메뉴 건너뛰기




Volumn 7, Issue , 2016, Pages

Dynamic capsule restructuring by the main pneumococcal autolysin LytA in response to the epithelium

Author keywords

[No Author keywords available]

Indexed keywords

AUTOLYSIN; BACTERIAL ENZYME; BACTERIAL PROTEIN; CATHELICIDIN ANTIMICROBIAL PEPTIDE LL 37; HYDROLASE; LYTA PROTEIN; UNCLASSIFIED DRUG; N ACETYLMURAMOYLALANINE AMIDASE;

EID: 84959377704     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms10859     Document Type: Article
Times cited : (64)

References (57)
  • 1
    • 0025083176 scopus 로고
    • Covalent linkage between the capsular polysaccharide and the cell wall peptidoglycan of Streptococcus pneumoniae revealed by immunochemical methods
    • Sorensen, U. B., Henrichsen, J., Chen, H. C. & Szu, S. C. Covalent linkage between the capsular polysaccharide and the cell wall peptidoglycan of Streptococcus pneumoniae revealed by immunochemical methods. Microb. Pathog. 8, 325-334 (1990).
    • (1990) Microb. Pathog. , vol.8 , pp. 325-334
    • Sorensen, U.B.1    Henrichsen, J.2    Chen, H.C.3    Szu, S.C.4
  • 2
    • 23344444876 scopus 로고    scopus 로고
    • Illustration of pneumococcal polysaccharide capsule during adherence and invasion of epithelial cells
    • Hammerschmidt, S. et al. Illustration of pneumococcal polysaccharide capsule during adherence and invasion of epithelial cells. Infect. Immun. 73, 4653-4667 (2005).
    • (2005) Infect. Immun. , vol.73 , pp. 4653-4667
    • Hammerschmidt, S.1
  • 3
    • 0028907760 scopus 로고
    • Relationship between colonial morphology and adherence of Streptococcus pneumoniae
    • Cundell, D. R., Weiser, J. N., Shen, J., Young, A. & Tuomanen, E. I. Relationship between colonial morphology and adherence of Streptococcus pneumoniae. Infect. Immun. 63, 757-761 (1995).
    • (1995) Infect. Immun. , vol.63 , pp. 757-761
    • Cundell, D.R.1    Weiser, J.N.2    Shen, J.3    Young, A.4    Tuomanen, E.I.5
  • 4
    • 0030949875 scopus 로고    scopus 로고
    • Human b-defensin-1 is a salt-sensitive antibiotic in lung that is inactivated in cystic fibrosis
    • Goldman, M. J. et al. Human b-defensin-1 is a salt-sensitive antibiotic in lung that is inactivated in cystic fibrosis. Cell 88, 553-560 (1997).
    • (1997) Cell , vol.88 , pp. 553-560
    • Goldman, M.J.1
  • 6
    • 0032482980 scopus 로고    scopus 로고
    • The peptide antibiotic LL-37/hCAP-18 is expressed in epithelia of the human lung where it has broad antimicrobial activity at the airway surface
    • Bals, R., Wang, X., Zasloff, M. & Wilson, J. M. The peptide antibiotic LL-37/hCAP-18 is expressed in epithelia of the human lung where it has broad antimicrobial activity at the airway surface. Proc. Natl Acad. Sci. USA 95, 9541-9546 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 9541-9546
    • Bals, R.1    Wang, X.2    Zasloff, M.3    Wilson, J.M.4
  • 7
    • 0036528903 scopus 로고    scopus 로고
    • Increased levels of antimicrobial peptides in tracheal aspirates of newborn infants during infection
    • Schaller-Bals, S., Schulze, A. & Bals, R. Increased levels of antimicrobial peptides in tracheal aspirates of newborn infants during infection. Am. J. Respir. Crit. Care Med. 165, 992-995 (2002).
    • (2002) Am. J. Respir. Crit. Care Med. , vol.165 , pp. 992-995
    • Schaller-Bals, S.1    Schulze, A.2    Bals, R.3
  • 8
    • 84883431889 scopus 로고    scopus 로고
    • The human cathelicidin LL-37 has antiviral activity against respiratory syncytial virus
    • Currie, S. M. et al. The human cathelicidin LL-37 has antiviral activity against respiratory syncytial virus. PLoS ONE 8, e73659 (2013).
    • (2013) PLoS ONE , vol.8
    • Currie, S.M.1
  • 9
    • 84902340880 scopus 로고    scopus 로고
    • Cathelicidin host defence peptide augments clearance of pulmonary Pseudomonas aeruginosa infection by its influence on neutrophil function in vivo
    • Beaumont, P. E. et al. Cathelicidin host defence peptide augments clearance of pulmonary Pseudomonas aeruginosa infection by its influence on neutrophil function in vivo. PLoS ONE 9, e99029 (2014).
    • (2014) PLoS ONE , vol.9
    • Beaumont, P.E.1
  • 10
    • 77953629095 scopus 로고    scopus 로고
    • Human lung mast cells mediate pneumococcal cell death in response to activation by pneumolysin
    • Cruse, G. et al. Human lung mast cells mediate pneumococcal cell death in response to activation by pneumolysin. J. Immunol. 184, 7108-7115 (2010).
    • (2010) J. Immunol. , vol.184 , pp. 7108-7115
    • Cruse, G.1
  • 11
    • 48849104512 scopus 로고    scopus 로고
    • The capsule sensitizes Streptococcus pneumoniae to alphadefensins human neutrophil proteins 1 to 3
    • Beiter, K. et al. The capsule sensitizes Streptococcus pneumoniae to alphadefensins human neutrophil proteins 1 to 3. Infect. Immun. 76, 3710-3716 (2008).
    • (2008) Infect. Immun. , vol.76 , pp. 3710-3716
    • Beiter, K.1
  • 12
    • 58949097012 scopus 로고    scopus 로고
    • Capsule polysaccharide is a bacterial decoy for antimicrobial peptides
    • Llobet, E., Tomás, J. M. & Bengoechea, J. A. Capsule polysaccharide is a bacterial decoy for antimicrobial peptides. Microbiology 154, 3877-3886 (2008).
    • (2008) Microbiology , vol.154 , pp. 3877-3886
    • Llobet, E.1    Tomás, J.M.2    Bengoechea, J.A.3
  • 13
    • 77649181946 scopus 로고    scopus 로고
    • Early biofilm formation on microtiter plates is not correlated with the invasive disease potential of Streptococcus pneumoniae
    • Lizcano, A., Chin, T., Sauer, K., Tuomanen, E. I. & Orihuela, C. J. Early biofilm formation on microtiter plates is not correlated with the invasive disease potential of Streptococcus pneumoniae. Microb. Pathog. 48, 124-130 (2010).
    • (2010) Microb. Pathog. , vol.48 , pp. 124-130
    • Lizcano, A.1    Chin, T.2    Sauer, K.3    Tuomanen, E.I.4    Orihuela, C.J.5
  • 14
    • 1642405248 scopus 로고    scopus 로고
    • B-defensins and LL-37 in bronchoalveolar lavage fluid of patients with cystic fibrosis
    • Chen, C. I. U., Schaller-Bals, S., Paul, K. P., Wahn, U. & Bals, R. b-defensins and LL-37 in bronchoalveolar lavage fluid of patients with cystic fibrosis. J. Cyst. Fibros. 3, 45-50 (2004).
    • (2004) J. Cyst. Fibros. , vol.3 , pp. 45-50
    • Chen, C.I.U.1    Schaller-Bals, S.2    Paul, K.P.3    Wahn, U.4    Bals, R.5
  • 15
    • 73849117463 scopus 로고    scopus 로고
    • Generic and specific adaptive responses of Streptococcus pneumoniae to challenge with three distinct antimicrobial peptides, bacitracin, LL-37, and nisin
    • Majchrzykiewicz, J. A., Kuipers, O. P. & Bijlsma, J. J. Generic and specific adaptive responses of Streptococcus pneumoniae to challenge with three distinct antimicrobial peptides, bacitracin, LL-37, and nisin. Antimicrob. Agents Chemother. 54, 440-451 (2010).
    • (2010) Antimicrob. Agents Chemother. , vol.54 , pp. 440-451
    • Majchrzykiewicz, J.A.1    Kuipers, O.P.2    Bijlsma, J.J.3
  • 16
    • 0002774418 scopus 로고
    • Murein hydrolases and the lytic and killing action of penicillin
    • Tomasz, A. & Holtje, J. Murein hydrolases and the lytic and killing action of penicillin. Microbiology 1977, 209-215 (1977).
    • (1977) Microbiology , vol.1977 , pp. 209-215
    • Tomasz, A.1    Holtje, J.2
  • 17
    • 16244401405 scopus 로고    scopus 로고
    • Function of neisserial outer membrane phospholipase A in autolysis and assessment of its vaccine potential
    • Bos, M. P. et al. Function of neisserial outer membrane phospholipase A in autolysis and assessment of its vaccine potential. Infect. Immun. 73, 2222-2231 (2005).
    • (2005) Infect. Immun. , vol.73 , pp. 2222-2231
    • Bos, M.P.1
  • 19
    • 0005413121 scopus 로고
    • Mechanism of action of penicillin: Triggering of the pneumococcal autolytic enzyme by inhibitors of cell wall synthesis
    • Tomasz, A. & Waks, S. Mechanism of action of penicillin: triggering of the pneumococcal autolytic enzyme by inhibitors of cell wall synthesis. Proc. Natl Acad. Sci. USA 72, 4162-4166 (1975).
    • (1975) Proc. Natl Acad. Sci. USA , vol.72 , pp. 4162-4166
    • Tomasz, A.1    Waks, S.2
  • 20
    • 0025070744 scopus 로고
    • Autolysins are direct involved in the bactericidal effect caused by penicillin in wild type and in tolerant pneumococci
    • Lopez, R., Ronda, C. & Garcia, E. Autolysins are direct involved in the bactericidal effect caused by penicillin in wild type and in tolerant pneumococci. FEMS Microbiol. Lett. 54, 317-322 (1990).
    • (1990) FEMS Microbiol. Lett. , vol.54 , pp. 317-322
    • Lopez, R.1    Ronda, C.2    Garcia, E.3
  • 21
    • 0016429293 scopus 로고
    • Coordinated incorporation of nascent peptidoglycan and teichoic acid into pneumococcal cell walls and conservation of peptidoglycan during growth
    • Tomasz, A., McDonnell, M., Westphal, M. & Zanati, E. Coordinated incorporation of nascent peptidoglycan and teichoic acid into pneumococcal cell walls and conservation of peptidoglycan during growth. J. Biol. Chem. 250, 337-341 (1975).
    • (1975) J. Biol. Chem. , vol.250 , pp. 337-341
    • Tomasz, A.1    McDonnell, M.2    Westphal, M.3    Zanati, E.4
  • 22
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff, M. Antimicrobial peptides of multicellular organisms. Nature 415, 389-395 (2002).
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 23
    • 0035910508 scopus 로고    scopus 로고
    • Specific binding of nisin to the peptidoglycan precursor lipid II combines pore formation and inhibition of cell wall biosynthesis for potent antibiotic activity
    • Wiedemann, I. et al. Specific binding of nisin to the peptidoglycan precursor lipid II combines pore formation and inhibition of cell wall biosynthesis for potent antibiotic activity. J. Biol. Chem. 276, 1772-1779 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 1772-1779
    • Wiedemann, I.1
  • 24
    • 0038298097 scopus 로고    scopus 로고
    • Ramoplanin inhibits bacterial transglycosylases by binding as a dimer to lipid II
    • Hu, Y., Helm, J. S., Chen, L., Ye, X. Y. & Walker, S. Ramoplanin inhibits bacterial transglycosylases by binding as a dimer to lipid II. J. Am. Chem. Soc. 125, 8736-8737 (2003).
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 8736-8737
    • Hu, Y.1    Helm, J.S.2    Chen, L.3    Ye, X.Y.4    Walker, S.5
  • 25
    • 77952693839 scopus 로고    scopus 로고
    • Human beta-defensin 3 inhibits cell wall biosynthesis in Staphylococci
    • Sass, V. et al. Human beta-defensin 3 inhibits cell wall biosynthesis in Staphylococci. Infect. Immun. 78, 2793-2800 (2010).
    • (2010) Infect. Immun. , vol.78 , pp. 2793-2800
    • Sass, V.1
  • 26
    • 0033579207 scopus 로고    scopus 로고
    • Use of the cell wall precursor lipid II by a pore-forming peptide antibiotic
    • Breukink, E. et al. Use of the cell wall precursor lipid II by a pore-forming peptide antibiotic. Science 286, 2361-2364 (1999).
    • (1999) Science , vol.286 , pp. 2361-2364
    • Breukink, E.1
  • 27
    • 21144432881 scopus 로고    scopus 로고
    • Initiation and synthesis of the Streptococcus pneumoniae type 3 capsule on a phosphatidylglycerol membrane anchor
    • Cartee, R. T., Forsee, W. T. & Yother, J. Initiation and synthesis of the Streptococcus pneumoniae type 3 capsule on a phosphatidylglycerol membrane anchor. J. Bacteriol. 187, 4470-4479 (2005).
    • (2005) J. Bacteriol. , vol.187 , pp. 4470-4479
    • Cartee, R.T.1    Forsee, W.T.2    Yother, J.3
  • 28
    • 0033529627 scopus 로고    scopus 로고
    • The human antibacterial cathelicidin, hCAP-18, is bound to lipoproteins in plasma
    • Sorensen, O., Bratt, T., Johnsen, A. H., Madsen, M. T. & Borregaard, N. The human antibacterial cathelicidin, hCAP-18, is bound to lipoproteins in plasma. J. Biol. Chem. 274, 22445-22451 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 22445-22451
    • Sorensen, O.1    Bratt, T.2    Johnsen, A.H.3    Madsen, M.T.4    Borregaard, N.5
  • 29
    • 0031906480 scopus 로고    scopus 로고
    • Association of intrastrain phase variation in quantity of capsular polysaccharide and teichoic acid with the virulence of Streptococcus pneumoniae
    • Kim, J. O. & Weiser, J. N. Association of intrastrain phase variation in quantity of capsular polysaccharide and teichoic acid with the virulence of Streptococcus pneumoniae. J. Infect. Dis. 177, 368-377 (1998).
    • (1998) J. Infect. Dis. , vol.177 , pp. 368-377
    • Kim, J.O.1    Weiser, J.N.2
  • 30
    • 0029934982 scopus 로고    scopus 로고
    • Relationship between phase variation in colony morphology, intrastrain variation in cell wall physiology, and nasopharyngeal colonization by Streptococcus pneumoniae
    • Weiser, J. N., Markiewicz, Z., Tuomanen, E. I. & Wani, J. H. Relationship between phase variation in colony morphology, intrastrain variation in cell wall physiology, and nasopharyngeal colonization by Streptococcus pneumoniae. Infect. Immun. 64, 2240-2245 (1996).
    • (1996) Infect. Immun. , vol.64 , pp. 2240-2245
    • Weiser, J.N.1    Markiewicz, Z.2    Tuomanen, E.I.3    Wani, J.H.4
  • 31
    • 0033929389 scopus 로고    scopus 로고
    • Differential protein expression in phenotypic variants of Streptococcus pneumoniae
    • Overweg, K. et al. Differential protein expression in phenotypic variants of Streptococcus pneumoniae. Infect. Immun. 68, 4604-4610 (2000).
    • (2000) Infect. Immun. , vol.68 , pp. 4604-4610
    • Overweg, K.1
  • 32
    • 79953871095 scopus 로고    scopus 로고
    • Streptococcus pneumoniae isolates from middle ear fluid and nasopharynx of children with acute otitis media exhibit phase variation
    • Arai, J. et al. Streptococcus pneumoniae isolates from middle ear fluid and nasopharynx of children with acute otitis media exhibit phase variation. J. Clin. Microbiol. 49, 1646-1649 (2011).
    • (2011) J. Clin. Microbiol. , vol.49 , pp. 1646-1649
    • Arai, J.1
  • 33
    • 0036067905 scopus 로고    scopus 로고
    • The genes encoding virulenceassociated proteins and the capsule of Streptococcus pneumoniae are upregulated and differentially expressed in vivo
    • Ogunniyi, A. D., Giammarinaro, P. & Paton, J. C. The genes encoding virulenceassociated proteins and the capsule of Streptococcus pneumoniae are upregulated and differentially expressed in vivo. Microbiology 148, 2045-2053 (2002).
    • (2002) Microbiology , vol.148 , pp. 2045-2053
    • Ogunniyi, A.D.1    Giammarinaro, P.2    Paton, J.C.3
  • 34
    • 0029852095 scopus 로고    scopus 로고
    • Immune response to type III group B streptococcal polysaccharide-tetanus toxoid conjugate vaccine
    • Kasper, D. L. et al. Immune response to type III group B streptococcal polysaccharide-tetanus toxoid conjugate vaccine. J. Clin. Invest. 98, 2308-2314 (1996).
    • (1996) J. Clin. Invest. , vol.98 , pp. 2308-2314
    • Kasper, D.L.1
  • 35
    • 0037075260 scopus 로고    scopus 로고
    • Use of a Staphylococcus aureus conjugate vaccine in patients receiving hemodialysis
    • Shinefield, H. et al. Use of a Staphylococcus aureus conjugate vaccine in patients receiving hemodialysis. N. Engl. J. Med. 346, 491-496 (2002).
    • (2002) N. Engl. J. Med. , vol.346 , pp. 491-496
    • Shinefield, H.1
  • 36
    • 23644436035 scopus 로고    scopus 로고
    • The epidemiology of childhood pneumococcal disease in the United States in the era of conjugate vaccine use
    • Toltzis, P. & Jacobs, M. R. The epidemiology of childhood pneumococcal disease in the United States in the era of conjugate vaccine use. Infect. Dis. Clin. North Am. 19, 629-645 (2005).
    • (2005) Infect. Dis. Clin. North Am. , vol.19 , pp. 629-645
    • Toltzis, P.1    Jacobs, M.R.2
  • 37
    • 79251544864 scopus 로고    scopus 로고
    • Rapid pneumococcal evolution in response to clinical interventions
    • Croucher, N. J. et al. Rapid pneumococcal evolution in response to clinical interventions. Science 331, 430-434 (2011).
    • (2011) Science , vol.331 , pp. 430-434
    • Croucher, N.J.1
  • 38
    • 0019542941 scopus 로고
    • Multiple antibiotic resistance in South African strains of Streptococcus pneumoniae: Mechanism of resistance to beta-lactam antibiotics
    • Zighelboim, S. & Tomasz, A. Multiple antibiotic resistance in South African strains of Streptococcus pneumoniae: mechanism of resistance to beta-lactam antibiotics. Rev. Infect. Dis. 3, 267-276 (1981).
    • (1981) Rev. Infect. Dis. , vol.3 , pp. 267-276
    • Zighelboim, S.1    Tomasz, A.2
  • 39
    • 0028307194 scopus 로고
    • Phase variation in pneumococcal opacity: Relationship between colonial morphology and nasopharyngeal colonization
    • Weiser, J. N., Austrian, R., Sreenivasan, P. K. & Masure, H. R. Phase variation in pneumococcal opacity: relationship between colonial morphology and nasopharyngeal colonization. Infect. Immun. 62, 2582-2589 (1994).
    • (1994) Infect. Immun. , vol.62 , pp. 2582-2589
    • Weiser, J.N.1    Austrian, R.2    Sreenivasan, P.K.3    Masure, H.R.4
  • 40
    • 7644243116 scopus 로고    scopus 로고
    • Release of DNA into the medium by competent Streptococcus pneumoniae: Kinetics, mechanism and stability of the liberated DNA
    • Moscoso, M. & Claverys, J.-P. Release of DNA into the medium by competent Streptococcus pneumoniae: kinetics, mechanism and stability of the liberated DNA. Mol. Microbiol. 54, 783-794 (2004).
    • (2004) Mol. Microbiol. , vol.54 , pp. 783-794
    • Moscoso, M.1    Claverys, J.-P.2
  • 41
    • 33751119902 scopus 로고    scopus 로고
    • Biofilm formation by Streptococcus pneumoniae: Role of choline, extracellular DNA, and capsular polysaccharide in microbial accretion
    • Moscoso, M., García, E. & López, R. Biofilm formation by Streptococcus pneumoniae: role of choline, extracellular DNA, and capsular polysaccharide in microbial accretion. J. Bacteriol. 188, 7785-7795 (2006).
    • (2006) J. Bacteriol. , vol.188 , pp. 7785-7795
    • Moscoso, M.1    García, E.2    López, R.3
  • 42
    • 84921370338 scopus 로고    scopus 로고
    • Pleiotropic effects of cell wall amidase LytA on Streptococcus pneumoniae sensitivity to the host immune response
    • Ramos-Sevillano, E. et al. Pleiotropic effects of cell wall amidase LytA on Streptococcus pneumoniae sensitivity to the host immune response. Infect. Immun. 83, 591-603 (2015).
    • (2015) Infect. Immun. , vol.83 , pp. 591-603
    • Ramos-Sevillano, E.1
  • 43
    • 0022001683 scopus 로고
    • The induction of meningeal inflammation by components of the pneumococcal cell wall
    • Tuomanen, E., Liu, H., Hengstler, B., Zak, O. & Tomasz, A. The induction of meningeal inflammation by components of the pneumococcal cell wall. J. Infect. Dis. 151, 859-868 (1985).
    • (1985) J. Infect. Dis. , vol.151 , pp. 859-868
    • Tuomanen, E.1    Liu, H.2    Hengstler, B.3    Zak, O.4    Tomasz, A.5
  • 45
    • 75349097193 scopus 로고    scopus 로고
    • Detection of pneumolysin and autolysin genes among antibiotic resistant Streptococcus pneumoniae in invasive infections
    • Sourav, S. et al. Detection of pneumolysin and autolysin genes among antibiotic resistant Streptococcus pneumoniae in invasive infections. Indian. J. Med. Microbiol. 28, 34-39 (2010).
    • (2010) Indian. J. Med. Microbiol. , vol.28 , pp. 34-39
    • Sourav, S.1
  • 46
    • 84855245939 scopus 로고    scopus 로고
    • Pep27 and lytA in vancomycin-tolerant pneumococci
    • Olivares, A. et al. pep27 and lytA in vancomycin-tolerant pneumococci. J. Microbiol. Biotechnol. 21, 1345-1351 (2011).
    • (2011) J. Microbiol. Biotechnol. , vol.21 , pp. 1345-1351
    • Olivares, A.1
  • 47
    • 0036305458 scopus 로고    scopus 로고
    • Molecular peculiarities of the lytA gene isolated from clinical pneumococcal strains that are bile insoluble
    • Obregon, V. et al. Molecular peculiarities of the lytA gene isolated from clinical pneumococcal strains that are bile insoluble. J. Clin. Microbiol. 40, 2545-2554 (2002).
    • (2002) J. Clin. Microbiol. , vol.40 , pp. 2545-2554
    • Obregon, V.1
  • 48
    • 84859483346 scopus 로고    scopus 로고
    • LytA, major autolysin of Streptococcus pneumoniae, requires access to nascent peptidoglycan
    • Mellroth, P. et al. LytA, major autolysin of Streptococcus pneumoniae, requires access to nascent peptidoglycan. J. Biol. Chem. 287, 11018-11029 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 11018-11029
    • Mellroth, P.1
  • 49
    • 52649112223 scopus 로고    scopus 로고
    • Calcium efflux is essential for bacterial survival in the eukaryotic host
    • Rosch, J. W., Sublett, J., Gao, G., Wang, Y.-D. & Tuomanen, E. I. Calcium efflux is essential for bacterial survival in the eukaryotic host. Mol. Microbiol. 70, 435-444 (2008).
    • (2008) Mol. Microbiol. , vol.70 , pp. 435-444
    • Rosch, J.W.1    Sublett, J.2    Gao, G.3    Wang, Y.-D.4    Tuomanen, E.I.5
  • 50
    • 0024556150 scopus 로고
    • Engineering hybrid genes without the use of restriction enzymes: Gene splicing by overlap extension
    • Horton, R. M., Hunt, H. D., Ho, S. N., Pullen, J. K. & Pease, L. R. Engineering hybrid genes without the use of restriction enzymes: gene splicing by overlap extension. Gene 77, 61-68 (1989).
    • (1989) Gene , vol.77 , pp. 61-68
    • Horton, R.M.1    Hunt, H.D.2    Ho, S.N.3    Pullen, J.K.4    Pease, L.R.5
  • 51
    • 0034090275 scopus 로고    scopus 로고
    • The RofA binding site in streptococcus pyogenes is utilized in multiple transcriptional pathways
    • Granok, A. B., Parsonage, D., Ross, R. P. & Caparon, M. G. The RofA binding site in streptococcus pyogenes is utilized in multiple transcriptional pathways. J. Bacteriol. 182, 1529-1540 (2000).
    • (2000) J. Bacteriol. , vol.182 , pp. 1529-1540
    • Granok, A.B.1    Parsonage, D.2    Ross, R.P.3    Caparon, M.G.4
  • 52
    • 0024295204 scopus 로고
    • Structural requirements of choline derivatives for 'conversion' of pneumococcal amidase A new single-step procedure for purification of this autolysin
    • Sanz, J. M., Lopez, R. & Garcia, J. L. Structural requirements of choline derivatives for 'conversion' of pneumococcal amidase A new single-step procedure for purification of this autolysin. FEBS Lett. 232, 308-312 (1988).
    • (1988) FEBS Lett. , vol.232 , pp. 308-312
    • Sanz, J.M.1    Lopez, R.2    Garcia, J.L.3
  • 53
    • 0033963751 scopus 로고    scopus 로고
    • Signal transduction by a death signal peptide: Uncovering the mechanism of bacterial killing by penicillin
    • Novak, R., Charpentier, E., Braun, J. S. & Tuomanen, E. Signal transduction by a death signal peptide: uncovering the mechanism of bacterial killing by penicillin. Mol. Cell 5, 49-57 (2000).
    • (2000) Mol. Cell , vol.5 , pp. 49-57
    • Novak, R.1    Charpentier, E.2    Braun, J.S.3    Tuomanen, E.4
  • 54
    • 46449092820 scopus 로고    scopus 로고
    • Convergence of Regulatory Networks on the Pilus Locus of Streptococcus pneumoniae
    • Rosch, J. W., Mann, B., Thornton, J., Sublett, J. & Tuomanen, E. Convergence of Regulatory Networks on the Pilus Locus of Streptococcus pneumoniae. Infect. Immun. 76, 3187-3196 (2008).
    • (2008) Infect. Immun. , vol.76 , pp. 3187-3196
    • Rosch, J.W.1    Mann, B.2    Thornton, J.3    Sublett, J.4    Tuomanen, E.5
  • 55
    • 84898964001 scopus 로고    scopus 로고
    • Broadly protective protein-based pneumococcal vaccine composed of pneumolysin toxoid-CbpA peptide recombinant fusion protein
    • Mann, B. et al. Broadly protective protein-based pneumococcal vaccine composed of pneumolysin toxoid-CbpA peptide recombinant fusion protein. J. Infect. Dis. 209, 1116-1125 (2014).
    • (2014) J. Infect. Dis. , vol.209 , pp. 1116-1125
    • Mann, B.1
  • 56
    • 31844451911 scopus 로고    scopus 로고
    • Multifunctional role of choline binding protein G in pneumococcal pathogenesis
    • Mann, B. et al. Multifunctional role of choline binding protein G in pneumococcal pathogenesis. Infect. Immun. 74, 821-829 (2006).
    • (2006) Infect. Immun. , vol.74 , pp. 821-829
    • Mann, B.1
  • 57
    • 0035055410 scopus 로고    scopus 로고
    • Visualizing pneumococcal infections in the lungs of live mice using bioluminescent Streptococcus pneumoniae transformed with a novel Gram-positive lux transposon
    • Francis, K. P. et al. Visualizing pneumococcal infections in the lungs of live mice using bioluminescent Streptococcus pneumoniae transformed with a novel Gram-positive lux transposon. Infect. Immun. 69, 3350-3358 (2001).
    • (2001) Infect. Immun. , vol.69 , pp. 3350-3358
    • Francis, K.P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.