메뉴 건너뛰기




Volumn 112, Issue 22, 2015, Pages 7073-7078

Identification of an epithelial cell receptor responsible for Clostridium difficile TcdB-induced cytotoxicity

Author keywords

Nectin 3; PVRL3; Toxin

Indexed keywords

CELL RECEPTOR; CLOSTRIDIUM DIFFICILE TOXIN A; CLOSTRIDIUM DIFFICILE TOXIN B; MONOCLONAL ANTIBODY; MUTANT PROTEIN; POLIOVIRUS RECEPTOR LIKE 3; SHORT HAIRPIN RNA; UNCLASSIFIED DRUG; VIRULENCE FACTOR; VIRUS RECEPTOR; BACTERIAL PROTEIN; BACTERIAL TOXIN; CELL ADHESION MOLECULE; ENTEROTOXIN; NECTINS; TOXB PROTEIN, CLOSTRIDIUM DIFFICILE;

EID: 84930965989     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1500791112     Document Type: Article
Times cited : (127)

References (58)
  • 1
    • 55249105923 scopus 로고    scopus 로고
    • Clostridium difficile - More difficult than ever
    • Kelly CP, LaMont JT (2008) Clostridium difficile - more difficult than ever. N Engl J Med 359(18):1932-1940.
    • (2008) N Engl J Med , vol.359 , Issue.18 , pp. 1932-1940
    • Kelly, C.P.1    LaMont, J.T.2
  • 2
    • 77952764840 scopus 로고    scopus 로고
    • Increased Clostridium difficile virulence demands new treatment approach
    • Voelker R (2010) Increased Clostridium difficile virulence demands new treatment approach. JAMA 303(20):2017-2019.
    • (2010) JAMA , vol.303 , Issue.20 , pp. 2017-2019
    • Voelker, R.1
  • 3
    • 28844441314 scopus 로고    scopus 로고
    • A predominantly clonal multi-institutional outbreak of Clostridium difficile-associated diarrhea with high morbidity and mortality
    • Loo VG, et al. (2005) A predominantly clonal multi-institutional outbreak of Clostridium difficile-associated diarrhea with high morbidity and mortality. N Engl J Med 353(23):2442-2449.
    • (2005) N Engl J Med , vol.353 , Issue.23 , pp. 2442-2449
    • Loo, V.G.1
  • 4
    • 28844494086 scopus 로고    scopus 로고
    • An epidemic, toxin gene-variant strain of Clostridium difficile
    • McDonald LC, et al. (2005) An epidemic, toxin gene-variant strain of Clostridium difficile. N Engl J Med 353(23):2433-2441.
    • (2005) N Engl J Med , vol.353 , Issue.23 , pp. 2433-2441
    • McDonald, L.C.1
  • 5
    • 17444366186 scopus 로고    scopus 로고
    • Clostridium difficile toxins: Mechanism of action and role in disease
    • Voth DE, Ballard JD (2005) Clostridium difficile toxins: Mechanism of action and role in disease. Clin Microbiol Rev 18(2):247-263.
    • (2005) Clin Microbiol Rev , vol.18 , Issue.2 , pp. 247-263
    • Voth, D.E.1    Ballard, J.D.2
  • 7
    • 79952418425 scopus 로고    scopus 로고
    • Structural determinants for membrane insertion, pore formation and translocation of Clostridium difficile toxin B
    • Genisyuerek S, et al. (2011) Structural determinants for membrane insertion, pore formation and translocation of Clostridium difficile toxin B. Mol Microbiol 79(6): 1643-1654.
    • (2011) Mol Microbiol , vol.79 , Issue.6 , pp. 1643-1654
    • Genisyuerek, S.1
  • 8
    • 33947502604 scopus 로고    scopus 로고
    • Autocatalytic cleavage of Clostridium difficile toxin B
    • Reineke J, et al. (2007) Autocatalytic cleavage of Clostridium difficile toxin B. Nature 446(7134):415-419.
    • (2007) Nature , vol.446 , Issue.7134 , pp. 415-419
    • Reineke, J.1
  • 9
    • 0029011449 scopus 로고
    • The enterotoxin from Clostridium difficile (ToxA) monoglucosylates the Rho proteins
    • Just I, et al. (1995) The enterotoxin from Clostridium difficile (ToxA) monoglucosylates the Rho proteins. J Biol Chem 270(23):13932-13936.
    • (1995) J Biol Chem , vol.270 , Issue.23 , pp. 13932-13936
    • Just, I.1
  • 10
    • 0029054398 scopus 로고
    • Glucosylation of Rho proteins by Clostridium difficile toxin B
    • Just I, et al. (1995) Glucosylation of Rho proteins by Clostridium difficile toxin B. Nature 375(6531):500-503.
    • (1995) Nature , vol.375 , Issue.6531 , pp. 500-503
    • Just, I.1
  • 11
    • 0036312873 scopus 로고    scopus 로고
    • Clostridium difficile toxin B activates dual caspase-dependent and caspase-independent apoptosis in intoxicated cells
    • Qa'Dan M, et al. (2002) Clostridium difficile toxin B activates dual caspase-dependent and caspase-independent apoptosis in intoxicated cells. Cell Microbiol 4(7):425-434.
    • (2002) Cell Microbiol , vol.4 , Issue.7 , pp. 425-434
    • Qa'Dan, M.1
  • 12
    • 84872017421 scopus 로고    scopus 로고
    • Clostridium difficile Toxin B causes epithelial cell necrosis through an autoprocessing-independent mechanism
    • Chumbler NM, et al. (2012) Clostridium difficile Toxin B causes epithelial cell necrosis through an autoprocessing-independent mechanism. PLoS Pathog 8(12):e1003072.
    • (2012) PLoS Pathog , vol.8 , Issue.12
    • Chumbler, N.M.1
  • 13
    • 84887476533 scopus 로고    scopus 로고
    • Clostridium difficile toxin B-induced necrosis is mediated by the host epithelial cell NADPH oxidase complex
    • Farrow MA, et al. (2013) Clostridium difficile toxin B-induced necrosis is mediated by the host epithelial cell NADPH oxidase complex. Proc Natl Acad Sci USA 110(46):18674-18679.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.46 , pp. 18674-18679
    • Farrow, M.A.1
  • 14
    • 67349114409 scopus 로고    scopus 로고
    • Toxin B is essential for virulence of Clostridium difficile
    • Lyras D, et al. (2009) Toxin B is essential for virulence of Clostridium difficile. Nature 458(7242):1176-1179.
    • (2009) Nature , vol.458 , Issue.7242 , pp. 1176-1179
    • Lyras, D.1
  • 15
    • 77957988127 scopus 로고    scopus 로고
    • The role of toxin A and toxin B in Clostridium difficile infection
    • Kuehne SA, et al. (2010) The role of toxin A and toxin B in Clostridium difficile infection. Nature 467(7316):711-713.
    • (2010) Nature , vol.467 , Issue.7316 , pp. 711-713
    • Kuehne, S.A.1
  • 16
    • 0030931082 scopus 로고    scopus 로고
    • Toxins A and B from Clostridium difficile differ with respect to enzymatic potencies, cellular substrate specificities, and surface binding to cultured cells
    • Chaves-Olarte E, Weidmann M, Eichel-Streiber C, Thelestam M (1997) Toxins A and B from Clostridium difficile differ with respect to enzymatic potencies, cellular substrate specificities, and surface binding to cultured cells. J Clin Invest 100(7):1734-1741.
    • (1997) J Clin Invest , vol.100 , Issue.7 , pp. 1734-1741
    • Chaves-Olarte, E.1    Weidmann, M.2    Eichel-Streiber, C.3    Thelestam, M.4
  • 17
    • 58149115498 scopus 로고    scopus 로고
    • Functional properties of the carboxy-terminal host cell-binding domains of the two toxins, TcdA and TcdB, expressed by Clostridium difficile
    • Dingle T, et al. (2008) Functional properties of the carboxy-terminal host cell-binding domains of the two toxins, TcdA and TcdB, expressed by Clostridium difficile. Glycobiology 18(9):698-706.
    • (2008) Glycobiology , vol.18 , Issue.9 , pp. 698-706
    • Dingle, T.1
  • 18
    • 0022525082 scopus 로고
    • Cell surface binding site for Clostridium difficile enterotoxin: Evidence for a glycoconjugate containing the sequence Gal alpha 1-3Gal beta 1-4GlcNAc
    • Krivan HC, Clark GF, Smith DF, Wilkins TD (1986) Cell surface binding site for Clostridium difficile enterotoxin: Evidence for a glycoconjugate containing the sequence Gal alpha 1-3Gal beta 1-4GlcNAc. Infect Immun 53(3):573-581.
    • (1986) Infect Immun , vol.53 , Issue.3 , pp. 573-581
    • Krivan, H.C.1    Clark, G.F.2    Smith, D.F.3    Wilkins, T.D.4
  • 19
    • 0037449918 scopus 로고    scopus 로고
    • The complete receptor-binding domain of Clostridium difficile toxin A is required for endocytosis
    • Frisch C, Gerhard R, Aktories K, Hofmann F, Just I (2003) The complete receptor-binding domain of Clostridium difficile toxin A is required for endocytosis. Biochem Biophys Res Commun 300(3):706-711.
    • (2003) Biochem Biophys Res Commun , vol.300 , Issue.3 , pp. 706-711
    • Frisch, C.1    Gerhard, R.2    Aktories, K.3    Hofmann, F.4    Just, I.5
  • 20
    • 46449130378 scopus 로고    scopus 로고
    • gp96 is a human colonocyte plasma membrane binding protein for Clostridium difficile toxin A
    • Na X, Kim H, Moyer MP, Pothoulakis C, LaMont JT (2008) gp96 is a human colonocyte plasma membrane binding protein for Clostridium difficile toxin A. Infect Immun 76(7):2862-2871.
    • (2008) Infect Immun , vol.76 , Issue.7 , pp. 2862-2871
    • Na, X.1    Kim, H.2    Moyer, M.P.3    Pothoulakis, C.4    LaMont, J.T.5
  • 21
    • 0026078094 scopus 로고
    • Toxin A of Clostridium difficile binds to the human carbohydrate antigens I, X, and Y
    • Tucker KD, Wilkins TD (1991) Toxin A of Clostridium difficile binds to the human carbohydrate antigens I, X, and Y. Infect Immun 59(1):73-78.
    • (1991) Infect Immun , vol.59 , Issue.1 , pp. 73-78
    • Tucker, K.D.1    Wilkins, T.D.2
  • 22
    • 10244233005 scopus 로고    scopus 로고
    • Rabbit sucrase-isomaltase contains a functional intestinal receptor for Clostridium difficile toxin A
    • Pothoulakis C, et al. (1996) Rabbit sucrase-isomaltase contains a functional intestinal receptor for Clostridium difficile toxin A. J Clin Invest 98(3):641-649.
    • (1996) J Clin Invest , vol.98 , Issue.3 , pp. 641-649
    • Pothoulakis, C.1
  • 23
    • 33745086500 scopus 로고    scopus 로고
    • Carbohydrate recognition by Clostridium difficile toxin A
    • Greco A, et al. (2006) Carbohydrate recognition by Clostridium difficile toxin A. Nat Struct Mol Biol 13(5):460-461.
    • (2006) Nat Struct Mol Biol , vol.13 , Issue.5 , pp. 460-461
    • Greco, A.1
  • 24
    • 0025667927 scopus 로고
    • Clostridium difficile toxin A carries a C-terminal repetitive structure homologous to the carbohydrate binding region of streptococcal glycosyltransferases
    • von Eichel-Streiber C, Sauerborn M (1990) Clostridium difficile toxin A carries a C-terminal repetitive structure homologous to the carbohydrate binding region of streptococcal glycosyltransferases. Gene 96(1):107-113.
    • (1990) Gene , vol.96 , Issue.1 , pp. 107-113
    • Von Eichel-Streiber, C.1    Sauerborn, M.2
  • 25
    • 0026764540 scopus 로고
    • Localization of two epitopes recognized by monoclonal antibody PCG-4 on Clostridium difficile toxin A
    • Frey SM, Wilkins TD (1992) Localization of two epitopes recognized by monoclonal antibody PCG-4 on Clostridium difficile toxin A. Infect Immun 60(6):2488-2492.
    • (1992) Infect Immun , vol.60 , Issue.6 , pp. 2488-2492
    • Frey, S.M.1    Wilkins, T.D.2
  • 26
    • 84903537030 scopus 로고    scopus 로고
    • Mechanism of action and epitopes of Clostridium difficile toxin B-neutralizing antibody bezlotoxumab revealed by X-ray crystallography
    • Orth P, et al. (2014) Mechanism of action and epitopes of Clostridium difficile toxin B-neutralizing antibody bezlotoxumab revealed by X-ray crystallography. J Biol Chem 289(26):18008-18021.
    • (2014) J Biol Chem , vol.289 , Issue.26 , pp. 18008-18021
    • Orth, P.1
  • 27
    • 0031446325 scopus 로고    scopus 로고
    • The C-terminal ligand-binding domain of Clostridium difficile toxin A (TcdA) abrogates TcdA-specific binding to cells and prevents mouse lethality
    • Sauerborn M, Leukel P, von Eichel-Streiber C (1997) The C-terminal ligand-binding domain of Clostridium difficile toxin A (TcdA) abrogates TcdA-specific binding to cells and prevents mouse lethality. FEMS Microbiol Lett 155(1):45-54.
    • (1997) FEMS Microbiol Lett , vol.155 , Issue.1 , pp. 45-54
    • Sauerborn, M.1    Leukel, P.2    Von Eichel-Streiber, C.3
  • 28
    • 79952803707 scopus 로고    scopus 로고
    • The repetitive oligopeptide sequences modulate cytopathic potency but are not crucial for cellular uptake of Clostridium difficile toxin A
    • Olling A, et al. (2011) The repetitive oligopeptide sequences modulate cytopathic potency but are not crucial for cellular uptake of Clostridium difficile toxin A. PLoS ONE 6(3):e17623.
    • (2011) PLoS ONE , vol.6 , Issue.3
    • Olling, A.1
  • 29
    • 84899641495 scopus 로고    scopus 로고
    • LRP1 is a receptor for Clostridium perfringens TpeL toxin indicating a two-receptor model of clostridial glycosylating toxins
    • Schorch B, et al. (2014) LRP1 is a receptor for Clostridium perfringens TpeL toxin indicating a two-receptor model of clostridial glycosylating toxins. Proc Natl Acad Sci USA 111(17):6431-6436.
    • (2014) Proc Natl Acad Sci USA , vol.111 , Issue.17 , pp. 6431-6436
    • Schorch, B.1
  • 30
    • 34247229774 scopus 로고    scopus 로고
    • A novel toxin homologous to large clostridial cytotoxins found in culture supernatant of Clostridium perfringens type C
    • Amimoto K, Noro T, Oishi E, Shimizu M (2007) A novel toxin homologous to large clostridial cytotoxins found in culture supernatant of Clostridium perfringens type C. Microbiology 153(Pt 4):1198-1206.
    • (2007) Microbiology , vol.153 , Issue.4 , pp. 1198-1206
    • Amimoto, K.1    Noro, T.2    Oishi, E.3    Shimizu, M.4
  • 31
    • 84922252575 scopus 로고    scopus 로고
    • Chondroitin sulfate proteoglycan 4 functions as the cellular receptor for Clostridium difficile toxin B
    • Yuan P, et al. (2015) Chondroitin sulfate proteoglycan 4 functions as the cellular receptor for Clostridium difficile toxin B. Cell Res 25(2):157-168.
    • (2015) Cell Res , vol.25 , Issue.2 , pp. 157-168
    • Yuan, P.1
  • 32
    • 3042796396 scopus 로고    scopus 로고
    • Activation of cryptic 3′ splice sites within introns of cellular genes following gene entrapment
    • Osipovich AB, et al. (2004) Activation of cryptic 3′ splice sites within introns of cellular genes following gene entrapment. Nucleic Acids Res 32(9):2912-2924.
    • (2004) Nucleic Acids Res , vol.32 , Issue.9 , pp. 2912-2924
    • Osipovich, A.B.1
  • 33
    • 33748949587 scopus 로고    scopus 로고
    • Immunohistochemical study of NG2 chondroitin sulfate proteoglycan expression in the small and large intestines
    • Terada N, et al. (2006) Immunohistochemical study of NG2 chondroitin sulfate proteoglycan expression in the small and large intestines. Histochem Cell Biol 126(4):483-490.
    • (2006) Histochem Cell Biol , vol.126 , Issue.4 , pp. 483-490
    • Terada, N.1
  • 34
    • 70849098603 scopus 로고    scopus 로고
    • Haploid genetic screens in human cells identify host factors used by pathogens
    • Carette JE, et al. (2009) Haploid genetic screens in human cells identify host factors used by pathogens. Science 326(5957):1231-1235.
    • (2009) Science , vol.326 , Issue.5957 , pp. 1231-1235
    • Carette, J.E.1
  • 35
    • 2442667691 scopus 로고    scopus 로고
    • Translocation of Clostridium difficile toxin B across polarized Caco-2 cell monolayers is enhanced by toxin A
    • Du T, Alfa MJ (2004) Translocation of Clostridium difficile toxin B across polarized Caco-2 cell monolayers is enhanced by toxin A. Can J Infect Dis Med Microbiol 15(2):83-88.
    • (2004) Can J Infect Dis Med Microbiol , vol.15 , Issue.2 , pp. 83-88
    • Du, T.1    Alfa, M.J.2
  • 36
    • 0028786481 scopus 로고
    • The human intestinal epithelial cell line Caco-2; pharmacological and pharmacokinetic applications
    • Meunier V, Bourrié M, Berger Y, Fabre G (1995) The human intestinal epithelial cell line Caco-2; pharmacological and pharmacokinetic applications. Cell Biol Toxicol 11(3-4):187-194.
    • (1995) Cell Biol Toxicol , vol.11 , Issue.3-4 , pp. 187-194
    • Meunier, V.1    Bourrié, M.2    Berger, Y.3    Fabre, G.4
  • 37
    • 79952589531 scopus 로고    scopus 로고
    • Gene-trap mutagenesis identifies mammalian genes contributing to intoxication by Clostridium perfringens ε-toxin
    • Ivie SE, Fennessey CM, Sheng J, Rubin DH, McClain MS (2011) Gene-trap mutagenesis identifies mammalian genes contributing to intoxication by Clostridium perfringens ε-toxin. PLoS ONE 6(3):e17787.
    • (2011) PLoS ONE , vol.6 , Issue.3
    • Ivie, S.E.1    Fennessey, C.M.2    Sheng, J.3    Rubin, D.H.4    McClain, M.S.5
  • 38
    • 35548932931 scopus 로고    scopus 로고
    • Nectin and nectin-like molecules: Biology and pathology
    • Miyoshi J, Takai Y (2007) Nectin and nectin-like molecules: Biology and pathology. Am J Nephrol 27(6):590-604.
    • (2007) Am J Nephrol , vol.27 , Issue.6 , pp. 590-604
    • Miyoshi, J.1    Takai, Y.2
  • 39
    • 0024519677 scopus 로고
    • Cellular receptor for poliovirus: Molecular cloning, nucleotide sequence, and expression of a new member of the immunoglobulin superfamily
    • Mendelsohn CL, Wimmer E, Racaniello VR (1989) Cellular receptor for poliovirus: Molecular cloning, nucleotide sequence, and expression of a new member of the immunoglobulin superfamily. Cell 56(5):855-865.
    • (1989) Cell , vol.56 , Issue.5 , pp. 855-865
    • Mendelsohn, C.L.1    Wimmer, E.2    Racaniello, V.R.3
  • 40
    • 0031797729 scopus 로고    scopus 로고
    • The ectodomain of a novel member of the immunoglobulin subfamily related to the poliovirus receptor has the attributes of a bona fide receptor for herpes simplex virus types 1 and 2 in human cells
    • Cocchi F, Menotti L, Mirandola P, Lopez M, Campadelli-Fiume G (1998) The ectodomain of a novel member of the immunoglobulin subfamily related to the poliovirus receptor has the attributes of a bona fide receptor for herpes simplex virus types 1 and 2 in human cells. J Virol 72(12):9992-10002.
    • (1998) J Virol , vol.72 , Issue.12 , pp. 9992-10002
    • Cocchi, F.1    Menotti, L.2    Mirandola, P.3    Lopez, M.4    Campadelli-Fiume, G.5
  • 41
    • 0032486317 scopus 로고    scopus 로고
    • Entry of alphaherpesviruses mediated by poliovirus receptor-related protein 1 and poliovirus receptor
    • Geraghty RJ, Krummenacher C, Cohen GH, Eisenberg RJ, Spear PG (1998) Entry of alphaherpesviruses mediated by poliovirus receptor-related protein 1 and poliovirus receptor. Science 280(5369):1618-1620.
    • (1998) Science , vol.280 , Issue.5369 , pp. 1618-1620
    • Geraghty, R.J.1    Krummenacher, C.2    Cohen, G.H.3    Eisenberg, R.J.4    Spear, P.G.5
  • 42
    • 84355161614 scopus 로고    scopus 로고
    • Adherens junction protein nectin-4 is the epithelial receptor for measles virus
    • Mühlebach MD, et al. (2011) Adherens junction protein nectin-4 is the epithelial receptor for measles virus. Nature 480(7378):530-533.
    • (2011) Nature , vol.480 , Issue.7378 , pp. 530-533
    • Mühlebach, M.D.1
  • 43
    • 80052315535 scopus 로고    scopus 로고
    • Tumor cell marker PVRL4 (nectin 4) is an epithelial cell receptor for measles virus
    • Noyce RS, et al. (2011) Tumor cell marker PVRL4 (nectin 4) is an epithelial cell receptor for measles virus. PLoS Pathog 7(8):e1002240.
    • (2011) PLoS Pathog , vol.7 , Issue.8
    • Noyce, R.S.1
  • 44
    • 84866150205 scopus 로고    scopus 로고
    • Nectin4 is an epithelial cell receptor for canine distemper virus and involved in neurovirulence
    • Pratakpiriya W, et al. (2012) Nectin4 is an epithelial cell receptor for canine distemper virus and involved in neurovirulence. J Virol 86(18):10207-10210.
    • (2012) J Virol , vol.86 , Issue.18 , pp. 10207-10210
    • Pratakpiriya, W.1
  • 45
    • 84901926679 scopus 로고    scopus 로고
    • The tumor-associated marker, PVRL4 (nectin-4), is the epithelial receptor for morbilliviruses
    • Delpeut S, Noyce RS, Richardson CD (2014) The tumor-associated marker, PVRL4 (nectin-4), is the epithelial receptor for morbilliviruses. Viruses 6(6):2268-2286.
    • (2014) Viruses , vol.6 , Issue.6 , pp. 2268-2286
    • Delpeut, S.1    Noyce, R.S.2    Richardson, C.D.3
  • 46
    • 0034616002 scopus 로고    scopus 로고
    • Nectin-3, a new member of immunoglobulin-like cell adhesion molecules that shows homophilic and heterophilic cell-cell adhesion activities
    • Satoh-Horikawa K, et al. (2000) Nectin-3, a new member of immunoglobulin-like cell adhesion molecules that shows homophilic and heterophilic cell-cell adhesion activities. J Biol Chem 275(14):10291-10299.
    • (2000) J Biol Chem , vol.275 , Issue.14 , pp. 10291-10299
    • Satoh-Horikawa, K.1
  • 47
    • 80052155237 scopus 로고    scopus 로고
    • Nectins establish a checkerboard-like cellular pattern in the auditory epithelium
    • Togashi H, et al. (2011) Nectins establish a checkerboard-like cellular pattern in the auditory epithelium. Science 333(6046):1144-1147.
    • (2011) Science , vol.333 , Issue.6046 , pp. 1144-1147
    • Togashi, H.1
  • 48
    • 30344475861 scopus 로고    scopus 로고
    • Virus-induced Abl and Fyn kinase signals permit coxsackievirus entry through epithelial tight junctions
    • Coyne CB, Bergelson JM (2006) Virus-induced Abl and Fyn kinase signals permit coxsackievirus entry through epithelial tight junctions. Cell 124(1):119-131.
    • (2006) Cell , vol.124 , Issue.1 , pp. 119-131
    • Coyne, C.B.1    Bergelson, J.M.2
  • 49
    • 0035830509 scopus 로고    scopus 로고
    • Junction adhesion molecule is a receptor for reovirus
    • Barton ES, et al. (2001) Junction adhesion molecule is a receptor for reovirus. Cell 104(3):441-451.
    • (2001) Cell , vol.104 , Issue.3 , pp. 441-451
    • Barton, E.S.1
  • 50
    • 63249098521 scopus 로고    scopus 로고
    • Tight junctions as targets of infectious agents
    • Guttman JA, Finlay BB (2009) Tight junctions as targets of infectious agents. Biochim Biophys Acta 1788(4):832-841.
    • (2009) Biochim Biophys Acta , vol.1788 , Issue.4 , pp. 832-841
    • Guttman, J.A.1    Finlay, B.B.2
  • 51
    • 0030846016 scopus 로고    scopus 로고
    • Molecular cloning and functional characterization of the receptor for Clostridium perfringens enterotoxin
    • Katahira J, Inoue N, Horiguchi Y, Matsuda M, Sugimoto N (1997) Molecular cloning and functional characterization of the receptor for Clostridium perfringens enterotoxin. J Cell Biol 136(6):1239-1247.
    • (1997) J Cell Biol , vol.136 , Issue.6 , pp. 1239-1247
    • Katahira, J.1    Inoue, N.2    Horiguchi, Y.3    Matsuda, M.4    Sugimoto, N.5
  • 52
    • 33645777012 scopus 로고    scopus 로고
    • Listeria monocytogenes invades the epithelial junctions at sites of cell extrusion
    • Pentecost M, Otto G, Theriot JA, Amieva MR (2006) Listeria monocytogenes invades the epithelial junctions at sites of cell extrusion. PLoS Pathog 2(1):e3.
    • (2006) PLoS Pathog , vol.2 , Issue.1 , pp. e3
    • Pentecost, M.1    Otto, G.2    Theriot, J.A.3    Amieva, M.R.4
  • 53
    • 0024204607 scopus 로고
    • Clostridium difficile toxin A perturbs cytoskeletal structure and tight junction permeability of cultured human intestinal epithelial monolayers
    • Hecht G, Pothoulakis C, LaMont JT, Madara JL (1988) Clostridium difficile toxin A perturbs cytoskeletal structure and tight junction permeability of cultured human intestinal epithelial monolayers. J Clin Invest 82(5):1516-1524.
    • (1988) J Clin Invest , vol.82 , Issue.5 , pp. 1516-1524
    • Hecht, G.1    Pothoulakis, C.2    LaMont, J.T.3    Madara, J.L.4
  • 54
  • 55
    • 0023269823 scopus 로고
    • Cellular internalisation of Clostridium difficile toxin A
    • Henriques B, Florin I, Thelestam M (1987) Cellular internalisation of Clostridium difficile toxin A. Microb Pathog 2(6):455-463.
    • (1987) Microb Pathog , vol.2 , Issue.6 , pp. 455-463
    • Henriques, B.1    Florin, I.2    Thelestam, M.3
  • 56
    • 0035815642 scopus 로고    scopus 로고
    • Low pH-induced formation of ion channels by clostridium difficile toxin B in target cells
    • Barth H, et al. (2001) Low pH-induced formation of ion channels by clostridium difficile toxin B in target cells. J Biol Chem 276(14):10670-10676.
    • (2001) J Biol Chem , vol.276 , Issue.14 , pp. 10670-10676
    • Barth, H.1
  • 57
    • 26444569379 scopus 로고    scopus 로고
    • Inhibition of cell movement and proliferation by cell-cell contact-induced interaction of Necl-5 with nectin-3
    • Fujito T, et al. (2005) Inhibition of cell movement and proliferation by cell-cell contact-induced interaction of Necl-5 with nectin-3. J Cell Biol 171(1):165-173.
    • (2005) J Cell Biol , vol.171 , Issue.1 , pp. 165-173
    • Fujito, T.1
  • 58
    • 24644515265 scopus 로고    scopus 로고
    • Rab9 GTPase is required for replication of human immunodeficiency virus type 1, filoviruses, and measles virus
    • Murray JL, et al. (2005) Rab9 GTPase is required for replication of human immunodeficiency virus type 1, filoviruses, and measles virus. J Virol 79(18):11742-11751.
    • (2005) J Virol , vol.79 , Issue.18 , pp. 11742-11751
    • Murray, J.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.