메뉴 건너뛰기




Volumn 20, Issue 10, 2014, Pages 571-578

Invasive meningococcal disease: A disease of the endothelial cells

Author keywords

CD147; Endothelium; Meningitis; Neisseria meningitidis; Purpura fulminans; 2 adrenoceptor

Indexed keywords

BETA 2 ADRENERGIC RECEPTOR; CD147 ANTIGEN; BSG PROTEIN, HUMAN;

EID: 84908149558     PISSN: 14714914     EISSN: 1471499X     Source Type: Journal    
DOI: 10.1016/j.molmed.2014.08.002     Document Type: Review
Times cited : (40)

References (71)
  • 1
    • 84901505870 scopus 로고    scopus 로고
    • Neisseria meningitidis; clones, carriage, and disease
    • Read R.C. Neisseria meningitidis; clones, carriage, and disease. Clin. Microbiol. Infect. 2014, 20:391-395.
    • (2014) Clin. Microbiol. Infect. , vol.20 , pp. 391-395
    • Read, R.C.1
  • 2
    • 57549114614 scopus 로고    scopus 로고
    • Association of a bacteriophage with meningococcal disease in young adults
    • Bille E., et al. Association of a bacteriophage with meningococcal disease in young adults. PLoS ONE 2008, 3:e3885.
    • (2008) PLoS ONE , vol.3 , pp. e3885
    • Bille, E.1
  • 3
    • 67650659120 scopus 로고    scopus 로고
    • Epidemiological evidence for the role of the hemoglobin receptor, hmbR, in meningococcal virulence
    • Harrison O.B., et al. Epidemiological evidence for the role of the hemoglobin receptor, hmbR, in meningococcal virulence. J. Infect. Dis. 2009, 200:94-98.
    • (2009) J. Infect. Dis. , vol.200 , pp. 94-98
    • Harrison, O.B.1
  • 4
    • 0037987829 scopus 로고    scopus 로고
    • A model of meningococcal bacteremia after respiratory superinfection in influenza A virus-infected mice
    • Alonso J.M., et al. A model of meningococcal bacteremia after respiratory superinfection in influenza A virus-infected mice. FEMS Microbiol. Lett. 2003, 222:99-106.
    • (2003) FEMS Microbiol. Lett. , vol.222 , pp. 99-106
    • Alonso, J.M.1
  • 5
    • 84860234453 scopus 로고    scopus 로고
    • Genetics and genomics in pediatric septic shock
    • Wong H.R. Genetics and genomics in pediatric septic shock. Crit. Care Med. 2012, 40:1618-1626.
    • (2012) Crit. Care Med. , vol.40 , pp. 1618-1626
    • Wong, H.R.1
  • 6
    • 0017712048 scopus 로고
    • The infant rat as a model of bacterial meningitis
    • Moxon E.R., et al. The infant rat as a model of bacterial meningitis. J. Infect. Dis. 1977, 136(Suppl):S186-S190.
    • (1977) J. Infect. Dis. , vol.136 , pp. S186-S190
    • Moxon, E.R.1
  • 7
    • 35148828105 scopus 로고    scopus 로고
    • Meningococcal A, C, Y and W-135 polysaccharide-protein conjugate vaccines
    • Pace D., Pollard A.J. Meningococcal A, C, Y and W-135 polysaccharide-protein conjugate vaccines. Arch. Dis. Child. 2007, 92:909-915.
    • (2007) Arch. Dis. Child. , vol.92 , pp. 909-915
    • Pace, D.1    Pollard, A.J.2
  • 8
    • 0023272273 scopus 로고
    • An IgG monoclonal antibody to group B meningococci cross-reacts with developmentally regulated polysialic acid units of glycoproteins in neural and extraneural tissues
    • Finne J., et al. An IgG monoclonal antibody to group B meningococci cross-reacts with developmentally regulated polysialic acid units of glycoproteins in neural and extraneural tissues. J. Immunol. 1987, 138:4402-4407.
    • (1987) J. Immunol. , vol.138 , pp. 4402-4407
    • Finne, J.1
  • 9
    • 0033064808 scopus 로고    scopus 로고
    • Iron acquisition systems in the pathogenic Neisseria
    • Schryvers A.B., Stojiljkovic I. Iron acquisition systems in the pathogenic Neisseria. Mol. Microbiol. 1999, 32:1117-1123.
    • (1999) Mol. Microbiol. , vol.32 , pp. 1117-1123
    • Schryvers, A.B.1    Stojiljkovic, I.2
  • 10
    • 58449121716 scopus 로고    scopus 로고
    • Factor H-binding protein is important for meningococcal survival in human whole blood and serum and in the presence of the antimicrobial peptide LL-37
    • Seib K.L., et al. Factor H-binding protein is important for meningococcal survival in human whole blood and serum and in the presence of the antimicrobial peptide LL-37. Infect. Immun. 2009, 77:292-299.
    • (2009) Infect. Immun. , vol.77 , pp. 292-299
    • Seib, K.L.1
  • 11
    • 57649220619 scopus 로고    scopus 로고
    • Factor H and Neisserial pathogenesis
    • Welsch J.A., Ram S. Factor H and Neisserial pathogenesis. Vaccine 2008, 26(Suppl. 8):I40-I45.
    • (2008) Vaccine , vol.26 , pp. I40-I45
    • Welsch, J.A.1    Ram, S.2
  • 12
    • 84861133426 scopus 로고    scopus 로고
    • The new multicomponent vaccine against meningococcal serogroup B, 4CMenB: immunological, functional and structural characterization of the antigens
    • Serruto D., et al. The new multicomponent vaccine against meningococcal serogroup B, 4CMenB: immunological, functional and structural characterization of the antigens. Vaccine 2012, 30(Suppl. 2):B87-B97.
    • (2012) Vaccine , vol.30 , pp. B87-B97
    • Serruto, D.1
  • 13
    • 84900385250 scopus 로고    scopus 로고
    • Use of a multicomponent, recombinant, meningococcal serogroup B vaccine (4CMenB) for bacterial meningitis prevention
    • Esposito S., et al. Use of a multicomponent, recombinant, meningococcal serogroup B vaccine (4CMenB) for bacterial meningitis prevention. Immunotherapy 2014, 6:395-408.
    • (2014) Immunotherapy , vol.6 , pp. 395-408
    • Esposito, S.1
  • 14
    • 0036716480 scopus 로고    scopus 로고
    • Analysis of pathogen-host cell interactions in purpura fulminans: expression of capsule, type IV pili, and PorA by Neisseria meningitidis in vivo
    • Harrison O.B., et al. Analysis of pathogen-host cell interactions in purpura fulminans: expression of capsule, type IV pili, and PorA by Neisseria meningitidis in vivo. Infect. Immun. 2002, 70:5193-5201.
    • (2002) Infect. Immun. , vol.70 , pp. 5193-5201
    • Harrison, O.B.1
  • 15
    • 0030612732 scopus 로고    scopus 로고
    • Interaction of Neisseria maningitidis with the components of the blood-brain barrier correlates with an increased expression of PilC
    • Pron B., et al. Interaction of Neisseria maningitidis with the components of the blood-brain barrier correlates with an increased expression of PilC. J. Infect. Dis. 1997, 176:1285-1292.
    • (1997) J. Infect. Dis. , vol.176 , pp. 1285-1292
    • Pron, B.1
  • 16
    • 84859055553 scopus 로고    scopus 로고
    • Chronic meningococcemia cutaneous lesions involve meningococcal perivascular invasion through the remodeling of endothelial barriers
    • Dupin N., et al. Chronic meningococcemia cutaneous lesions involve meningococcal perivascular invasion through the remodeling of endothelial barriers. Clin. Infect. Dis. 2012, 54:1162-1165.
    • (2012) Clin. Infect. Dis. , vol.54 , pp. 1162-1165
    • Dupin, N.1
  • 17
    • 41949117894 scopus 로고    scopus 로고
    • Type IV pili: paradoxes in form and function
    • Craig L., Li J. Type IV pili: paradoxes in form and function. Curr. Opin. Struct. Biol. 2008, 18:267-277.
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 267-277
    • Craig, L.1    Li, J.2
  • 18
    • 0034406525 scopus 로고    scopus 로고
    • Components and dynamics of fiber formation define a ubiquitous biogenesis pathway for bacterial pili
    • Wolfgang M., et al. Components and dynamics of fiber formation define a ubiquitous biogenesis pathway for bacterial pili. EMBO J. 2000, 19:6408-6418.
    • (2000) EMBO J. , vol.19 , pp. 6408-6418
    • Wolfgang, M.1
  • 19
    • 0023780725 scopus 로고
    • DNA transformation leads to pilin antigenic variation in Neisseria gonorrhoeae
    • Seifert H.S., et al. DNA transformation leads to pilin antigenic variation in Neisseria gonorrhoeae. Nature 1988, 336:392-395.
    • (1988) Nature , vol.336 , pp. 392-395
    • Seifert, H.S.1
  • 20
    • 0032982528 scopus 로고    scopus 로고
    • The comP locus of Neisseria gonorrhoeae encodes a type IV prepilin that is dispensable for pilus biogenesis but essential for natural transformation
    • Wolfgang M., et al. The comP locus of Neisseria gonorrhoeae encodes a type IV prepilin that is dispensable for pilus biogenesis but essential for natural transformation. Mol. Microbiol. 1999, 31:1345-1357.
    • (1999) Mol. Microbiol. , vol.31 , pp. 1345-1357
    • Wolfgang, M.1
  • 21
    • 12344257661 scopus 로고    scopus 로고
    • PilX, a pilus-associated protein essential for bacterial aggregation, is a key to pilus-facilitated attachment of Neisseria meningitidis to human cells
    • Helaine S., et al. PilX, a pilus-associated protein essential for bacterial aggregation, is a key to pilus-facilitated attachment of Neisseria meningitidis to human cells. Mol. Microbiol. 2005, 55:65-77.
    • (2005) Mol. Microbiol. , vol.55 , pp. 65-77
    • Helaine, S.1
  • 22
    • 61449161195 scopus 로고    scopus 로고
    • Extracellular bacterial pathogen induces host cell surface reorganization to resist shear stress
    • Mikaty G., et al. Extracellular bacterial pathogen induces host cell surface reorganization to resist shear stress. PLoS Pathog. 2009, 5:e1000314.
    • (2009) PLoS Pathog. , vol.5 , pp. e1000314
    • Mikaty, G.1
  • 23
    • 3142631733 scopus 로고    scopus 로고
    • Type IV pilus retraction in pathogenic Neisseria is regulated by the PilC proteins
    • Morand P.C., et al. Type IV pilus retraction in pathogenic Neisseria is regulated by the PilC proteins. EMBO J. 2004, 23:2009-2017.
    • (2004) EMBO J. , vol.23 , pp. 2009-2017
    • Morand, P.C.1
  • 24
    • 0027255820 scopus 로고
    • Antigenic variation of pilin regulates adhesion of Neisseria meningitidis to human epithelial cells
    • Nassif X., et al. Antigenic variation of pilin regulates adhesion of Neisseria meningitidis to human epithelial cells. Mol. Microbiol. 1993, 8:719-725.
    • (1993) Mol. Microbiol. , vol.8 , pp. 719-725
    • Nassif, X.1
  • 25
    • 0025766876 scopus 로고
    • The role of pili in the interactions of pathogenic Neisseria with cultured human endothelial cells
    • Virji M., et al. The role of pili in the interactions of pathogenic Neisseria with cultured human endothelial cells. Mol. Microbiol. 1991, 5:1831-1841.
    • (1991) Mol. Microbiol. , vol.5 , pp. 1831-1841
    • Virji, M.1
  • 26
    • 0028979820 scopus 로고
    • Role of pili and the phase-variable PilC protein in natural competence for transformation of Neisseria gonorrhoeae
    • Rudel T., et al. Role of pili and the phase-variable PilC protein in natural competence for transformation of Neisseria gonorrhoeae. Proc. Natl. Acad. Sci. U.S.A. 1995, 92:7986-7990.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 7986-7990
    • Rudel, T.1
  • 27
    • 0030779080 scopus 로고    scopus 로고
    • Membrane cofactor protein (MCP or CD46) is a cellular pilus receptor for pathogenic Neisseria
    • Kallstrom H., et al. Membrane cofactor protein (MCP or CD46) is a cellular pilus receptor for pathogenic Neisseria. Mol. Microbiol. 1997, 25:639-647.
    • (1997) Mol. Microbiol. , vol.25 , pp. 639-647
    • Kallstrom, H.1
  • 28
    • 17644417153 scopus 로고    scopus 로고
    • CD46-independent binding of neisserial type IV pili and the major pilus adhesin, PilC, to human epithelial cells
    • Kirchner M., et al. CD46-independent binding of neisserial type IV pili and the major pilus adhesin, PilC, to human epithelial cells. Infect. Immun. 2005, 73:3072-3082.
    • (2005) Infect. Immun. , vol.73 , pp. 3072-3082
    • Kirchner, M.1
  • 29
    • 0034518454 scopus 로고    scopus 로고
    • Interactions of pathogenic Neisseriae with epithelial cell membranes
    • Merz A.J., So M. Interactions of pathogenic Neisseriae with epithelial cell membranes. Annu. Rev. Cell Dev. Biol. 2000, 16:423-457.
    • (2000) Annu. Rev. Cell Dev. Biol. , vol.16 , pp. 423-457
    • Merz, A.J.1    So, M.2
  • 30
    • 35649008942 scopus 로고    scopus 로고
    • 3D structure/function analysis of PilX reveals how minor pilins can modulate the virulence properties of type IV pili
    • Helaine S., et al. 3D structure/function analysis of PilX reveals how minor pilins can modulate the virulence properties of type IV pili. Proc. Natl. Acad. Sci. U.S.A. 2007, 104:15888-15893.
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 15888-15893
    • Helaine, S.1
  • 31
    • 0036405357 scopus 로고    scopus 로고
    • Type IV pili and twitching motility
    • Mattick J.S. Type IV pili and twitching motility. Annu. Rev. Microbiol. 2002, 56:289-314.
    • (2002) Annu. Rev. Microbiol. , vol.56 , pp. 289-314
    • Mattick, J.S.1
  • 32
    • 79951506883 scopus 로고    scopus 로고
    • Posttranslational modification of pili upon cell contact triggers N. meningitidis dissemination
    • Chamot-Rooke J., et al. Posttranslational modification of pili upon cell contact triggers N. meningitidis dissemination. Science 2011, 331:778-782.
    • (2011) Science , vol.331 , pp. 778-782
    • Chamot-Rooke, J.1
  • 33
    • 33746894115 scopus 로고    scopus 로고
    • Cerebral microcirculation shear stress levels determine Neisseria meningitidis attachment sites along the blood-brain barrier
    • Mairey E., et al. Cerebral microcirculation shear stress levels determine Neisseria meningitidis attachment sites along the blood-brain barrier. J. Exp. Med. 2006, 203:1939-1950.
    • (2006) J. Exp. Med. , vol.203 , pp. 1939-1950
    • Mairey, E.1
  • 34
    • 0033059203 scopus 로고    scopus 로고
    • Type IV pili of pathogenic Neisseria elicit cortical plaque formation in epithelial cells
    • Merz A.J., et al. Type IV pili of pathogenic Neisseria elicit cortical plaque formation in epithelial cells. Mol. Microbiol. 1999, 32:1316-1332.
    • (1999) Mol. Microbiol. , vol.32 , pp. 1316-1332
    • Merz, A.J.1
  • 35
    • 0027400824 scopus 로고
    • Human/severe combined immunodeficient mouse chimeras. An experimental in vivo model system to study the regulation of human endothelial cell-leukocyte adhesion molecules
    • Yan H.C., et al. Human/severe combined immunodeficient mouse chimeras. An experimental in vivo model system to study the regulation of human endothelial cell-leukocyte adhesion molecules. J. Clin. Invest. 1993, 91:986-996.
    • (1993) J. Clin. Invest. , vol.91 , pp. 986-996
    • Yan, H.C.1
  • 36
    • 63149103168 scopus 로고    scopus 로고
    • Role of CCL17 in the generation of cutaneous inflammatory reactions in Hu-PBMC-SCID mice grafted with human skin
    • Gilet J., et al. Role of CCL17 in the generation of cutaneous inflammatory reactions in Hu-PBMC-SCID mice grafted with human skin. J. Invest. Dermatol. 2009, 129:879-890.
    • (2009) J. Invest. Dermatol. , vol.129 , pp. 879-890
    • Gilet, J.1
  • 37
    • 84888630325 scopus 로고    scopus 로고
    • Meningococcal interaction to microvasculature triggers the tissular lesions of purpura fulminans
    • Join-Lambert O., et al. Meningococcal interaction to microvasculature triggers the tissular lesions of purpura fulminans. J. Infect. Dis. 2013, 208:1590-1597.
    • (2013) J. Infect. Dis. , vol.208 , pp. 1590-1597
    • Join-Lambert, O.1
  • 38
    • 84875072891 scopus 로고    scopus 로고
    • Adhesion of Neisseria meningitidis to dermal vessels leads to local vascular damage and purpura in a humanized mouse model
    • Melican K., et al. Adhesion of Neisseria meningitidis to dermal vessels leads to local vascular damage and purpura in a humanized mouse model. PLoS Pathog. 2013, 9:e1003139.
    • (2013) PLoS Pathog. , vol.9 , pp. e1003139
    • Melican, K.1
  • 39
    • 0029844602 scopus 로고    scopus 로고
    • The N-domain of the human CD66a adhesion molecule is a target for Opa proteins of Neisseria meningitidis and Neisseria gonorrhoeae
    • Virji M., et al. The N-domain of the human CD66a adhesion molecule is a target for Opa proteins of Neisseria meningitidis and Neisseria gonorrhoeae. Mol. Microbiol. 1996, 22:929-939.
    • (1996) Mol. Microbiol. , vol.22 , pp. 929-939
    • Virji, M.1
  • 40
    • 0032489349 scopus 로고    scopus 로고
    • Vitronectin-dependent invasion of epithelial cells by Neisseria gonorrhoeae involves alpha(v) integrin receptors
    • Dehio M., et al. Vitronectin-dependent invasion of epithelial cells by Neisseria gonorrhoeae involves alpha(v) integrin receptors. FEBS Lett. 1998, 424:84-88.
    • (1998) FEBS Lett. , vol.424 , pp. 84-88
    • Dehio, M.1
  • 41
    • 0027524614 scopus 로고
    • Meningococcal Opa and Opc proteins: their role in colonization and invasion of human epithelial and endothelial cells
    • Virji M., et al. Meningococcal Opa and Opc proteins: their role in colonization and invasion of human epithelial and endothelial cells. Mol. Microbiol. 1993, 10:499-510.
    • (1993) Mol. Microbiol. , vol.10 , pp. 499-510
    • Virji, M.1
  • 42
    • 0034106438 scopus 로고    scopus 로고
    • Interactions of Neisseria meningitidis with cells of the human meninges
    • Hardy S.J., et al. Interactions of Neisseria meningitidis with cells of the human meninges. Mol. Microbiol. 2000, 36:817-829.
    • (2000) Mol. Microbiol. , vol.36 , pp. 817-829
    • Hardy, S.J.1
  • 43
    • 0034872590 scopus 로고    scopus 로고
    • Inverse relationship between pilus-mediated gonococcal adherence and surface expression of the pilus receptor, CD46
    • Tobiason D.M., Seifert H.S. Inverse relationship between pilus-mediated gonococcal adherence and surface expression of the pilus receptor, CD46. Microbiology 2001, 147:2333-2340.
    • (2001) Microbiology , vol.147 , pp. 2333-2340
    • Tobiason, D.M.1    Seifert, H.S.2
  • 44
    • 84878514516 scopus 로고    scopus 로고
    • Dual pili post-translational modifications synergize to mediate meningococcal adherence to platelet activating factor receptor on human airway cells
    • Jen F.E., et al. Dual pili post-translational modifications synergize to mediate meningococcal adherence to platelet activating factor receptor on human airway cells. PLoS Pathog. 2013, 9:e1003377.
    • (2013) PLoS Pathog. , vol.9 , pp. e1003377
    • Jen, F.E.1
  • 45
    • 84904049840 scopus 로고    scopus 로고
    • Pathogenic Neisseria meningitidis utilizes CD147 for vascular colonization
    • Bernard S.C., et al. Pathogenic Neisseria meningitidis utilizes CD147 for vascular colonization. Nat. Med. 2014, 20:725-731.
    • (2014) Nat. Med. , vol.20 , pp. 725-731
    • Bernard, S.C.1
  • 46
    • 36048958229 scopus 로고    scopus 로고
    • CD147 immunoglobulin superfamily receptor function and role in pathology
    • Iacono K.T., et al. CD147 immunoglobulin superfamily receptor function and role in pathology. Exp. Mol. Pathol. 2007, 83:283-295.
    • (2007) Exp. Mol. Pathol. , vol.83 , pp. 283-295
    • Iacono, K.T.1
  • 47
    • 0033851302 scopus 로고    scopus 로고
    • Expression of emmprin (CD147), a cell surface inducer of matrix metalloproteinases, in normal human brain and gliomas
    • Sameshima T., et al. Expression of emmprin (CD147), a cell surface inducer of matrix metalloproteinases, in normal human brain and gliomas. Int. J. Cancer 2000, 88:21-27.
    • (2000) Int. J. Cancer , vol.88 , pp. 21-27
    • Sameshima, T.1
  • 48
    • 0036594027 scopus 로고    scopus 로고
    • Developmental changes of HT7 expression in the microvessels of the chick embryo brain
    • Bertossi M., et al. Developmental changes of HT7 expression in the microvessels of the chick embryo brain. Anat. Embryol. (Berl.) 2002, 205:229-233.
    • (2002) Anat. Embryol. (Berl.) , vol.205 , pp. 229-233
    • Bertossi, M.1
  • 49
    • 84903370958 scopus 로고    scopus 로고
    • The hypervariable region of meningococcal major pilin PilE controls the host cell response via antigenic variation
    • e01024-13
    • Miller F., et al. The hypervariable region of meningococcal major pilin PilE controls the host cell response via antigenic variation. mBio 2014, 5. e01024-13.
    • (2014) mBio , vol.5
    • Miller, F.1
  • 50
    • 78650476918 scopus 로고    scopus 로고
    • Meningococcus hijacks a beta2-adrenoceptor/beta-arrestin pathway to cross brain microvasculature endothelium
    • Coureuil M., et al. Meningococcus hijacks a beta2-adrenoceptor/beta-arrestin pathway to cross brain microvasculature endothelium. Cell 2010, 143:1149-1160.
    • (2010) Cell , vol.143 , pp. 1149-1160
    • Coureuil, M.1
  • 51
    • 33947401068 scopus 로고    scopus 로고
    • Beta-arrestins and cell signaling
    • DeWire S.M., et al. Beta-arrestins and cell signaling. Annu. Rev. Physiol. 2007, 69:483-510.
    • (2007) Annu. Rev. Physiol. , vol.69 , pp. 483-510
    • DeWire, S.M.1
  • 52
    • 41949089470 scopus 로고    scopus 로고
    • Beta-arrestin-biased agonism at the beta2-adrenergic receptor
    • Drake M.T., et al. beta-arrestin-biased agonism at the beta2-adrenergic receptor. J. Biol. Chem. 2008, 283:5669-5676.
    • (2008) J. Biol. Chem. , vol.283 , pp. 5669-5676
    • Drake, M.T.1
  • 53
    • 33646806054 scopus 로고    scopus 로고
    • Neisseria meningitidis infection of human endothelial cells interferes with leukocyte transmigration by preventing the formation of endothelial docking structures
    • Doulet N., et al. Neisseria meningitidis infection of human endothelial cells interferes with leukocyte transmigration by preventing the formation of endothelial docking structures. J. Cell Biol. 2006, 173:627-637.
    • (2006) J. Cell Biol. , vol.173 , pp. 627-637
    • Doulet, N.1
  • 54
    • 0035494437 scopus 로고    scopus 로고
    • Activation of ErbB2 receptor tyrosine kinase supports invasion of endothelial cells by Neisseria meningitidis
    • Hoffmann I., et al. Activation of ErbB2 receptor tyrosine kinase supports invasion of endothelial cells by Neisseria meningitidis. J. Cell Biol. 2001, 155:133-143.
    • (2001) J. Cell Biol. , vol.155 , pp. 133-143
    • Hoffmann, I.1
  • 55
    • 67650079165 scopus 로고    scopus 로고
    • Meningococcal type IV pili recruit the polarity complex to cross the brain endothelium
    • Coureuil M., et al. Meningococcal type IV pili recruit the polarity complex to cross the brain endothelium. Science 2009, 325:83-87.
    • (2009) Science , vol.325 , pp. 83-87
    • Coureuil, M.1
  • 56
    • 0141654989 scopus 로고    scopus 로고
    • Erythrocyte G protein-coupled receptor signaling in malarial infection
    • Harrison T., et al. Erythrocyte G protein-coupled receptor signaling in malarial infection. Science 2003, 301:1734-1736.
    • (2003) Science , vol.301 , pp. 1734-1736
    • Harrison, T.1
  • 57
    • 84355161568 scopus 로고    scopus 로고
    • Basigin is a receptor essential for erythrocyte invasion by Plasmodium falciparum
    • Crosnier C., et al. Basigin is a receptor essential for erythrocyte invasion by Plasmodium falciparum. Nature 2011, 480:534-537.
    • (2011) Nature , vol.480 , pp. 534-537
    • Crosnier, C.1
  • 58
    • 0035932951 scopus 로고    scopus 로고
    • CD147 facilitates HIV-1 infection by interacting with virus-associated cyclophilin A
    • Pushkarsky T., et al. CD147 facilitates HIV-1 infection by interacting with virus-associated cyclophilin A. Proc. Natl. Acad. Sci. U.S.A. 2001, 98:6360-6365.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 6360-6365
    • Pushkarsky, T.1
  • 59
    • 14744289370 scopus 로고    scopus 로고
    • Par-3 controls tight junction assembly through the Rac exchange factor Tiam1
    • Chen X., Macara I.G. Par-3 controls tight junction assembly through the Rac exchange factor Tiam1. Nat. Cell Biol. 2005, 7:262-269.
    • (2005) Nat. Cell Biol. , vol.7 , pp. 262-269
    • Chen, X.1    Macara, I.G.2
  • 60
    • 77950803559 scopus 로고    scopus 로고
    • CD147/EMMPRIN acts as a functional entry receptor for measles virus on epithelial cells
    • Watanabe A., et al. CD147/EMMPRIN acts as a functional entry receptor for measles virus on epithelial cells. J. Virol. 2010, 84:4183-4193.
    • (2010) J. Virol. , vol.84 , pp. 4183-4193
    • Watanabe, A.1
  • 61
    • 40949130849 scopus 로고    scopus 로고
    • A role for membrane-bound CD147 in NOD2-mediated recognition of bacterial cytoinvasion
    • Till A., et al. A role for membrane-bound CD147 in NOD2-mediated recognition of bacterial cytoinvasion. J. Cell Sci. 2008, 121:487-495.
    • (2008) J. Cell Sci. , vol.121 , pp. 487-495
    • Till, A.1
  • 62
    • 0037087613 scopus 로고    scopus 로고
    • Microvilli-like structures are associated with the internalization of virulent capsulated Neisseria meningitidis into vascular endothelial cells
    • Eugene E., et al. Microvilli-like structures are associated with the internalization of virulent capsulated Neisseria meningitidis into vascular endothelial cells. J. Cell Sci. 2002, 115:1231-1241.
    • (2002) J. Cell Sci. , vol.115 , pp. 1231-1241
    • Eugene, E.1
  • 63
    • 24944587299 scopus 로고    scopus 로고
    • Invasion of endothelial cells by Neisseria meningitidis requires cortactin recruitment by a phosphoinositide-3-kinase/Rac1 signalling pathway triggered by the lipo-oligosaccharide
    • Lambotin M., et al. Invasion of endothelial cells by Neisseria meningitidis requires cortactin recruitment by a phosphoinositide-3-kinase/Rac1 signalling pathway triggered by the lipo-oligosaccharide. J. Cell Sci. 2005, 118:3805-3816.
    • (2005) J. Cell Sci. , vol.118 , pp. 3805-3816
    • Lambotin, M.1
  • 64
    • 0035090317 scopus 로고    scopus 로고
    • Activation of Arp2/3 complex-mediated actin polymerization by cortactin
    • Uruno T., et al. Activation of Arp2/3 complex-mediated actin polymerization by cortactin. Nat. Cell Biol. 2001, 3:259-266.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 259-266
    • Uruno, T.1
  • 65
    • 84894261244 scopus 로고    scopus 로고
    • Role of epidermal growth factor receptor signaling in the interaction of Neisseria meningitidis with endothelial cells
    • Slanina H., et al. Role of epidermal growth factor receptor signaling in the interaction of Neisseria meningitidis with endothelial cells. Infect. Immun. 2014, 82:1243-1255.
    • (2014) Infect. Immun. , vol.82 , pp. 1243-1255
    • Slanina, H.1
  • 66
    • 84903473067 scopus 로고    scopus 로고
    • Differential activation of acid sphingomyelinase and ceramide release determines invasiveness of Neisseria meningitidis into brain endothelial cells
    • Simonis A., et al. Differential activation of acid sphingomyelinase and ceramide release determines invasiveness of Neisseria meningitidis into brain endothelial cells. PLoS Pathog. 2014, 10:e1004160.
    • (2014) PLoS Pathog. , vol.10 , pp. e1004160
    • Simonis, A.1
  • 67
    • 84865625411 scopus 로고    scopus 로고
    • Endothelial membrane reorganization during leukocyte extravasation
    • Reglero-Real N., et al. Endothelial membrane reorganization during leukocyte extravasation. Cell. Mol. Life Sci. 2012, 69:3079-3099.
    • (2012) Cell. Mol. Life Sci. , vol.69 , pp. 3079-3099
    • Reglero-Real, N.1
  • 68
    • 84900542541 scopus 로고    scopus 로고
    • The C2 fragment from Neisseria meningitidis antigen NHBA increases endothelial permeability by destabilizing adherens junctions
    • Casellato A., et al. The C2 fragment from Neisseria meningitidis antigen NHBA increases endothelial permeability by destabilizing adherens junctions. Cell. Microbiol. 2014, 16:925-937.
    • (2014) Cell. Microbiol. , vol.16 , pp. 925-937
    • Casellato, A.1
  • 69
    • 77954054834 scopus 로고    scopus 로고
    • Neisseria meningitidis induces brain microvascular endothelial cell detachment from the matrix and cleavage of occludin: a role for MMP-8
    • Schubert-Unkmeir A., et al. Neisseria meningitidis induces brain microvascular endothelial cell detachment from the matrix and cleavage of occludin: a role for MMP-8. PLoS Pathog. 2010, 6:e1000874.
    • (2010) PLoS Pathog. , vol.6 , pp. e1000874
    • Schubert-Unkmeir, A.1
  • 70
    • 2342471420 scopus 로고    scopus 로고
    • The blood-brain barrier: an overview: structure, regulation, and clinical implications
    • Ballabh P., et al. The blood-brain barrier: an overview: structure, regulation, and clinical implications. Neurobiol. Dis. 2004, 16:1-13.
    • (2004) Neurobiol. Dis. , vol.16 , pp. 1-13
    • Ballabh, P.1
  • 71
    • 84866364390 scopus 로고    scopus 로고
    • The anatomical and cellular basis of immune surveillance in the central nervous system
    • Ransohoff R.M., Engelhardt B. The anatomical and cellular basis of immune surveillance in the central nervous system. Nat. Rev. Immunol. 2012, 12:623-635.
    • (2012) Nat. Rev. Immunol. , vol.12 , pp. 623-635
    • Ransohoff, R.M.1    Engelhardt, B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.