway is required for virulence in Streptococcus pyogenes
    • Rosch JW, Vega LA, Beyer JM, Lin A, Caparon MG. 2008. The signal recognition particle pathway is required for virulence in Streptococcus pyogenes. Infect. Immun. 76:2612-2619.
    • (2008) Infect. Immun , vol.76 , pp. 2612-2619
    • Rosch, J.W.1    Vega, L.A.2    Beyer, J.M.3    Lin, A.4    Caparon, M.G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.