메뉴 건너뛰기




Volumn 9, Issue 11, 2014, Pages

Staphylococcus aureus manganese transport protein C (MntC) is an extracellular matrix-and plasminogen-binding protein

Author keywords

[No Author keywords available]

Indexed keywords

AMINOCAPROIC ACID; BINDING PROTEIN; COLLAGEN TYPE 4; FIBRINOGEN; FIBRONECTIN; LAMININ; LYSINE; MANGANESE TRANSPORT PROTEIN C; PLASMIN; PLASMINOGEN; UNCLASSIFIED DRUG; UROKINASE; BACTERIAL PROTEIN; PROTEIN BINDING;

EID: 84914706558     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0112730     Document Type: Article
Times cited : (28)

References (53)
  • 1
    • 84871406895 scopus 로고    scopus 로고
    • Matched-cohort DNA microarray diversity analysis of methicillin sensitive and methicillin resistant Staphylococcus aureus isolates from hospital admission patients
    • Ruffing U, Akulenko R, Bischoff M, Helms V, Herrmann M, et al. (2012) Matched-cohort DNA microarray diversity analysis of methicillin sensitive and methicillin resistant Staphylococcus aureus isolates from hospital admission patients. PLoS ONE 7: e52487.
    • (2012) PLoS ONE , vol.7 , pp. e52487
    • Ruffing, U.1    Akulenko, R.2    Bischoff, M.3    Helms, V.4    Herrmann, M.5
  • 2
    • 84914693816 scopus 로고
    • Preliminary description of the Staphylococcus aureus liquefacians
    • Ernst HC (1896) Preliminary description of the Staphylococcus aureus liquefacians. J Boston Soc Med Sci 1: 3-4.
    • (1896) J Boston Soc Med Sci , vol.1 , pp. 3-4
    • Ernst, H.C.1
  • 3
    • 84914685702 scopus 로고
    • A study of the charges produced in the kidneys by the toxins of the Staphylococcus pyogenes aureus
    • Morse JL (1896) A study of the charges produced in the kidneys by the toxins of the Staphylococcus pyogenes aureus. J Exp Med 1: 613-622.
    • (1896) J Exp Med , vol.1 , pp. 613-622
    • Morse, J.L.1
  • 4
    • 0035925904 scopus 로고    scopus 로고
    • Whole genome sequencing of meticillin-resistant Staphylococcus aureus
    • Kuroda M, Ohta T, Uchiyama I, Baba T, Yuzawa H, et al. (2001) Whole genome sequencing of meticillin-resistant Staphylococcus aureus. Lancet 357: 1225-1240.
    • (2001) Lancet , vol.357 , pp. 1225-1240
    • Kuroda, M.1    Ohta, T.2    Uchiyama, I.3    Baba, T.4    Yuzawa, H.5
  • 6
    • 84890522378 scopus 로고    scopus 로고
    • Adhesion, invasion and evasion: The many functions of the surface proteins of Staphylococcus aureus
    • Foster TJ, Geoghegan JA, Ganesh VK, Höök M (2014) Adhesion, invasion and evasion: the many functions of the surface proteins of Staphylococcus aureus. Nature Reviews Microbiology 12: 49-62.
    • (2014) Nature Reviews Microbiology , vol.12 , pp. 49-62
    • Foster, T.J.1    Geoghegan, J.A.2    Ganesh, V.K.3    Höök, M.4
  • 8
    • 84874258606 scopus 로고    scopus 로고
    • Role of an iron-dependent transcriptional regulator in the pathogenesis and host response to infection with Streptococcus pneumoniae
    • Gupta R, Bhatty M, Swiatlo E, Nanduri B (2013) Role of an iron-dependent transcriptional regulator in the pathogenesis and host response to infection with Streptococcus pneumoniae. PLoS ONE 8: e55157.
    • (2013) PLoS ONE , vol.8 , pp. e55157
    • Gupta, R.1    Bhatty, M.2    Swiatlo, E.3    Nanduri, B.4
  • 9
    • 31844444872 scopus 로고    scopus 로고
    • 2+-dependent regulation of multiple genes in Streptococcus pneumoniae through PsaR and the resultant impact on virulence
    • Johnston JW, Briles DE, Myers LE, Hollingshead SK (2006) Mn2+-dependent regulation of multiple genes in Streptococcus pneumoniae through PsaR and the resultant impact on virulence. Infect Immun 74: 1171-1180.
    • (2006) Infect Immun , vol.74 , pp. 1171-1180
    • Johnston, J.W.1    Briles, D.E.2    Myers, L.E.3    Hollingshead, S.K.4
  • 10
    • 0142074789 scopus 로고    scopus 로고
    • Role and regulation of the superoxide dismutases of Staphylococcus aureus
    • Karavolos MH, Horsburgh MJ, Ingham E, Foster SJ (2003) Role and regulation of the superoxide dismutases of Staphylococcus aureus. Microbiology 149: 2749-2758.
    • (2003) Microbiology , vol.149 , pp. 2749-2758
    • Karavolos, M.H.1    Horsburgh, M.J.2    Ingham, E.3    Foster, S.J.4
  • 11
    • 84886634648 scopus 로고    scopus 로고
    • Regulation of Staphylococcus aureus MntC expression and its role in response to oxidative stress
    • Handke LD, Hawkins JC, Miller AA, Jansen KU, Anderson AS (2013) Regulation of Staphylococcus aureus MntC expression and its role in response to oxidative stress. PLoS ONE 8: e77874.
    • (2013) PLoS ONE , vol.8 , pp. e77874
    • Handke, L.D.1    Hawkins, J.C.2    Miller, A.A.3    Jansen, K.U.4    Anderson, A.S.5
  • 12
    • 84884257375 scopus 로고    scopus 로고
    • MntABC and MntH contribute to systemic Staphylococcus aureus infection by competing with calprotectin for nutrient manganese
    • Kehl-Fie TE, Zhang Y, Moore JL, Farrand AJ, Hood MI, et al. (2013) MntABC and MntH contribute to systemic Staphylococcus aureus infection by competing with calprotectin for nutrient manganese. Infect Immun 81 (9): 3395-3405.
    • (2013) Infect Immun , vol.81 , Issue.9 , pp. 3395-3405
    • Kehl-Fie, T.E.1    Zhang, Y.2    Moore, J.L.3    Farrand, A.J.4    Hood, M.I.5
  • 13
    • 84861073276 scopus 로고    scopus 로고
    • Staphylococcus aureus manganese transport protein C is a highly conserved cell surface protein that elicits protective immunity against S. Aureus and Staphylococcus epidermidis
    • Anderson AS, Scully IL, Timofeyeva Y, Murphy E, McNeil LK, et al. (2012) Staphylococcus aureus manganese transport protein C is a highly conserved cell surface protein that elicits protective immunity against S. aureus and Staphylococcus epidermidis. J Infect Dis 205: 1688-1696.
    • (2012) J Infect Dis , vol.205 , pp. 1688-1696
    • Anderson, A.S.1    Scully, I.L.2    Timofeyeva, Y.3    Murphy, E.4    McNeil, L.K.5
  • 14
    • 84883298486 scopus 로고    scopus 로고
    • Threedimensional structure and biophysical characterization of Staphylococcus aureus cell surface antigen-manganese transporter MntC
    • Gribenko A, Mosyak L, Ghosh S, Parris K, Svenson K, et al. (2013) Threedimensional structure and biophysical characterization of Staphylococcus aureus cell surface antigen-manganese transporter MntC. J Mol Biol 425: 3429-3445.
    • (2013) J Mol Biol , vol.425 , pp. 3429-3445
    • Gribenko, A.1    Mosyak, L.2    Ghosh, S.3    Parris, K.4    Svenson, K.5
  • 15
    • 84891604899 scopus 로고    scopus 로고
    • Emergence of the epidemic methicillin-resistant Staphylococcus aureus strain USA300 coincides with horizontal transfer of the arginine catabolic mobile element and speGmediated adaptations for survival on skin
    • Planet PJ, LaRussa SJ, Dana A, Smith H, Xu A, et al. (2013) Emergence of the epidemic methicillin-resistant Staphylococcus aureus strain USA300 coincides with horizontal transfer of the arginine catabolic mobile element and speGmediated adaptations for survival on skin. MBio 4: e00889-13.
    • (2013) MBio , vol.4 , pp. e00889-e00913
    • Planet, P.J.1    Larussa, S.J.2    Dana, A.3    Smith, H.4    Xu, A.5
  • 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 JP (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. Molecular Microbiology 25: 727-739.
    • (1997) Molecular Microbiology , vol.25 , pp. 727-739
    • Dintilhac, A.1    Alloing, G.2    Granadel, C.3    Claverys, J.P.4
  • 17
    • 34247485877 scopus 로고    scopus 로고
    • E-cadherin is a receptor for the common protein pneumococcal surface adhesin A (PsaA) of Streptococcus pneumoniae
    • Anderton JM, Rajam G, Romero-Steiner S, Summer S, Kowalczyk AP, et al. (2007) E-cadherin is a receptor for the common protein pneumococcal surface adhesin A (PsaA) of Streptococcus pneumoniae. Microb Pathog 42: 225-236.
    • (2007) Microb Pathog , vol.42 , pp. 225-236
    • Anderton, J.M.1    Rajam, G.2    Romero-Steiner, S.3    Summer, S.4    Kowalczyk, A.P.5
  • 18
    • 33746632534 scopus 로고    scopus 로고
    • Intranasal immunization with the cholera toxin B subunit-pneumococcal surface antigen A fusion protein induces protection against colonization with Streptococcus pneumoniae and has negligible impact on the nasopharyngeal and oral microbiota of mice
    • Pimenta FC, Miyaji EN, Arêas AP, Oliveira ML, de Andrade AL, et al. (2006) Intranasal immunization with the cholera toxin B subunit-pneumococcal surface antigen A fusion protein induces protection against colonization with Streptococcus pneumoniae and has negligible impact on the nasopharyngeal and oral microbiota of mice. Infect Immun 74: 4939-4944.
    • (2006) Infect Immun , vol.74 , pp. 4939-4944
    • Pimenta, F.C.1    Miyaji, E.N.2    Arêas, A.P.3    Oliveira, M.L.4    De Andrade, A.L.5
  • 19
    • 3543037586 scopus 로고    scopus 로고
    • Expression and characterization of cholera toxin B-pneumococcal surface adhesin A fusion protein in Escherichia coli: Ability of CTB-PsaA to induce humoral immune response in mice
    • Arêas AP, Oliveira ML, Miyaji EN, Leite LC, Aires KA, et al. (2004) Expression and characterization of cholera toxin B-pneumococcal surface adhesin A fusion protein in Escherichia coli: ability of CTB-PsaA to induce humoral immune response in mice. Biochem Biophys Res Commun 321: 192-196.
    • (2004) Biochem Biophys Res Commun , vol.321 , pp. 192-196
    • Arêas, A.P.1    Oliveira, M.L.2    Miyaji, E.N.3    Leite, L.C.4    Aires, K.A.5
  • 20
    • 84899520606 scopus 로고    scopus 로고
    • Identifying potential therapeutic targets of Methicillin-resistant Staphylococcus aureus through in vivo proteomic analysis
    • Diep BA, Phung Q, Date S, Arnott D, Bakalarski C, et al. (2014) Identifying potential therapeutic targets of Methicillin-resistant Staphylococcus aureus through in vivo proteomic analysis. J Infect Dis.209 (10): 1533-1541.
    • (2014) J Infect Dis , vol.209 , Issue.10 , pp. 1533-1541
    • Diep, B.A.1    Phung, Q.2    Date, S.3    Arnott, D.4    Bakalarski, C.5
  • 21
    • 84894283827 scopus 로고    scopus 로고
    • Interaction of Leptospira Elongation Factor Tu with plasminogen and complement factor H: A metabolic Leptospiral protein with moonlighting activities
    • Wolff DG, Castiblanco-Valencia MM, Abe CM, Monaris D, Morais ZM, et al. (2013) Interaction of Leptospira Elongation Factor Tu with plasminogen and complement factor H: A metabolic Leptospiral protein with moonlighting activities. PLoS ONE 8: e81818.
    • (2013) PLoS ONE , vol.8 , pp. e81818
    • Wolff, D.G.1    Castiblanco-Valencia, M.M.2    Abe, C.M.3    Monaris, D.4    Morais, Z.M.5
  • 22
    • 84872035059 scopus 로고    scopus 로고
    • Nasal colonisation by Staphylococcus aureus depends upon clumping factor B binding to the squamous epithelial cell envelope protein loricrin
    • Mulcahy ME, Geoghegan JA, Monk IR, O'Keeffe KM, Walsh EJ, et al. (2012) Nasal colonisation by Staphylococcus aureus depends upon clumping factor B binding to the squamous epithelial cell envelope protein loricrin. PLoS Pathogens 8 (12): e1003092.
    • (2012) PLoS Pathogens , vol.8 , Issue.12 , pp. e1003092
    • Mulcahy, M.E.1    Geoghegan, J.A.2    Monk, I.R.3    O'keeffe, K.M.4    Walsh, E.J.5
  • 23
    • 84867640103 scopus 로고    scopus 로고
    • Bacterial adhesion to animal tissues: Protein determinants for recognition of extracellular matrix components
    • Chagnot C, Listrat A, Astruc T, Desvaux M (2012) Bacterial adhesion to animal tissues: protein determinants for recognition of extracellular matrix components. Cellular Microbiology 14 (11): 1687-1696.
    • (2012) Cellular Microbiology , vol.14 , Issue.11 , pp. 1687-1696
    • Chagnot, C.1    Listrat, A.2    Astruc, T.3    Desvaux, M.4
  • 24
    • 77949904457 scopus 로고    scopus 로고
    • Molecular characterization of the interaction of staphylococcal microbial surface components recognizing adhesive matrix molecules (mscramm) clfa and fbl with fibrinogen
    • Geoghegan JA, Ganesh VK, Smeds E, Liang X, Höök M, et al. (2010) Molecular characterization of the interaction of Staphylococcal Microbial Surface Components Recognizing Adhesive Matrix Molecules (MSCRAMM) ClfA and Fbl with Fibrinogen. The Journal of Biological Chemistry 285 (9): 6208-6216.
    • (2010) The Journal of Biological Chemistry , vol.285 , Issue.9 , pp. 6208-6216
    • Geoghegan, J.A.1    Ganesh, V.K.2    Smeds, E.3    Liang, X.4    Höök, M.5
  • 25
    • 0037165649 scopus 로고    scopus 로고
    • Enhanced activation of bound plasminogen on Staphylococcus aureus by Staphylokinase
    • Mölkänen T, Tyynelä J, Helin J, Kalkkinen N, Kuusela P (2002) Enhanced activation of bound plasminogen on Staphylococcus aureus by Staphylokinase. FEBS Lett. 517 (1-3): 72-78.
    • (2002) FEBS Lett , vol.517 , Issue.1-3 , pp. 72-78
    • Mölkänen, T.1    Tyynelä, J.2    Helin, J.3    Kalkkinen, N.4    Kuusela, P.5
  • 27
    • 77953940510 scopus 로고    scopus 로고
    • Functional characterization of lcpa, a surface-exposed protein of Leptospira spp. That binds the human complement regulator C4BP
    • Barbosa AS, Monaris D, Silva LB, Morais ZM, Vasconcellos SA, et al. (2010) Functional characterization of LcpA, a surface-exposed protein of Leptospira spp. that binds the human complement regulator C4BP. Infect Immun 78: 3207-3216.
    • (2010) Infect Immun , vol.78 , pp. 3207-3216
    • Barbosa, A.S.1    Monaris, D.2    Silva, L.B.3    Morais, Z.M.4    Vasconcellos, S.A.5
  • 28
    • 84857588385 scopus 로고    scopus 로고
    • Leptospiral immunoglobulin-like proteins interact with human complement regulators factor H, FHL-1, FHR-1, and C4BP
    • Castiblanco-Valencia MM, Fraga TR, Silva LB, Monaris D, Abreu PA, et al. (2012) Leptospiral immunoglobulin-like proteins interact with human complement regulators factor H, FHL-1, FHR-1, and C4BP. J Infect Dis 205: 995-1004.
    • (2012) J Infect Dis , vol.205 , pp. 995-1004
    • Castiblanco-Valencia, M.M.1    Fraga, T.R.2    Silva, L.B.3    Monaris, D.4    Abreu, P.A.5
  • 29
    • 0037408253 scopus 로고    scopus 로고
    • Identification of a Treponema pallidum laminin-binding protein
    • Cameron CE (2003) Identification of a Treponema pallidum laminin-binding protein. Infect Immun 71: 2525-2533.
    • (2003) Infect Immun , vol.71 , pp. 2525-2533
    • Cameron, C.E.1
  • 30
    • 34248368916 scopus 로고    scopus 로고
    • Physiological osmotic induction of Leptospira interrogans adhesion: LigA and LigB bind extracellular matrix proteins and fibrinogen
    • Choy HA, Kelley MM, Chen TL, Møller AK, Matsunaga J, et al. (2007) Physiological osmotic induction of Leptospira interrogans adhesion: LigA and LigB bind extracellular matrix proteins and fibrinogen. Infect Immun 75: 2441-2450.
    • (2007) Infect Immun , vol.75 , pp. 2441-2450
    • Choy, H.A.1    Kelley, M.M.2    Chen, T.L.3    Møller, A.K.4    Matsunaga, J.5
  • 31
    • 34548224154 scopus 로고    scopus 로고
    • A domain of the Leptospira LigB contributes to high affinity binding of fibronectin
    • Lin YP, Chang YF (2007) A domain of the Leptospira LigB contributes to high affinity binding of fibronectin. Biochem Biophys Res Commun 362: 443-448.
    • (2007) Biochem Biophys Res Commun , vol.362 , pp. 443-448
    • Lin, Y.P.1    Chang, Y.F.2
  • 32
    • 45749085306 scopus 로고    scopus 로고
    • The C-terminal variable domain of LigB from Leptospira mediates binding to fibronectin
    • Lin YP, Chang YF (2008) The C-terminal variable domain of LigB from Leptospira mediates binding to fibronectin. J Vet Sci 9: 133-144.
    • (2008) J Vet Sci , vol.9 , pp. 133-144
    • Lin, Y.P.1    Chang, Y.F.2
  • 33
    • 54449094484 scopus 로고    scopus 로고
    • Calcium binds to leptospiral immunoglobulin-like protein, LigB, and modulates fibronectin binding
    • Lin YP, Raman R, Sharma Y, Chang YF (2008) Calcium binds to leptospiral immunoglobulin-like protein, LigB, and modulates fibronectin binding. J Biol Chem 283: 25140-25149.
    • (2008) J Biol Chem , vol.283 , pp. 25140-25149
    • Lin, Y.P.1    Raman, R.2    Sharma, Y.3    Chang, Y.F.4
  • 34
    • 67749102258 scopus 로고    scopus 로고
    • Repeated domains of Leptospira immunoglobulin-like proteins interact with elastin and tropoelastin
    • Lin YP, Lee DW, McDonough SP, Nicholson LK, Sharma Y, et al. (2009) Repeated domains of Leptospira immunoglobulin-like proteins interact with elastin and tropoelastin. J Biol Chem 284: 19380-19391.
    • (2009) J Biol Chem , vol.284 , pp. 19380-19391
    • Lin, Y.P.1    Lee, D.W.2    McDonough, S.P.3    Nicholson, L.K.4    Sharma, Y.5
  • 35
    • 69949134804 scopus 로고    scopus 로고
    • Fibronectin binds to and induces conformational change in a disordered region of leptospiral immunoglobulin-like protein B
    • Lin YP, Greenwood A, Nicholson LK, Sharma Y, McDonough SP, et al. (2009) Fibronectin binds to and induces conformational change in a disordered region of leptospiral immunoglobulin-like protein B. J Biol Chem 284: 23547-23557.
    • (2009) J Biol Chem , vol.284 , pp. 23547-23557
    • Lin, Y.P.1    Greenwood, A.2    Nicholson, L.K.3    Sharma, Y.4    McDonough, S.P.5
  • 36
    • 70349152999 scopus 로고    scopus 로고
    • A novel fibronectin type III module binding motif identified on C-terminus of Leptospira immunoglobulin-like protein, LigB
    • Lin YP, Greenwood A, Yan W, Nicholson LK, Sharma Y, et al. (2009) A novel fibronectin type III module binding motif identified on C-terminus of Leptospira immunoglobulin-like protein, LigB. Biochem Biophys Res Commun 389: 57-62.
    • (2009) Biochem Biophys Res Commun , vol.389 , pp. 57-62
    • Lin, Y.P.1    Greenwood, A.2    Yan, W.3    Nicholson, L.K.4    Sharma, Y.5
  • 37
    • 77955295092 scopus 로고    scopus 로고
    • The terminal immunoglobulin-like repeats of LigA and LigB of Leptospira enhance their binding to gelatin binding domain of fibronectin and host cells
    • Lin YP, McDonough SP, Sharma Y, Chang YF (2010) The terminal immunoglobulin-like repeats of LigA and LigB of Leptospira enhance their binding to gelatin binding domain of fibronectin and host cells. PLoS ONE 5: e11301.
    • (2010) PLoS ONE , vol.5 , pp. e11301
    • Lin, Y.P.1    McDonough, S.P.2    Sharma, Y.3    Chang, Y.F.4
  • 38
    • 77951239052 scopus 로고    scopus 로고
    • Leptospiral endostatin-like protein A is a bacterial cell surface receptor for human plasminogen
    • Verma A, Brissette CA, Bowman AA, Shah ST, Zipfel PF, et al. (2010) Leptospiral endostatin-like protein A is a bacterial cell surface receptor for human plasminogen. Infect Immun 78: 2053-2059.
    • (2010) Infect Immun , vol.78 , pp. 2053-2059
    • Verma, A.1    Brissette, C.A.2    Bowman, A.A.3    Shah, S.T.4    Zipfel, P.F.5
  • 39
    • 84897935824 scopus 로고    scopus 로고
    • Covering all the bases: Preclinical development of an effective Staphylococcus aureus vaccine
    • art 109
    • Scully IL, Liberator PA, Jansen KU, Anderson AS (2014) Covering all the bases: preclinical development of an effective Staphylococcus aureus vaccine. Frontiers in Immunology 5 (art 109): 1-7.
    • (2014) Frontiers in Immunology , vol.5 , pp. 1-7
    • Scully, I.L.1    Liberator, P.A.2    Jansen, K.U.3    Anderson, A.S.4
  • 40
    • 84885491516 scopus 로고    scopus 로고
    • Interrelationship of Streptococcus pneumoniae, Haemophilus influenzae and Staphylococcus aureus colonization within and between pneumococcal-vaccine naïve mother-child dyads
    • Shiri T, Nunes MC, Adrian PV, Van Niekerk N, Klugman KP, et al. (2013) Interrelationship of Streptococcus pneumoniae, Haemophilus influenzae and Staphylococcus aureus colonization within and between pneumococcal-vaccine naïve mother-child dyads. BMC Infectious Diseases 13: 483-492.
    • (2013) BMC Infectious Diseases , vol.13 , pp. 483-492
    • Shiri, T.1    Nunes, M.C.2    Adrian, P.V.3    Van Niekerk, N.4    Klugman, K.P.5
  • 41
    • 84903362395 scopus 로고    scopus 로고
    • Live attenuated influenza vaccine enhances colonization of Streptococcus pneumoniae and Staphylococcus aureus in mice
    • Mina MJ, McCullers JA, Klugman KP (2014) Live attenuated influenza vaccine enhances colonization of Streptococcus pneumoniae and Staphylococcus aureus in mice. mBio, 5(1): e01040-13.
    • (2014) MBio , vol.5 , Issue.1 , pp. e01040-e01113
    • Mina, M.J.1    McCullers, J.A.2    Klugman, K.P.3
  • 42
    • 0025009728 scopus 로고
    • Binding and activation of plasminogen at the surface of Staphylococcus aureus
    • Kuusela P, Saksela O (1990) Binding and activation of plasminogen at the surface of Staphylococcus aureus. European journal of biochemistry 193: 759-765.
    • (1990) European Journal of Biochemistry , vol.193 , pp. 759-765
    • Kuusela, P.1    Saksela, O.2
  • 43
    • 0026501830 scopus 로고
    • Tissue-type plasminogen activator-mediated activation of plasminogen on the surface of group A, C, and G streptococci
    • Kuusela P, Ullberg M, Saksela O, Kronvall G (1992) Tissue-type plasminogen activator-mediated activation of plasminogen on the surface of group A, C, and G streptococci. Infect Immun 60: 196-201.
    • (1992) Infect Immun , vol.60 , pp. 196-201
    • Kuusela, P.1    Ullberg, M.2    Saksela, O.3    Kronvall, G.4
  • 45
    • 58449096795 scopus 로고    scopus 로고
    • Borrelia burgdorferi infection-associated surface proteins ErpP, ErpA, and ErpC bind human plasminogen
    • Brissette CA, Haupt K, Barthel D, Cooley AE, Bowman A, et al. (2009) Borrelia burgdorferi infection-associated surface proteins ErpP, ErpA, and ErpC bind human plasminogen. Infect Immun, 77: 300-306.
    • (2009) Infect Immun , vol.77 , pp. 300-306
    • Brissette, C.A.1    Haupt, K.2    Barthel, D.3    Cooley, A.E.4    Bowman, A.5
  • 46
    • 77949700513 scopus 로고    scopus 로고
    • Intracellular persisting Staphylococcus aureus is the major pathogen in recurrent tonsillitis
    • Zautner AE, Krause M, Stropahl G, Holtfreter S, Frickmann H, et al.(2010) Intracellular persisting Staphylococcus aureus is the major pathogen in recurrent tonsillitis. PLoS ONE, 5(3): e9452.
    • (2010) PLoS ONE , vol.5 , Issue.3 , pp. e9452
    • Zautner, A.E.1    Krause, M.2    Stropahl, G.3    Holtfreter, S.4    Frickmann, H.5
  • 49
    • 63449118440 scopus 로고    scopus 로고
    • Borrelia recurrentis employs a novel multifunctional surface protein with anticomplement, anti-opsonic and invasive potential to escape innate immunity
    • Grosskinsky S, Schott M, Brenner C, Cutler SJ, Kraiczy P, et al. (2009) Borrelia recurrentis employs a novel multifunctional surface protein with anticomplement, anti-opsonic and invasive potential to escape innate immunity. PLoS ONE 4: e4858.
    • (2009) PLoS ONE , vol.4 , pp. e4858
    • Grosskinsky, S.1    Schott, M.2    Brenner, C.3    Cutler, S.J.4    Kraiczy, P.5
  • 51
    • 84867415024 scopus 로고    scopus 로고
    • Staphylococcus aureus proteins Sbi and Efb recruit human plasmin to degrade complement C3 and C3b
    • Koch TK, Reuter M, Barthel D, Böhm S, van den Elsen J, et al. (2012) Staphylococcus aureus proteins Sbi and Efb recruit human plasmin to degrade complement C3 and C3b. PLoS ONE 7 (10): e47638.
    • (2012) PLoS ONE , vol.7 , Issue.10 , pp. e47638
    • Koch, T.K.1    Reuter, M.2    Barthel, D.3    Böhm, S.4    Van Den Elsen, J.5
  • 52
    • 69949148010 scopus 로고    scopus 로고
    • Interaction of triosephosphate isomerase from the cell surface of Staphylococcus aureus and α-(1->3)-mannooligosaccharides derived from glucuronoxylomannan of Cryptococcus neoformans
    • Furuya H, Ikeda R (2009) Interaction of triosephosphate isomerase from the cell surface of Staphylococcus aureus and α-(1->3)-mannooligosaccharides derived from glucuronoxylomannan of Cryptococcus neoformans. Microbiology 155 (Pt 8): 2707-2713.
    • (2009) Microbiology , vol.155 , pp. 2707-2713
    • Furuya, H.1    Ikeda, R.2
  • 53
    • 37349048926 scopus 로고    scopus 로고
    • Evolution and pathogenesis of Staphylococcus aureus: Lessons learned from genotyping and comparative genomics
    • Feng YE, Chen C-J, Su L-H, Hu S, Yu JE, et al. (2008) Evolution and pathogenesis of Staphylococcus aureus: lessons learned from genotyping and comparative genomics. FEMS Microbiology Reviews 32: 23-37.
    • (2008) FEMS Microbiology Reviews , vol.32 , pp. 23-37
    • Feng, Y.E.1    Chen, C.-J.2    Su, L.-H.3    Hu, S.4    Yu, J.E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.