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Volumn 155, Issue 7, 2009, Pages 2401-2410

Surface-associated lipoprotein PpmA of Streptococcus pneumoniae is involved in colonization in a strain-specific manner

Author keywords

[No Author keywords available]

Indexed keywords

LIPOPROTEIN; PUTATIVE PROTEINASE MATURATION PROTEIN A; UNCLASSIFIED DRUG;

EID: 69949143516     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/mic.0.026765-0     Document Type: Article
Times cited : (51)

References (54)
  • 1
    • 0028028168 scopus 로고
    • Immunization of mice with pneumolysin toxoid confers a significant degree of protection against at least nine serotypes of Streptococcus pneumoniae
    • Alexander, J. E., Lock, R. A., Peeters, C. C., Poolman, J. T., Andrew, P. W., Mitchell, T. J., Hansman, D. & Paton, J. C. (1994). Immunization of mice with pneumolysin toxoid confers a significant degree of protection against at least nine serotypes of Streptococcus pneumoniae. Infect Immun 62, 5683-5688.
    • (1994) Infect Immun , vol.62 , pp. 5683-5688
    • Alexander, J.E.1    Lock, R.A.2    Peeters, C.C.3    Poolman, J.T.4    Andrew, P.W.5    Mitchell, T.J.6    Hansman, D.7    Paton, J.C.8
  • 3
    • 0034931519 scopus 로고    scopus 로고
    • alpha-Enolase of Streptococcus pneumoniae is a plasmin(ogen) binding protein displayed on the bacterial cell surface
    • Bergmann, S., Rohde, M., Chhatwal, G. S. & Hammerschmidt, S. (2001). alpha-Enolase of Streptococcus pneumoniae is a plasmin(ogen) binding protein displayed on the bacterial cell surface. Mol Microbiol 40, 1273-1287.
    • (2001) Mol Microbiol , vol.40 , pp. 1273-1287
    • Bergmann, S.1    Rohde, M.2    Chhatwal, G.S.3    Hammerschmidt, S.4
  • 4
    • 0038501069 scopus 로고    scopus 로고
    • Identification of a novel plasmin(ogen)-binding motif in surface displayed alpha-enolase of Streptococcus pneumoniae
    • Bergmann, S., Wild, D., Diekmann, O., Frank, R., Bracht, D., Chhatwal, G. S. & Hammerschmidt, S. (2003). Identification of a novel plasmin(ogen)-binding motif in surface displayed alpha-enolase of Streptococcus pneumoniae. Mol Microbiol 49, 411-423.
    • (2003) Mol Microbiol , vol.49 , pp. 411-423
    • Bergmann, S.1    Wild, D.2    Diekmann, O.3    Frank, R.4    Bracht, D.5    Chhatwal, G.S.6    Hammerschmidt, S.7
  • 5
    • 1842535489 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase of Streptococcus pneumoniae is a surface-displayed plasminogen-binding protein
    • Bergmann, S., Rohde, M. & Hammerschmidt, S. (2004). Glyceraldehyde-3-phosphate dehydrogenase of Streptococcus pneumoniae is a surface-displayed plasminogen-binding protein. Infect Immun 72, 2416-2419.
    • (2004) Infect Immun , vol.72 , pp. 2416-2419
    • Bergmann, S.1    Rohde, M.2    Hammerschmidt, S.3
  • 6
    • 0041989857 scopus 로고    scopus 로고
    • Contribution of a response regulator to the virulence of Streptococcus pneumoniae is strain dependent
    • Blue, C. E. & Mitchell, T. J. (2003). Contribution of a response regulator to the virulence of Streptococcus pneumoniae is strain dependent. Infect Immun 71, 4405-4413.
    • (2003) Infect Immun , vol.71 , pp. 4405-4413
    • Blue, C.E.1    Mitchell, T.J.2
  • 7
    • 1442299471 scopus 로고    scopus 로고
    • Streptococcus pneumoniae colonisation: The key to pneumococcal disease
    • Bogaert, D., de Groot, R. & Hermans, P. W. (2004). Streptococcus pneumoniae colonisation: the key to pneumococcal disease. Lancet Infect Dis 4, 144-154.
    • (2004) Lancet Infect Dis , vol.4 , pp. 144-154
    • Bogaert, D.1    de Groot, R.2    Hermans, P.W.3
  • 8
    • 35648958724 scopus 로고    scopus 로고
    • Analysis of the in vitro transcriptional response of human pharyngeal epithelial cells to adherent Streptococcus pneumoniae: Evidence for a distinct response to encapsulated strains
    • Bootsma, H. J., Egmont-Petersen, M. & Hermans, P. W. (2007). Analysis of the in vitro transcriptional response of human pharyngeal epithelial cells to adherent Streptococcus pneumoniae: evidence for a distinct response to encapsulated strains. Infect Immun 75, 5489-5499.
    • (2007) Infect Immun , vol.75 , pp. 5489-5499
    • Bootsma, H.J.1    Egmont-Petersen, M.2    Hermans, P.W.3
  • 9
    • 25444447356 scopus 로고    scopus 로고
    • Nasal colonization with Streptococcus pneumoniae includes subpopulations of surface and invasive pneumococci
    • Briles, D. E., Novak, L., Hotomi, M., van Ginkel, F. W. & King, J. (2005). Nasal colonization with Streptococcus pneumoniae includes subpopulations of surface and invasive pneumococci. Infect Immun 73, 6945-6951.
    • (2005) Infect Immun , vol.73 , pp. 6945-6951
    • Briles, D.E.1    Novak, L.2    Hotomi, M.3    van Ginkel, F.W.4    King, J.5
  • 10
    • 0036717717 scopus 로고    scopus 로고
    • The human polymeric immunoglobulin receptor facilitates invasion of epithelial cells by Streptococcus pneumoniae in a strain-specific and cell type-specific manner
    • Brock, S. C., McGraw, P. A., Wright, P. F. & Crowe, J. E., Jr (2002). The human polymeric immunoglobulin receptor facilitates invasion of epithelial cells by Streptococcus pneumoniae in a strain-specific and cell type-specific manner. Infect Immun 70, 5091-5095.
    • (2002) Infect Immun , vol.70 , pp. 5091-5095
    • Brock, S.C.1    McGraw, P.A.2    Wright, P.F.3    Crowe Jr, J.E.4
  • 11
    • 34548552756 scopus 로고    scopus 로고
    • Search for genes essential for pneumococcal transformation: The RadA DNA repair protein plays a role in genomic recombination of donor DNA
    • Burghout, P., Bootsma, H. J., Kloosterman, T. G., Bijlsma, J. J., de Jongh, C. E., Kuipers, O. P. & Hermans, P. W. (2007). Search for genes essential for pneumococcal transformation: the RadA DNA repair protein plays a role in genomic recombination of donor DNA. J Bacteriol 189, 6540-6550.
    • (2007) J Bacteriol , vol.189 , pp. 6540-6550
    • Burghout, P.1    Bootsma, H.J.2    Kloosterman, T.G.3    Bijlsma, J.J.4    de Jongh, C.E.5    Kuipers, O.P.6    Hermans, P.W.7
  • 12
    • 0026684173 scopus 로고
    • Legionella pneumophila mip gene potentiates intracellular infection of protozoa and human macrophages
    • Cianciotto, N. P. & Fields, B. S. (1992). Legionella pneumophila mip gene potentiates intracellular infection of protozoa and human macrophages. Proc Natl Acad Sci U S A 89, 5188-5191.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 5188-5191
    • Cianciotto, N.P.1    Fields, B.S.2
  • 13
    • 0024522755 scopus 로고
    • A Legionella pneumophila gene encoding a species-specific surface protein potentiates initiation of intracellular infection
    • Cianciotto, N. P., Eisenstein, B. I., Mody, C. H., Toews, G. B. & Engleberg, N. C. (1989). A Legionella pneumophila gene encoding a species-specific surface protein potentiates initiation of intracellular infection. Infect Immun 57, 1255-1262.
    • (1989) Infect Immun , vol.57 , pp. 1255-1262
    • Cianciotto, N.P.1    Eisenstein, B.I.2    Mody, C.H.3    Toews, G.B.4    Engleberg, N.C.5
  • 14
    • 0029165459 scopus 로고
    • Streptococcus pneumoniae anchor to activated human cells by the receptor for platelet-activating factor
    • Cundell, D. R., Gerard, N. P., Gerard, C., Idanpaan-Heikkila, I. & Tuomanen, E. I. (1995). Streptococcus pneumoniae anchor to activated human cells by the receptor for platelet-activating factor. Nature 377, 435-438.
    • (1995) Nature , vol.377 , pp. 435-438
    • Cundell, D.R.1    Gerard, N.P.2    Gerard, C.3    Idanpaan-Heikkila, I.4    Tuomanen, E.I.5
  • 15
    • 0032527831 scopus 로고    scopus 로고
    • A new heat-shock gene, ppiD, encodes a peptidyl-prolyl isomerase required for folding of outer membrane proteins in Escherichia coli
    • Dartigalongue, C. & Raina, S. (1998). A new heat-shock gene, ppiD, encodes a peptidyl-prolyl isomerase required for folding of outer membrane proteins in Escherichia coli. EMBO J 17, 3968-3980.
    • (1998) EMBO J , vol.17 , pp. 3968-3980
    • Dartigalongue, C.1    Raina, S.2
  • 16
    • 0030868591 scopus 로고    scopus 로고
    • Competence and virulence of Streptococcus pneumoniae: Adc and PsaA mutants exhibit a requirement for Zn and Mn resulting from inactivation of putative ABC metal permeases
    • Dintilhac, A., Alloing, G., Granadel, C. & Claverys, J. P. (1997). Competence and virulence of Streptococcus pneumoniae: Adc and PsaA mutants exhibit a requirement for Zn and Mn resulting from inactivation of putative ABC metal permeases. Mol Microbiol 25, 727-739.
    • (1997) Mol Microbiol , vol.25 , pp. 727-739
    • Dintilhac, A.1    Alloing, G.2    Granadel, C.3    Claverys, J.P.4
  • 17
    • 0030692139 scopus 로고    scopus 로고
    • All cyclophilins and FK506 binding proteins are, individually and collectively, dispensable for viability in Saccharomyces cerevisiae
    • Dolinski, K., Muir, S., Cardenas, M. & Heitman, J. (1997). All cyclophilins and FK506 binding proteins are, individually and collectively, dispensable for viability in Saccharomyces cerevisiae. Proc Natl Acad Sci U S A 94, 13093-13098.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 13093-13098
    • Dolinski, K.1    Muir, S.2    Cardenas, M.3    Heitman, J.4
  • 18
    • 0036322876 scopus 로고    scopus 로고
    • The peptidyl-prolyl isomerase motif is lacking in PmpA, the PrsA-like protein involved in the secretion machinery of Lactococcus lactis
    • Drouault, S., Anba, J., Bonneau, S., Bolotin, A., Ehrlich, S. D. & Renault, P. (2002). The peptidyl-prolyl isomerase motif is lacking in PmpA, the PrsA-like protein involved in the secretion machinery of Lactococcus lactis. Appl Environ Microbiol 68, 3932-3942.
    • (2002) Appl Environ Microbiol , vol.68 , pp. 3932-3942
    • Drouault, S.1    Anba, J.2    Bonneau, S.3    Bolotin, A.4    Ehrlich, S.D.5    Renault, P.6
  • 19
    • 1342304130 scopus 로고    scopus 로고
    • Ectodomains 3 and 4 of human polymeric Immunoglobulin receptor (hpIgR) mediate invasion of Streptococcus pneumoniae into the epithelium
    • Elm, C., Braathen, R., Bergmann, S., Frank, R., Vaerman, J. P., Kaetzel, C. S., Chhatwal, G. S., Johansen, F. E. & Hammerschmidt, S. (2004). Ectodomains 3 and 4 of human polymeric Immunoglobulin receptor (hpIgR) mediate invasion of Streptococcus pneumoniae into the epithelium. J Biol Chem 279, 6296-6304.
    • (2004) J Biol Chem , vol.279 , pp. 6296-6304
    • Elm, C.1    Braathen, R.2    Bergmann, S.3    Frank, R.4    Vaerman, J.P.5    Kaetzel, C.S.6    Chhatwal, G.S.7    Johansen, F.E.8    Hammerschmidt, S.9
  • 20
    • 0035082972 scopus 로고    scopus 로고
    • Mosaic genes and mosaic chromosomes: Intraand interspecies genomic variation of Streptococcus pneumoniae
    • Hakenbeck, R., Balmelle, N., Weber, B., Gardès, C., Keck, W. & de Saizieu, A. (2001). Mosaic genes and mosaic chromosomes: intraand interspecies genomic variation of Streptococcus pneumoniae. Infect Immun 69, 2477-2486.
    • (2001) Infect Immun , vol.69 , pp. 2477-2486
    • Hakenbeck, R.1    Balmelle, N.2    Weber, B.3    Gardès, C.4    Keck, W.5    de Saizieu, A.6
  • 21
    • 31844450829 scopus 로고    scopus 로고
    • Adherence molecules of pathogenic pneumococci
    • Hammerschmidt, S. (2006). Adherence molecules of pathogenic pneumococci. Curr Opin Microbiol 9, 12-20.
    • (2006) Curr Opin Microbiol , vol.9 , pp. 12-20
    • Hammerschmidt, S.1
  • 22
    • 0033003470 scopus 로고    scopus 로고
    • Identification of pneumococcal surface protein A as a lactoferrin-binding protein of Streptococcus pneumoniae
    • Hammerschmidt, S., Bethe, G., Remane, P. H. & Chhatwal, G. S. (1999). Identification of pneumococcal surface protein A as a lactoferrin-binding protein of Streptococcus pneumoniae. Infect Immun 67, 1683-1687.
    • (1999) Infect Immun , vol.67 , pp. 1683-1687
    • Hammerschmidt, S.1    Bethe, G.2    Remane, P.H.3    Chhatwal, G.S.4
  • 23
    • 0034061865 scopus 로고    scopus 로고
    • Species-specific binding of human secretory component to SpsA protein of Streptococcus pneumoniae via a hexapeptide motif
    • Hammerschmidt, S., Tillig, M. P., Wolff, S., Vaerman, J. P. & Chhatwal, G. S. (2000). Species-specific binding of human secretory component to SpsA protein of Streptococcus pneumoniae via a hexapeptide motif. Mol Microbiol 36, 726-736.
    • (2000) Mol Microbiol , vol.36 , pp. 726-736
    • Hammerschmidt, S.1    Tillig, M.P.2    Wolff, S.3    Vaerman, J.P.4    Chhatwal, G.S.5
  • 24
    • 23344444876 scopus 로고    scopus 로고
    • Illustration of pneumococcal polysaccharide capsule during adherence and invasion of epithelial cells
    • Hammerschmidt, S., Wolff, S., Hocke, A., Rosseau, S., Muller, E. & Rohde, M. (2005). Illustration of pneumococcal polysaccharide capsule during adherence and invasion of epithelial cells. Infect Immun 73, 4653-4667.
    • (2005) Infect Immun , vol.73 , pp. 4653-4667
    • Hammerschmidt, S.1    Wolff, S.2    Hocke, A.3    Rosseau, S.4    Muller, E.5    Rohde, M.6
  • 25
    • 0036047758 scopus 로고    scopus 로고
    • Large-scale identification of serotype 4 Streptococcus pneumoniae virulence factors
    • Hava, D. L. & Camilli, A. (2002). Large-scale identification of serotype 4 Streptococcus pneumoniae virulence factors. Mol Microbiol 45, 1389-1406.
    • (2002) Mol Microbiol , vol.45 , pp. 1389-1406
    • Hava, D.L.1    Camilli, A.2
  • 29
    • 0034786512 scopus 로고    scopus 로고
    • The pavA gene of Streptococcus pneumoniae encodes a fibronectin-binding protein that is essential for virulence
    • Holmes, A. R., McNab, R., Millsap, K. W., Rohde, M., Hammerschmidt, S., Mawdsley, J. L. & Jenkinson, H. F. (2001). The pavA gene of Streptococcus pneumoniae encodes a fibronectin-binding protein that is essential for virulence. Mol Microbiol 41, 1395-1408.
    • (2001) Mol Microbiol , vol.41 , pp. 1395-1408
    • Holmes, A.R.1    McNab, R.2    Millsap, K.W.3    Rohde, M.4    Hammerschmidt, S.5    Mawdsley, J.L.6    Jenkinson, H.F.7
  • 30
    • 0032434029 scopus 로고    scopus 로고
    • Use of highly encapsulated Streptococcus pneumoniae strains in a flow-cytometric assay for assessment of the phagocytic capacity of serotype-specific antibodies
    • Jansen, W. T., Gootjes, J., Zelle, M., Madore, D. V., Verhoef, J., Snippe, H. & Verheul, A. F. (1998). Use of highly encapsulated Streptococcus pneumoniae strains in a flow-cytometric assay for assessment of the phagocytic capacity of serotype-specific antibodies. Clin Diagn Lab Immunol 5, 703-710.
    • (1998) Clin Diagn Lab Immunol , vol.5 , pp. 703-710
    • Jansen, W.T.1    Gootjes, J.2    Zelle, M.3    Madore, D.V.4    Verhoef, J.5    Snippe, H.6    Verheul, A.F.7
  • 31
    • 3042685720 scopus 로고    scopus 로고
    • The Ami-AliA/AliB permease of Streptococcus pneumoniae is involved in nasopharyngeal colonization but not in invasive disease
    • Kerr, A. R., Adrian, P. V., Estevão, S., de Groot, R., Alloing, G., Claverys, J. P., Mitchell, T. J. & Hermans, P. W. (2004). The Ami-AliA/AliB permease of Streptococcus pneumoniae is involved in nasopharyngeal colonization but not in invasive disease. Infect Immun 72, 3902-3906.
    • (2004) Infect Immun , vol.72 , pp. 3902-3906
    • Kerr, A.R.1    Adrian, P.V.2    Estevão, S.3    de Groot, R.4    Alloing, G.5    Claverys, J.P.6    Mitchell, T.J.7    Hermans, P.W.8
  • 32
    • 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. (1998). 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) J Infect Dis , vol.177 , pp. 368-377
    • Kim, J.O.1    Weiser, J.N.2
  • 33
    • 33845957666 scopus 로고    scopus 로고
    • Genome sequence of Avery's virulent serotype 2 strain D39 of Streptococcus pneumoniae and comparison with that of unencapsulated laboratory strain R6
    • Lanie, J. A., Ng, W. L., Kazmierczak, K. M., Andrzejewski, T. M., Davidsen, T. M., Wayne, K. J., Tettelin, H., Glass, J. I. & Winkler, M. E. (2007). Genome sequence of Avery's virulent serotype 2 strain D39 of Streptococcus pneumoniae and comparison with that of unencapsulated laboratory strain R6. J Bacteriol 189, 38-51.
    • (2007) J Bacteriol , vol.189 , pp. 38-51
    • Lanie, J.A.1    Ng, W.L.2    Kazmierczak, K.M.3    Andrzejewski, T.M.4    Davidsen, T.M.5    Wayne, K.J.6    Tettelin, H.7    Glass, J.I.8    Winkler, M.E.9
  • 35
    • 0029918686 scopus 로고    scopus 로고
    • SurA assists the folding of Escherichia coli outer membrane proteins
    • Lazar, S. W. & Kolter, R. (1996). SurA assists the folding of Escherichia coli outer membrane proteins. J Bacteriol 178, 1770-1773.
    • (1996) J Bacteriol , vol.178 , pp. 1770-1773
    • Lazar, S.W.1    Kolter, R.2
  • 36
    • 0029916122 scopus 로고    scopus 로고
    • A human peptidyl-prolyl isomerase essential for regulation of mitosis
    • Lu, K. P., Hanes, S. D. & Hunter, T. (1996). A human peptidyl-prolyl isomerase essential for regulation of mitosis. Nature 380, 544-547.
    • (1996) Nature , vol.380 , pp. 544-547
    • Lu, K.P.1    Hanes, S.D.2    Hunter, T.3
  • 37
    • 0032476656 scopus 로고    scopus 로고
    • A role for trigger factor and an Rgg-like regulator in the transcription, secretion and processing of the cysteine proteinase of Streptococcus pyogenes
    • Lyon, W. R., Gibson, C. M. & Caparon, M. G. (1998). A role for trigger factor and an Rgg-like regulator in the transcription, secretion and processing of the cysteine proteinase of Streptococcus pyogenes. EMBO J 17, 6263-6275.
    • (1998) EMBO J , vol.17 , pp. 6263-6275
    • Lyon, W.R.1    Gibson, C.M.2    Caparon, M.G.3
  • 38
    • 0035016182 scopus 로고    scopus 로고
    • Requirement for capsule in colonization by Streptococcus pneumoniae
    • Magee, A. D. & Yother, J. (2001). Requirement for capsule in colonization by Streptococcus pneumoniae. Infect Immun 69, 3755-3761.
    • (2001) Infect Immun , vol.69 , pp. 3755-3761
    • Magee, A.D.1    Yother, J.2
  • 39
    • 33846015873 scopus 로고    scopus 로고
    • Capsule enhances pneumococcal colonization by limiting mucus-mediated clearance
    • Nelson, A. L., Roche, A. M., Gould, J. M., Chim, K., Ratner, A. J. & Weiser, J. N. (2007). Capsule enhances pneumococcal colonization by limiting mucus-mediated clearance. Infect Immun 75, 83-90.
    • (2007) Infect Immun , vol.75 , pp. 83-90
    • Nelson, A.L.1    Roche, A.M.2    Gould, J.M.3    Chim, K.4    Ratner, A.J.5    Weiser, J.N.6
  • 40
    • 0033916706 scopus 로고    scopus 로고
    • The putative proteinase maturation protein A of Streptococcus pneumoniae is a conserved surface protein with potential to elicit protective immune responses
    • Overweg, K., Kerr, A., Sluijter, M., Jackson, M. H., Mitchell, T. J., de Jong, A. P., de Groot, R. & Hermans, P. W. (2000a). The putative proteinase maturation protein A of Streptococcus pneumoniae is a conserved surface protein with potential to elicit protective immune responses. Infect Immun 68, 4180-4188.
    • (2000) Infect Immun , vol.68 , pp. 4180-4188
    • Overweg, K.1    Kerr, A.2    Sluijter, M.3    Jackson, M.H.4    Mitchell, T.J.5    de Jong, A.P.6    de Groot, R.7    Hermans, P.W.8
  • 42
    • 0028124244 scopus 로고
    • Confirmation of the existence of a third family among peptidyl-prolyl cis/trans isomerases. Amino acid sequence and recombinant production of parvulin
    • Rahfeld, J. U., Rucknagel, K. P., Schelbert, B., Ludwig, B., Hacker, J., Mann, K. & Fischer, G. (1994). Confirmation of the existence of a third family among peptidyl-prolyl cis/trans isomerases. Amino acid sequence and recombinant production of parvulin. FEBS Lett 352, 180-184.
    • (1994) FEBS Lett , vol.352 , pp. 180-184
    • Rahfeld, J.U.1    Rucknagel, K.P.2    Schelbert, B.3    Ludwig, B.4    Hacker, J.5    Mann, K.6    Fischer, G.7
  • 44
    • 0030983804 scopus 로고    scopus 로고
    • Contribution of novel choline-binding proteins to adherence, colonization and immunogenicity of Streptococcus pneumoniae
    • Rosenow, C., Ryan, P., Weiser, J. N., Johnson, S., Fontan, P., Ortqvist, A. & Masure, H. R. (1997). Contribution of novel choline-binding proteins to adherence, colonization and immunogenicity of Streptococcus pneumoniae. Mol Microbiol 25, 819-829.
    • (1997) Mol Microbiol , vol.25 , pp. 819-829
    • Rosenow, C.1    Ryan, P.2    Weiser, J.N.3    Johnson, S.4    Fontan, P.5    Ortqvist, A.6    Masure, H.R.7
  • 45
    • 0030476750 scopus 로고    scopus 로고
    • SurA, a periplasmic protein with peptidyl-prolyl isomerase activity, participates in the assembly of outer membrane porins
    • Rouviere, P. E. & Gross, C. A. (1996). SurA, a periplasmic protein with peptidyl-prolyl isomerase activity, participates in the assembly of outer membrane porins. Genes Dev 10, 3170-3182.
    • (1996) Genes Dev , vol.10 , pp. 3170-3182
    • Rouviere, P.E.1    Gross, C.A.2
  • 46
    • 0018345747 scopus 로고
    • Pneumococcal adherence to human epithelial cells
    • Selinger, D. S. & Reed, W. P. (1979). Pneumococcal adherence to human epithelial cells. Infect Immun 23, 545-548.
    • (1979) Infect Immun , vol.23 , pp. 545-548
    • Selinger, D.S.1    Reed, W.P.2
  • 47
    • 4544281498 scopus 로고    scopus 로고
    • PspA protects Streptococcus pneumoniae from killing by apolactoferrin, and antibody to PspA enhances killing of pneumococci by apolactoferrin
    • Shaper, M., Hollingshead, S. K., Benjamin, W. H., Jr & Briles, D. E. (2004). PspA protects Streptococcus pneumoniae from killing by apolactoferrin, and antibody to PspA enhances killing of pneumococci by apolactoferrin. Infect Immun 72, 5031-5040.
    • (2004) Infect Immun , vol.72 , pp. 5031-5040
    • Shaper, M.1    Hollingshead, S.K.2    Benjamin Jr, W.H.3    Briles, D.E.4
  • 48
    • 0033941198 scopus 로고    scopus 로고
    • Non-typeable Haemophilus influenzae adhere to and invade human bronchial epithelial cells via an interaction of lipooligosaccharide with the PAF receptor
    • Swords, W. E., Buscher, B. A., Ver Steeg, I. K., Preston, A., Nichols, W. A., Weiser, J. N., Gibson, B. W. & Apicella, M. A. (2000). Non-typeable Haemophilus influenzae adhere to and invade human bronchial epithelial cells via an interaction of lipooligosaccharide with the PAF receptor. Mol Microbiol 37, 13-27.
    • (2000) Mol Microbiol , vol.37 , pp. 13-27
    • Swords, W.E.1    Buscher, B.A.2    Ver Steeg, I.K.3    Preston, A.4    Nichols, W.A.5    Weiser, J.N.6    Gibson, B.W.7    Apicella, M.A.8
  • 49
    • 0029756760 scopus 로고    scopus 로고
    • Uptake of Streptococcus pneumoniae by respiratory epithelial cells
    • Talbot, U. M., Paton, A. W. & Paton, J. C. (1996). Uptake of Streptococcus pneumoniae by respiratory epithelial cells. Infect Immun 64, 3772-3777.
    • (1996) Infect Immun , vol.64 , pp. 3772-3777
    • Talbot, U.M.1    Paton, A.W.2    Paton, J.C.3
  • 50
    • 0035919670 scopus 로고    scopus 로고
    • Tettelin, H., Nelson, K. E., Paulsen, I. T., Eisen, J. A., Read, T. D., Peterson, S., Heidelberg, J., DeBoy, R. T., Haft, D. H. & other authors (2001). Complete genome sequence of a virulent isolate of Streptococcus pneumoniae. Science 293, 498-506.
    • Tettelin, H., Nelson, K. E., Paulsen, I. T., Eisen, J. A., Read, T. D., Peterson, S., Heidelberg, J., DeBoy, R. T., Haft, D. H. & other authors (2001). Complete genome sequence of a virulent isolate of Streptococcus pneumoniae. Science 293, 498-506.
  • 52
    • 2442446271 scopus 로고    scopus 로고
    • Structure-function analysis of PrsA reveals roles for the parvulin-like and flanking N- and C-terminal domains in protein folding and secretion in Bacillus subtilis
    • Vitikainen, M., Lappalainen, I., Seppala, R., Antelmann, H., Boer, H., Taira, S., Savilahti, H., Hecker, M., Vihinen, M. & other authors (2004). Structure-function analysis of PrsA reveals roles for the parvulin-like and flanking N- and C-terminal domains in protein folding and secretion in Bacillus subtilis. J Biol Chem 279, 19302-19314.
    • (2004) J Biol Chem , vol.279 , pp. 19302-19314
    • Vitikainen, M.1    Lappalainen, I.2    Seppala, R.3    Antelmann, H.4    Boer, H.5    Taira, S.6    Savilahti, H.7    Hecker, M.8    Vihinen, M.9
  • 53
    • 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. (1994). Phase variation in pneumococcal opacity: relationship between colonial morphology and nasopharyngeal colonization. Infect Immun 62, 2582-2589.
    • (1994) Infect Immun , vol.62 , pp. 2582-2589
    • Weiser, J.N.1    Austrian, R.2    Sreenivasan, P.K.3    Masure, H.R.4
  • 54
    • 0034664821 scopus 로고    scopus 로고
    • The polymeric immunoglobulin receptor translocates pneumococci across human nasopharyngeal epithelial cells
    • Zhang, J. R., Mostov, K. E., Lamm, M. E., Nanno, M., Shimida, S., Ohwaki, M. & Tuomanen, E. (2000). The polymeric immunoglobulin receptor translocates pneumococci across human nasopharyngeal epithelial cells. Cell 102, 827-837.
    • (2000) Cell , vol.102 , pp. 827-837
    • Zhang, J.R.1    Mostov, K.E.2    Lamm, M.E.3    Nanno, M.4    Shimida, S.5    Ohwaki, M.6    Tuomanen, E.7


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