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Volumn 71, Issue 12, 2003, Pages 7043-7052

Characterization of an Extracellular Virulence Factor Made by Group A Streptococcus with Homology to the Listeria monocytogenes Internalin Family of Proteins

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; HISTIDINE; LEUCINE; LEUCINE RICH REPEAT; M PROTEIN; NITROGEN; UNCLASSIFIED DRUG; VIRULENCE FACTOR;

EID: 10744223970     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/IAI.71.12.7043-7052.2003     Document Type: Article
Times cited : (43)

References (83)
  • 2
    • 0037323799 scopus 로고    scopus 로고
    • Significant increase in the prevalence of erythromycin-resistant, clindamycin- and miocamycin-susceptible (M phenotype) Streptococcus pyogenes in Spain
    • Alos, J. I., B. Aracil, J. Oteo, and J. L. Gomez-Garces. 2003. Significant increase in the prevalence of erythromycin-resistant, clindamycin- and miocamycin-susceptible (M phenotype) Streptococcus pyogenes in Spain. J. Antimicrob. Chemother. 51:333-337.
    • (2003) J. Antimicrob. Chemother. , vol.51 , pp. 333-337
    • Alos, J.I.1    Aracil, B.2    Oteo, J.3    Gomez-Garces, J.L.4
  • 4
    • 0036267501 scopus 로고    scopus 로고
    • InIA- but not InIB-mediated internalization of Listeria monocytogenes by non-phagocytic mammalian cells needs the support of other internalins
    • Bergmann, B., D. Raffelsbauer, M. Kuhn, M. Goetz, S. Hom, and W. Goebel. 2002. InIA- but not InIB-mediated internalization of Listeria monocytogenes by non-phagocytic mammalian cells needs the support of other internalins. Mol. Microbiol. 43:557-570.
    • (2002) Mol. Microbiol. , vol.43 , pp. 557-570
    • Bergmann, B.1    Raffelsbauer, D.2    Kuhn, M.3    Goetz, M.4    Hom, S.5    Goebel, W.6
  • 5
    • 0036707468 scopus 로고    scopus 로고
    • InIB, a surface protein of Listeria monocytogenes that behaves as an invasin and a growth factor
    • Bierne, H., and P. Cossart. 2002. InIB, a surface protein of Listeria monocytogenes that behaves as an invasin and a growth factor. J. Cell Sci. 115:3357-3367.
    • (2002) J. Cell Sci. , vol.115 , pp. 3357-3367
    • Bierne, H.1    Cossart, P.2
  • 6
    • 0033920567 scopus 로고    scopus 로고
    • Interactions between Listeria monocytogenes and host mammalian cells
    • Braun, L., and P. Cossart. 2000. Interactions between Listeria monocytogenes and host mammalian cells. Microbes Infect. 2:803-811.
    • (2000) Microbes Infect. , vol.2 , pp. 803-811
    • Braun, L.1    Cossart, P.2
  • 7
    • 0032862519 scopus 로고    scopus 로고
    • The 213-amino-acid leucine-rich repeat region of the Listeria monocytogenes InIB protein is sufficient for entry into mammalian cells, stimulation of PI 3-kinase and membrane ruffling
    • Braun, L., F. Nato, B. Payrastre, J. C. Mazie, and P. Cossart. 1999. The 213-amino-acid leucine-rich repeat region of the Listeria monocytogenes InIB protein is sufficient for entry into mammalian cells, stimulation of PI 3-kinase and membrane ruffling. Mol. Microbiol. 34:10-23.
    • (1999) Mol. Microbiol. , vol.34 , pp. 10-23
    • Braun, L.1    Nato, F.2    Payrastre, B.3    Mazie, J.C.4    Cossart, P.5
  • 8
    • 0031594726 scopus 로고    scopus 로고
    • The InIB protein of Listeria monocytogenes is sufficient to promote entry into mammalian cells
    • Braun, L., H. Ohayon, and P. Cossart. 1998. The InIB protein of Listeria monocytogenes is sufficient to promote entry into mammalian cells. Mol. Microbiol. 27:1077-1087.
    • (1998) Mol. Microbiol. , vol.27 , pp. 1077-1087
    • Braun, L.1    Ohayon, H.2    Cossart, P.3
  • 9
    • 0037162392 scopus 로고    scopus 로고
    • Hint, Fhit, and GalT: Function, structure, evolution, and mechanism of three branches of the histidine triad superfamily of nucleotide hydrolases and transferases
    • Brenner, C. 2002. Hint, Fhit, and GalT: function, structure, evolution, and mechanism of three branches of the histidine triad superfamily of nucleotide hydrolases and transferases. Biochemistry 41:9003-9014.
    • (2002) Biochemistry , vol.41 , pp. 9003-9014
    • Brenner, C.1
  • 10
    • 0035139884 scopus 로고    scopus 로고
    • Identification of Rgg-regulated exoproteins of Streptococcus pyogenes
    • Chaussee, M. S., R. O. Watson, J. C. Smoot, and J. M. Musser. 2001. Identification of Rgg-regulated exoproteins of Streptococcus pyogenes. Infect. Immun. 69:822-831.
    • (2001) Infect. Immun. , vol.69 , pp. 822-831
    • Chaussee, M.S.1    Watson, R.O.2    Smoot, J.C.3    Musser, J.M.4
  • 11
    • 0028267319 scopus 로고
    • Expression vectors for affinity purification and radiolabeling of proteins using Escherichia coli as host
    • Chen, B. P. C., and T. Hai. 1994. Expression vectors for affinity purification and radiolabeling of proteins using Escherichia coli as host. Gene 139:73-75.
    • (1994) Gene , vol.139 , pp. 73-75
    • Chen, B.P.C.1    Hai, T.2
  • 12
    • 0037213412 scopus 로고    scopus 로고
    • Invasion of mammalian cells by Listeria monocytogenes: Functional mimicry to subvert cellular functions
    • Cossart, P., J. Pizarro-Cerda, and M. Lecuit. 2003. Invasion of mammalian cells by Listeria monocytogenes: functional mimicry to subvert cellular functions. Trends Cell Biol. 13:23-31.
    • (2003) Trends Cell Biol. , vol.13 , pp. 23-31
    • Cossart, P.1    Pizarro-Cerda, J.2    Lecuit, M.3
  • 13
    • 0006334728 scopus 로고    scopus 로고
    • Intracellular invasion by Streptococcus pyogenes: Invasins, host receptors, and relevance to human disease
    • V. A. Fischetti, R. P. Novick, J. J. Ferretti, D. A. Portnoy, and J. I. Rood (ed.). ASM Press, Washington, D.C.
    • Cue, D., P. E. Dombeck, and P. P. Cleary. 2000. Intracellular invasion by Streptococcus pyogenes: invasins, host receptors, and relevance to human disease, p. 27-33. In V. A. Fischetti, R. P. Novick, J. J. Ferretti, D. A. Portnoy, and J. I. Rood (ed.), Gram-positive pathogens. ASM Press, Washington, D.C.
    • (2000) Gram-Positive Pathogens , pp. 27-33
    • Cue, D.1    Dombeck, P.E.2    Cleary, P.P.3
  • 14
    • 0033939735 scopus 로고    scopus 로고
    • Pathogenesis of group A streptococcal infections
    • Cunningham, M. W. 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
  • 15
    • 0035818973 scopus 로고    scopus 로고
    • Group A Streptococcus tissue invasion by CD44-mediated cell signalling
    • Cywes, C., and M. R. Wessels. 2001. Group A Streptococcus tissue invasion by CD44-mediated cell signalling. Nature 414:648-652.
    • (2001) Nature , vol.414 , pp. 648-652
    • Cywes, C.1    Wessels, M.R.2
  • 16
    • 0032904116 scopus 로고    scopus 로고
    • High-frequency intracellular invasion of epithelial cells by serotype M1 group A streptococci: M1 protein-mediated invasion and cytoskeletal rearrangements
    • Dombek, P. E., D. Cue, J. Sedgewick, H. Lam, S. Ruschkowski, B. B. Finlay, and P. P. Cleary. 1999. High-frequency intracellular invasion of epithelial cells by serotype M1 group A streptococci: M1 protein-mediated invasion and cytoskeletal rearrangements. Mol. Microbiol. 31:859-870.
    • (1999) Mol. Microbiol. , vol.31 , pp. 859-870
    • Dombek, P.E.1    Cue, D.2    Sedgewick, J.3    Lam, H.4    Ruschkowski, S.5    Finlay, B.B.6    Cleary, P.P.7
  • 17
    • 0029063839 scopus 로고
    • Entry of Listeria monocytogenes into hepatocytes requires expression of InIB, a surface protein of the internalin multigene family
    • Dramsi, S., I. Biswas, E. Maguin, L. Braun, P. Mastroeni, and P. Cossart. 1995. Entry of Listeria monocytogenes into hepatocytes requires expression of InIB, a surface protein of the internalin multigene family. Mol. Microbiol. 16:251-261.
    • (1995) Mol. Microbiol. , vol.16 , pp. 251-261
    • Dramsi, S.1    Biswas, I.2    Maguin, E.3    Braun, L.4    Mastroeni, P.5    Cossart, P.6
  • 18
    • 0027219643 scopus 로고
    • Internalin-mediated invasion of epithelial cells by Listeria monocytogenes is regulated by the bacterial growth state, temperature and the pleiotropic activator prfA
    • Dramsi, S., C. Kocks, C. Forestier, and P. Cossart. 1993. Internalin-mediated invasion of epithelial cells by Listeria monocytogenes is regulated by the bacterial growth state, temperature and the pleiotropic activator prfA. Mol. Microbiol. 9:931-941.
    • (1993) Mol. Microbiol. , vol.9 , pp. 931-941
    • Dramsi, S.1    Kocks, C.2    Forestier, C.3    Cossart, P.4
  • 19
    • 0029745347 scopus 로고    scopus 로고
    • A new PrfA-regulated gene of Listeria monocytogenes encoding a small, secreted protein which belongs to the family of internalins
    • Engelbrecht, F., S. K. Chun, C. Ochs, J. Hess, F. Lottspeich, W. Goebel, and Z. Sokolovic. 1996. A new PrfA-regulated gene of Listeria monocytogenes encoding a small, secreted protein which belongs to the family of internalins. Mol. Microbiol. 21:823-837.
    • (1996) Mol. Microbiol. , vol.21 , pp. 823-837
    • Engelbrecht, F.1    Chun, S.K.2    Ochs, C.3    Hess, J.4    Lottspeich, F.5    Goebel, W.6    Sokolovic, Z.7
  • 20
    • 0035965144 scopus 로고    scopus 로고
    • Unusual molecular architecture of the Yersinia pestis cytotoxin YopM: A leucine-rich repeat protein with the shortest repeating unit
    • Evdokimov, A. G., D. E. Anderson, K. M. Routzahn, and D. S. Waugh. 2001. Unusual molecular architecture of the Yersinia pestis cytotoxin YopM: a leucine-rich repeat protein with the shortest repeating unit. J. Mol. Biol. 312:807-821.
    • (2001) J. Mol. Biol. , vol.312 , pp. 807-821
    • Evdokimov, A.G.1    Anderson, D.E.2    Routzahn, K.M.3    Waugh, D.S.4
  • 21
    • 0035822268 scopus 로고    scopus 로고
    • Association between erythromycin resistance and ability to enter human respiratory cells in group A streptococci
    • Facinelli, B., C. Spinaci, G. Magi, E. Giovanetti, and P. E. Varaldo. 2001. Association between erythromycin resistance and ability to enter human respiratory cells in group A streptococci. Lancet 358:30-33.
    • (2001) Lancet , vol.358 , pp. 30-33
    • Facinelli, B.1    Spinaci, C.2    Magi, G.3    Giovanetti, E.4    Varaldo, P.E.5
  • 22
    • 0034110502 scopus 로고    scopus 로고
    • Shigella flexneri IpaH(7.8) facilitates escape of virulent bacteria from the endocytic vacuoles of mouse and human macrophages
    • Fernandez-Prada, C. M., D. L. Hoover, B. D. Tall, A. B. Hartman, J. Kopelowitz, and M. M. Venkatesan. 2000. Shigella flexneri IpaH(7.8) facilitates escape of virulent bacteria from the endocytic vacuoles of mouse and human macrophages. Infect. Immun. 68:3608-3619.
    • (2000) Infect. Immun. , vol.68 , pp. 3608-3619
    • Fernandez-Prada, C.M.1    Hoover, D.L.2    Tall, B.D.3    Hartman, A.B.4    Kopelowitz, J.5    Venkatesan, M.M.6
  • 24
    • 0017693561 scopus 로고
    • Streptococcal M protein: An antiphagocytic molecule assembled on the cell wall
    • Fischetti, V. A., E. C. Gotschlich, G. Siviglia, and J. B. Zabriskie. 1977. Streptococcal M protein: an antiphagocytic molecule assembled on the cell wall. J. Infect. Dis. 136(Suppl.):S222-S233.
    • (1977) J. Infect. Dis. , vol.136 , Issue.SUPPL.
    • Fischetti, V.A.1    Gotschlich, E.C.2    Siviglia, G.3    Zabriskie, J.B.4
  • 25
    • 0031912707 scopus 로고    scopus 로고
    • Immunoglobulins to group A streptococcal surface molecules decrease adherence to and invasion of human pharyngeal cells
    • Fluckiger, U., K. F. Jones, and V. A. Fischetti. 1998. Immunoglobulins to group A streptococcal surface molecules decrease adherence to and invasion of human pharyngeal cells. Infect. Immun. 66:974-979.
    • (1998) Infect. Immun. , vol.66 , pp. 974-979
    • Fluckiger, U.1    Jones, K.F.2    Fischetti, V.A.3
  • 26
    • 0025739814 scopus 로고
    • Entry of L. monocytogenes into cells is mediated by internalin, a repeat protein reminiscent of surface antigens from gram-positive cocci
    • Gaillard, J. L., P. Berche, C. Frehel, E. Gouin, and P. Cossart. 1991. Entry of L. monocytogenes into cells is mediated by internalin, a repeat protein reminiscent of surface antigens from gram-positive cocci. Cell 65:1127-1141.
    • (1991) Cell , vol.65 , pp. 1127-1141
    • Gaillard, J.L.1    Berche, P.2    Frehel, C.3    Gouin, E.4    Cossart, P.5
  • 29
    • 0011158540 scopus 로고
    • The use of precipitin analysis in agar for the study of human streptococcal infections III. The purification of some of the antigens detected by these methods
    • Halbert, S. P. 1958. The use of precipitin analysis in agar for the study of human streptococcal infections III. The purification of some of the antigens detected by these methods. J. Exp. Med. 108:385-410.
    • (1958) J. Exp. Med. , vol.108 , pp. 385-410
    • Halbert, S.P.1
  • 30
    • 72949147455 scopus 로고
    • The use of precipitin analysis in agar for the study of human streptococcal infections. IV. Further observations on the purification of group A extracellular antigens
    • Halbert, S. P., and T. Auerbach. 1960. The use of precipitin analysis in agar for the study of human streptococcal infections. IV. Further observations on the purification of group A extracellular antigens. J. Exp. Med. 113:131-157.
    • (1960) J. Exp. Med. , vol.113 , pp. 131-157
    • Halbert, S.P.1    Auerbach, T.2
  • 31
    • 0000095655 scopus 로고
    • The analysis of streptococcal infections. VI. Immunoelectrophoretic observations on extracellular antigens detectable with human antibodies
    • Halbert, S. P., and S. L. Keatinge. 1961. The analysis of streptococcal infections. VI. Immunoelectrophoretic observations on extracellular antigens detectable with human antibodies. J. Exp. Med. 113:1013-1028.
    • (1961) J. Exp. Med. , vol.113 , pp. 1013-1028
    • Halbert, S.P.1    Keatinge, S.L.2
  • 32
    • 0011213737 scopus 로고
    • The use of precipitin analysis in agar for the study of human streptococcal infections. I. Oudin technic
    • Halbert, S. P., L. Swick, and C. Sonn. 1955. The use of precipitin analysis in agar for the study of human streptococcal infections. I. Oudin technic. J. Exp. Med. 101:539-556.
    • (1955) J. Exp. Med. , vol.101 , pp. 539-556
    • Halbert, S.P.1    Swick, L.2    Sonn, C.3
  • 33
    • 0000571709 scopus 로고
    • The use of precipitin analysis in agar for the study of human streptococcal infections. II. Ouchterlony and Oakley techniques
    • Halbert, S. P., L. Swick, and C. Sonn. 1955. The use of precipitin analysis in agar for the study of human streptococcal infections. II. Ouchterlony and Oakley techniques. J. Exp. Med. 101:557-575.
    • (1955) J. Exp. Med. , vol.101 , pp. 557-575
    • Halbert, S.P.1    Swick, L.2    Sonn, C.3
  • 34
    • 0025268544 scopus 로고
    • Sequence and molecular characterization of a multicopy invasion plasmid antigen gene, ipaH, of Shigella flexneri
    • Hartman, A. B., M. Venkatesan, E. V. Oaks, and J. M. Buysse. 1990. Sequence and molecular characterization of a multicopy invasion plasmid antigen gene, ipaH, of Shigella flexneri. J. Bacteriol. 172:1905-1915.
    • (1990) J. Bacteriol. , vol.172 , pp. 1905-1915
    • Hartman, A.B.1    Venkatesan, M.2    Oaks, E.V.3    Buysse, J.M.4
  • 37
    • 0036232188 scopus 로고    scopus 로고
    • Assessment of the ability to model proteins with leucine-rich repeats in light of the latest structural information
    • Kajava, A. V., and B. Kobe. 2002. Assessment of the ability to model proteins with leucine-rich repeats in light of the latest structural information. Protein Sci. 11:1082-1090.
    • (2002) Protein Sci. , vol.11 , pp. 1082-1090
    • Kajava, A.V.1    Kobe, B.2
  • 38
    • 0027931766 scopus 로고
    • Vaccination with streptococcal extracellular cysteine protease (interleukin-1 beta convertase) protects mice against challenge with heterologous group A streptococci
    • Kapur, V., J. T. Maffei, R. S. Greer, L. L. Li, G. J. Adams, and J. M. Musser. 1994. Vaccination with streptococcal extracellular cysteine protease (interleukin-1 beta convertase) protects mice against challenge with heterologous group A streptococci. Microb. Pathog. 16:443-450.
    • (1994) Microb. Pathog. , vol.16 , pp. 443-450
    • Kapur, V.1    Maffei, J.T.2    Greer, R.S.3    Li, L.L.4    Adams, G.J.5    Musser, J.M.6
  • 39
    • 0030296688 scopus 로고    scopus 로고
    • Horizontal gene transfer among group A streptococci: Implications for pathogenesis and epidemiology
    • Kehoe, M. A., V. Kapur, A. M. Whatmore, and J. M. Musser. 1996. Horizontal gene transfer among group A streptococci: implications for pathogenesis and epidemiology. Trends Microbiol. 4:436-443.
    • (1996) Trends Microbiol. , vol.4 , pp. 436-443
    • Kehoe, M.A.1    Kapur, V.2    Whatmore, A.M.3    Musser, J.M.4
  • 40
    • 0027718173 scopus 로고
    • Crystal structure of porcine ribonuclease inhibitor, a protein with leucine-rich repeats
    • Kobe, B., and J. Deisenhofer. 1993. Crystal structure of porcine ribonuclease inhibitor, a protein with leucine-rich repeats. Nature 366:751-756.
    • (1993) Nature , vol.366 , pp. 751-756
    • Kobe, B.1    Deisenhofer, J.2
  • 41
    • 0028080261 scopus 로고
    • The leucine-rich repeat: A versatile binding motif
    • Kobe, B., and J. Deisenhofer. 1994. The leucine-rich repeat: a versatile binding motif. Trends Biochem. Sci. 19:415-421.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 415-421
    • Kobe, B.1    Deisenhofer, J.2
  • 42
    • 0035692811 scopus 로고    scopus 로고
    • The leucine-rich repeat as a protein recognition motif
    • Kobe, B., and A. V. Kajava. 2001. The leucine-rich repeat as a protein recognition motif. Curr. Opin. Struct. Biol. 11:725-732.
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 725-732
    • Kobe, B.1    Kajava, A.V.2
  • 43
    • 0028046519 scopus 로고
    • Group A streptococci efficiently invade human respiratory epithelial cells
    • LaPenta, D., C. Rubens, E. Chi, and P. P. Cleary. 1994. Group A streptococci efficiently invade human respiratory epithelial cells. Proc. Natl. Acad. Sci. USA 91:12115-12119.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12115-12119
    • LaPenta, D.1    Rubens, C.2    Chi, E.3    Cleary, P.P.4
  • 44
    • 0030830882 scopus 로고    scopus 로고
    • Internalin of Listeria monocytogenes with an intact leucine-rich repeat region is sufficient to promote internalization
    • Lecuit, M., H. Ohayon, L. Braun, J. Mengaud, and P. Cossart. 1997. Internalin of Listeria monocytogenes with an intact leucine-rich repeat region is sufficient to promote internalization. Infect. Immun. 65:5309-5319.
    • (1997) Infect. Immun. , vol.65 , pp. 5309-5319
    • Lecuit, M.1    Ohayon, H.2    Braun, L.3    Mengaud, J.4    Cossart, P.5
  • 46
    • 0028986196 scopus 로고
    • Crystal structure of the A domain from the alpha subunit of integrin CR3 (CD11b/CD18)
    • Lee, J. O., P. Rieu, M. A. Arnaout, and R. Liddington. 1995. Crystal structure of the A domain from the alpha subunit of integrin CR3 (CD11b/CD18). Cell 80:631-638.
    • (1995) Cell , vol.80 , pp. 631-638
    • Lee, J.O.1    Rieu, P.2    Arnaout, M.A.3    Liddington, R.4
  • 47
    • 0034442652 scopus 로고    scopus 로고
    • Identification and immunogenicity of group A Streptococcus culture supernatant proteins
    • Lei, B., S. Mackie, S. Lukomski, and J. M. Musser. 2000. Identification and immunogenicity of group A Streptococcus culture supernatant proteins. Infect. Immun. 68:6807-6818.
    • (2000) Infect. Immun. , vol.68 , pp. 6807-6818
    • Lei, B.1    Mackie, S.2    Lukomski, S.3    Musser, J.M.4
  • 48
    • 0025006850 scopus 로고
    • YopM inhibits platelet aggregation and is necessary for virulence of Yersinia pestis in mice
    • Leung, K. Y., B. S. Reisner, and S. C. Straley. 1990. YopM inhibits platelet aggregation and is necessary for virulence of Yersinia pestis in mice. Infect. Immun. 58:3262-3271.
    • (1990) Infect. Immun. , vol.58 , pp. 3262-3271
    • Leung, K.Y.1    Reisner, B.S.2    Straley, S.C.3
  • 49
    • 0024364388 scopus 로고
    • The yopM gene of Yersinia pestis encodes a released protein having homology with the human platelet surface protein GPIb alpha
    • Leung, K. Y., and S. C. Straley. 1989. The yopM gene of Yersinia pestis encodes a released protein having homology with the human platelet surface protein GPIb alpha. J. Bacteriol. 171:4623-4632.
    • (1989) J. Bacteriol. , vol.171 , pp. 4623-4632
    • Leung, K.Y.1    Straley, S.C.2
  • 50
    • 0030831990 scopus 로고    scopus 로고
    • Structure-based analysis of catalysis and substrate definition in the HIT protein family
    • Lima, C. D., M. G. Klein, and W. A. Hendrickson. 1997. Structure-based analysis of catalysis and substrate definition in the HIT protein family. Science 278:286-290.
    • (1997) Science , vol.278 , pp. 286-290
    • Lima, C.D.1    Klein, M.G.2    Hendrickson, W.A.3
  • 51
    • 0033955513 scopus 로고    scopus 로고
    • Nonpolar inactivation of the hypervariable streptococcal inhibitor of complement gene (sic) in serotype M1 Streptococcus pyogenes significantly decreases mouse mucosal colonization
    • Lukomski, S., N. P. Hoe, I. Abdi, J. Rurangirwa, P. Kordari, M. Liu, S. J. Dou, G. G. Adams, and J. M. Musser. 2000. Nonpolar inactivation of the hypervariable streptococcal inhibitor of complement gene (sic) in serotype M1 Streptococcus pyogenes significantly decreases mouse mucosal colonization. Infect. Immun. 68:535-542.
    • (2000) Infect. Immun. , vol.68 , pp. 535-542
    • Lukomski, S.1    Hoe, N.P.2    Abdi, I.3    Rurangirwa, J.4    Kordari, P.5    Liu, M.6    Dou, S.J.7    Adams, G.G.8    Musser, J.M.9
  • 52
    • 0034441340 scopus 로고    scopus 로고
    • Identification and characterization of the scl gene encoding a group A Streptococcus ektracellular protein virulence factor with similarity to human collagen
    • Lukomski, S., K. Nakashima, I. Abdi, V. J. Cipriano, R. M. Ireland, S. D. Reid, G. G. Adams, and J. M. Musser. 2000. Identification and characterization of the scl gene encoding a group A Streptococcus ektracellular protein virulence factor with similarity to human collagen. Infect. Immun. 68:6542-6553.
    • (2000) Infect. Immun. , vol.68 , pp. 6542-6553
    • Lukomski, S.1    Nakashima, K.2    Abdi, I.3    Cipriano, V.J.4    Ireland, R.M.5    Reid, S.D.6    Adams, G.G.7    Musser, J.M.8
  • 53
    • 0034254929 scopus 로고    scopus 로고
    • A framework for interpreting the leucine-rich repeats of the Listeria internalins
    • Marino, M., L. Braun, P. Cossart, and P. Ghosh. 2000. A framework for interpreting the leucine-rich repeats of the Listeria internalins. Proc. Natl. Acad. Sci. USA 97:8784-8788.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8784-8788
    • Marino, M.1    Braun, L.2    Cossart, P.3    Ghosh, P.4
  • 54
    • 0033256246 scopus 로고    scopus 로고
    • Structure of the InIB leucine-rich repeats, a domain that triggers host cell invasion by the bacterial pathogen L. monocytogenes
    • Marino, M., L. Braun, P. Cossart, and P. Ghosh. 1999. Structure of the InIB leucine-rich repeats, a domain that triggers host cell invasion by the bacterial pathogen L. monocytogenes. Mol. Cell 4:1063-1072.
    • (1999) Mol. Cell , vol.4 , pp. 1063-1072
    • Marino, M.1    Braun, L.2    Cossart, P.3    Ghosh, P.4
  • 55
    • 0038719729 scopus 로고    scopus 로고
    • The Yersinia virulence factor YopM forms a novel protein complex with two cellular kinases
    • McDonald, C., P. O. Vacratsis, J. B. Bliska, and J. E. Dixon. 2003. The Yersinia virulence factor YopM forms a novel protein complex with two cellular kinases. J. Biol. Chem. 278:18514-18523.
    • (2003) J. Biol. Chem. , vol.278 , pp. 18514-18523
    • McDonald, C.1    Vacratsis, P.O.2    Bliska, J.B.3    Dixon, J.E.4
  • 56
    • 0030753825 scopus 로고    scopus 로고
    • Role of mga in growth phase regulation of virulence genes of the group A Streptococcus
    • McIver, K. S., and J. R. Scott. 1997. Role of mga in growth phase regulation of virulence genes of the group A Streptococcus. J. Bacteriol. 179:5178-5187.
    • (1997) J. Bacteriol. , vol.179 , pp. 5178-5187
    • McIver, K.S.1    Scott, J.R.2
  • 57
    • 0037443060 scopus 로고    scopus 로고
    • Survival of Streptococcus pyogenes within host phagocytic cells: A pathogenic mechanism for persistence and systemic invasion
    • Medina, E., O. Goldmann, A. W. Toppel, and G. S. Chhatwal. 2003. Survival of Streptococcus pyogenes within host phagocytic cells: a pathogenic mechanism for persistence and systemic invasion. J. Infect. Dis. 187:597-603.
    • (2003) J. Infect. Dis. , vol.187 , pp. 597-603
    • Medina, E.1    Goldmann, O.2    Toppel, A.W.3    Chhatwal, G.S.4
  • 58
    • 0029869384 scopus 로고    scopus 로고
    • E-cadherin is the receptor for internalin, a surface protein required for entry of L. monocytogenes into epithelial cells
    • Mengaud, J., H. Ohayon, P. Gounon, R. M. Mege, and P. Cossart. 1996. E-cadherin is the receptor for internalin, a surface protein required for entry of L. monocytogenes into epithelial cells. Cell 84:923-932.
    • (1996) Cell , vol.84 , pp. 923-932
    • Mengaud, J.1    Ohayon, H.2    Gounon, P.3    Mege, R.M.4    Cossart, P.5
  • 59
    • 0032701087 scopus 로고    scopus 로고
    • Salmonella typhimurium leucine-rich repeat proteins are targeted to the SPI1 and SPI2 type III secretion systems
    • Miao, E. A., C. A. Scherer, R. M. Tsolis, R. A. Kingsley, L. G. Adams, A. J. Baumler, and S. I. Miller. 1999. Salmonella typhimurium leucine-rich repeat proteins are targeted to the SPI1 and SPI2 type III secretion systems. Mol. Microbiol. 34:850-864.
    • (1999) Mol. Microbiol. , vol.34 , pp. 850-864
    • Miao, E.A.1    Scherer, C.A.2    Tsolis, R.M.3    Kingsley, R.A.4    Adams, L.G.5    Baumler, A.J.6    Miller, S.I.7
  • 60
    • 0030903802 scopus 로고    scopus 로고
    • The fibronectin-binding protein of Streptococcus pyogenes, SfbI, is involved in the internalization of group A streptococci by epithelial cells
    • Molinari, G., S. R. Talay, P. Valentin-Weigand, M. Rohde, and G. S. Chhatwal. 1997. The fibronectin-binding protein of Streptococcus pyogenes, SfbI, is involved in the internalization of group A streptococci by epithelial cells. Infect. Immun. 65:1357-1363.
    • (1997) Infect. Immun. , vol.65 , pp. 1357-1363
    • Molinari, G.1    Talay, S.R.2    Valentin-Weigand, P.3    Rohde, M.4    Chhatwal, G.S.5
  • 61
    • 0025790953 scopus 로고
    • Streptococcus pyogenes causing toxic-shock-like syndrome and other invasive diseases: Clonal diversity and pyrogenic exotoxin expression
    • Musser, J. M., A. R. Hauser, M. H. Kim, P. M. Schlievert, K. Nelson, and R. K. Selander. 1991. Streptococcus pyogenes causing toxic-shock-like syndrome and other invasive diseases: clonal diversity and pyrogenic exotoxin expression. Proc. Natl. Acad. Sci. USA 88:2668-2672.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 2668-2672
    • Musser, J.M.1    Hauser, A.R.2    Kim, M.H.3    Schlievert, P.M.4    Nelson, K.5    Selander, R.K.6
  • 62
    • 77957100477 scopus 로고    scopus 로고
    • The revival of group A streptococcal diseases, with a commentary on staphylococcal toxic shock syndrome
    • R. M. Krause (ed.). Academic Press, New York, N.Y.
    • Musser, J. M., and R. M. Krause. 1998. The revival of group A streptococcal diseases, with a commentary on staphylococcal toxic shock syndrome, p. 185-218. In R. M. Krause (ed.), Emerging infections. Academic Press, New York, N.Y.
    • (1998) Emerging Infections , pp. 185-218
    • Musser, J.M.1    Krause, R.M.2
  • 63
    • 0023626652 scopus 로고
    • In vivo Streptococcus pyogenes C5a peptidase activity: Analysis using transposon- and nitrosoguanidine-induced mutants
    • O'Connor, S. P., and P. P. Cleary. 1987. In vivo Streptococcus pyogenes C5a peptidase activity: analysis using transposon- and nitrosoguanidine-induced mutants. J. Infect. Dis. 156:495-504.
    • (1987) J. Infect. Dis. , vol.156 , pp. 495-504
    • O'Connor, S.P.1    Cleary, P.P.2
  • 64
    • 0030998695 scopus 로고    scopus 로고
    • Inactivation of recombinant monocyte cAMP-specific phosphodiesterase by cAMP analog, 8-[(4-bromo-2,3-dioxobutyl)thio]adenosine 3′,5′-cyclic monophosphate
    • Omburo, G. A., T. J. Torphy, G. Scott, S. Jacobitz, R. F. Colman, and R. W. Colman. 1997. Inactivation of recombinant monocyte cAMP-specific phosphodiesterase by cAMP analog, 8-[(4-bromo-2,3-dioxobutyl)thio]adenosine 3′,5′-cyclic monophosphate. Blood 89:1019-1026.
    • (1997) Blood , vol.89 , pp. 1019-1026
    • Omburo, G.A.1    Torphy, T.J.2    Scott, G.3    Jacobitz, S.4    Colman, R.F.5    Colman, R.W.6
  • 65
    • 0030600488 scopus 로고    scopus 로고
    • Novel series of plasmid vectors for gene inactivation and expression analysis in group A streptococci (GAS)
    • Podbielski, A., B. Spellerberg, M. Woischnik, B. Pohl, and R. Lutticken. 1996. Novel series of plasmid vectors for gene inactivation and expression analysis in group A streptococci (GAS). Gene 177:137-147.
    • (1996) Gene , vol.177 , pp. 137-147
    • Podbielski, A.1    Spellerberg, B.2    Woischnik, M.3    Pohl, B.4    Lutticken, R.5
  • 66
    • 0033039873 scopus 로고    scopus 로고
    • Characterization of nra, a global negative regulator gene in group A streptococci
    • Podbielski, A., M. Woischnik, B. A. Leonard, and K. H. Schmidt. 1999. Characterization of nra, a global negative regulator gene in group A streptococci. Mol. Microbiol. 31:1051-1064.
    • (1999) Mol. Microbiol. , vol.31 , pp. 1051-1064
    • Podbielski, A.1    Woischnik, M.2    Leonard, B.A.3    Schmidt, K.H.4
  • 67
    • 0031767765 scopus 로고    scopus 로고
    • The gene cluster inlC2DE of Listeria monocytogenes contains additional new internalin genes and is important for virulence in mice
    • Raffelsbauer, D., A. Bubert, F. Engelbrecht, J. Scheinpflug, A. Simm, J. Hess, S. H. Kaufmann, and W. Goebel. 1998. The gene cluster inlC2DE of Listeria monocytogenes contains additional new internalin genes and is important for virulence in mice. Mol. Gen. Genet. 260:144-158.
    • (1998) Mol. Gen. Genet. , vol.260 , pp. 144-158
    • Raffelsbauer, D.1    Bubert, A.2    Engelbrecht, F.3    Scheinpflug, J.4    Simm, A.5    Hess, J.6    Kaufmann, S.H.7    Goebel, W.8
  • 68
    • 0035912797 scopus 로고    scopus 로고
    • Multilocus analysis of extracellular putative virulence proteins made by group A Streptococcus: Population genetics, human serologic response, and gene transcription
    • Reid, S. D., N. M. Green, J. K. Buss, B. Lei, and J. M. Musser. 2001. Multilocus analysis of extracellular putative virulence proteins made by group A Streptococcus: population genetics, human serologic response, and gene transcription. Proc. Natl. Acad. Sci. USA 98:7552-7557.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 7552-7557
    • Reid, S.D.1    Green, N.M.2    Buss, J.K.3    Lei, B.4    Musser, J.M.5
  • 69
    • 0036842087 scopus 로고    scopus 로고
    • Postgenomic analysis of four novel antigens of group A Streptococcus: Growth-phase-dependent gene transcription and human serologic response
    • Reid, S. D., N. M. Green, G. L. Sylva, J. M. Voyich, E. T. Stenseth, F. R. DeLeo, T. M. Palzkill, D. E. Low, H. R. Hill, and J. M. Musser. 2002. Postgenomic analysis of four novel antigens of group A Streptococcus: growth-phase-dependent gene transcription and human serologic response. J. Bacteriol. 184:6316-6324.
    • (2002) J. Bacteriol. , vol.184 , pp. 6316-6324
    • Reid, S.D.1    Green, N.M.2    Sylva, G.L.3    Voyich, J.M.4    Stenseth, E.T.5    DeLeo, F.R.6    Palzkill, T.M.7    Low, D.E.8    Hill, H.R.9    Musser, J.M.10
  • 70
    • 0035114245 scopus 로고    scopus 로고
    • Group A Streptococcus: Allelic variation, population genetics, and host-pathogen interactions
    • Reid, S. D., N. P. Hoe, L. M. Smoot, and J. M. Musser. 2001. Group A Streptococcus: allelic variation, population genetics, and host-pathogen interactions. J. Clin. Investig. 107:393-399.
    • (2001) J. Clin. Investig. , vol.107 , pp. 393-399
    • Reid, S.D.1    Hoe, N.P.2    Smoot, L.M.3    Musser, J.M.4
  • 71
    • 70349192227 scopus 로고    scopus 로고
    • Group A Streptococcus vaccine research: Historical synopsis and new insights
    • R. W. Ellis and B. R. Brodeur (ed.), in press. Landes Bioscience, Georgetown, Tex.
    • Reid, S. D., K. Virtaneva, and J. M. Musser. Group A Streptococcus vaccine research: historical synopsis and new insights. In R. W. Ellis and B. R. Brodeur (ed.), New bacterial vaccines, in press. Landes Bioscience, Georgetown, Tex.
    • New Bacterial Vaccines
    • Reid, S.D.1    Virtaneva, K.2    Musser, J.M.3
  • 73
    • 0037074015 scopus 로고    scopus 로고
    • Structure of internalin, a major invasion protein of Listeria monocytogenes, in complex with its human receptor E-cadherin
    • Schubert, W. D., C. Urbanke, T. Ziehm, V. Beier, M. P. Machner, E. Domann, J. Wehland, T. Chakraborty, and D. W. Heinz. 2002. Structure of internalin, a major invasion protein of Listeria monocytogenes, in complex with its human receptor E-cadherin. Cell 111:825-836.
    • (2002) Cell , vol.111 , pp. 825-836
    • Schubert, W.D.1    Urbanke, C.2    Ziehm, T.3    Beier, V.4    Machner, M.P.5    Domann, E.6    Wehland, J.7    Chakraborty, T.8    Heinz, D.W.9
  • 75
    • 0036066456 scopus 로고    scopus 로고
    • Pattern searches for the identification of putative lipoprotein genes in gram-positive bacterial genomes
    • Sutcliffe, I. C., and D. J. Harrington. 2002. Pattern searches for the identification of putative lipoprotein genes in gram-positive bacterial genomes. Microbiology 148:2065-2077.
    • (2002) Microbiology , vol.148 , pp. 2065-2077
    • Sutcliffe, I.C.1    Harrington, D.J.2
  • 76
    • 0028987131 scopus 로고
    • Lipoproteins of gram-positive bacteria
    • Sutcliffe, I. C., and R. R. Russell. 1995. Lipoproteins of gram-positive bacteria. J. Bacteriol. 177:1123-1128.
    • (1995) J. Bacteriol. , vol.177 , pp. 1123-1128
    • Sutcliffe, I.C.1    Russell, R.R.2
  • 77
    • 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, J. D., D. G. Higgins, and T. J. Gibson. 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
  • 78
    • 0032699917 scopus 로고    scopus 로고
    • Identification of a putative Salmonella enterica serotype Typhimurium host range factor with homology to IpaH and YopM by signature-tagged mutagenesis
    • Tsolis, R. M., S. M. Townsend, E. A. Miao, S. I. Miller, T. A. Ficht, L. G. Adams, and A. J. Baumler. 1999. Identification of a putative Salmonella enterica serotype Typhimurium host range factor with homology to IpaH and YopM by signature-tagged mutagenesis. Infect. Immun. 67:6385-6393.
    • (1999) Infect. Immun. , vol.67 , pp. 6385-6393
    • Tsolis, R.M.1    Townsend, S.M.2    Miao, E.A.3    Miller, S.I.4    Ficht, T.A.5    Adams, L.G.6    Baumler, A.J.7
  • 80
    • 0025303335 scopus 로고
    • Zinc coordination, function, and structure of zinc enzymes and other proteins
    • Vallee, B. L., and D. S. Auld. 1990. Zinc coordination, function, and structure of zinc enzymes and other proteins. Biochemistry 29:5647-5659.
    • (1990) Biochemistry , vol.29 , pp. 5647-5659
    • Vallee, B.L.1    Auld, D.S.2
  • 82
    • 0006665413 scopus 로고    scopus 로고
    • Capsular polysaccharide of group A Streptococcus
    • V. A. Fischetti, R. P. Novick, J. J. Ferretti, D. A. Portnoy, and J. I. Rood (ed.). ASM Press, Washington, D.C.
    • Wessels, M. R. 2000. Capsular polysaccharide of group A Streptococcus, p. 34-42. In V. A. Fischetti, R. P. Novick, J. J. Ferretti, D. A. Portnoy, and J. I. Rood (ed.), Gram-positive pathogens. ASM Press, Washington, D.C.
    • (2000) Gram-Positive Pathogens , pp. 34-42
    • Wessels, M.R.1
  • 83
    • 0035007252 scopus 로고    scopus 로고
    • Recombinant PhpA protein, a unique histidine motif-containing protein from Streptococcus pneumoniae, protects mice against intranasal pneumococcal challenge
    • Zhang, Y., A. W. Masi, V. Barniak, K. Mountzouros, M. K. Hostetter, and B. A. Green. 2001. Recombinant PhpA protein, a unique histidine motif-containing protein from Streptococcus pneumoniae, protects mice against intranasal pneumococcal challenge. Infect. Immun. 69:3827-3836.
    • (2001) Infect. Immun. , vol.69 , pp. 3827-3836
    • Zhang, Y.1    Masi, A.W.2    Barniak, V.3    Mountzouros, K.4    Hostetter, M.K.5    Green, B.A.6


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