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Volumn 83, Issue 5, 2012, Pages 1006-1023

The mammalian cell entry (Mce) protein of pathogenic Leptospira species is responsible for RGD motif-dependent infection of cells and animals

Author keywords

[No Author keywords available]

Indexed keywords

ALPHAVBETA1 INTEGRIN; ARGINYLGLYCYLASPARTIC ACID; BACTERIAL PROTEIN; INTEGRIN; MAMMALIAN CELL ENTRY PROTEIN; MESSENGER RNA; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG; VIRULENCE FACTOR; VITRONECTIN RECEPTOR;

EID: 84862795039     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2012.07985.x     Document Type: Article
Times cited : (84)

References (72)
  • 1
    • 73949084950 scopus 로고    scopus 로고
    • Leptospira and leptospirosis
    • Adler, B., and Moctezuma, A. (2010) Leptospira and leptospirosis. Vet Microbiol 140: 287-296.
    • (2010) Vet Microbiol , vol.140 , pp. 287-296
    • Adler, B.1    Moctezuma, A.2
  • 2
    • 0027424110 scopus 로고
    • Cloning of a Mycobacterium tuberculosis DNA fragment associated with entry and survival inside cells
    • Arruda, S., Bomfim, G., Knights, R., Huima, B.T., and Riley, L.W. (1993) Cloning of a Mycobacterium tuberculosis DNA fragment associated with entry and survival inside cells. Science 261: 1454-1457.
    • (1993) Science , vol.261 , pp. 1454-1457
    • Arruda, S.1    Bomfim, G.2    Knights, R.3    Huima, B.T.4    Riley, L.W.5
  • 5
    • 0037352557 scopus 로고    scopus 로고
    • Construction and complementation of the first auxotrophic mutant in the spirochaete Leptospira meyeri
    • Bauby, H., Saint, G.I., and Picardeau, M. (2003) Construction and complementation of the first auxotrophic mutant in the spirochaete Leptospira meyeri. Microbiology 149: 689-693.
    • (2003) Microbiology , vol.149 , pp. 689-693
    • Bauby, H.1    Saint, G.I.2    Picardeau, M.3
  • 6
    • 0029923793 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis invades and replicates within type II alveolar cells
    • Bermudez, L.E., and Goodman, J. (1996) Mycobacterium tuberculosis invades and replicates within type II alveolar cells. Infect Immun 64: 1400-1406.
    • (1996) Infect Immun , vol.64 , pp. 1400-1406
    • Bermudez, L.E.1    Goodman, J.2
  • 8
    • 20444434362 scopus 로고    scopus 로고
    • Complete nucleotide sequence of the LE1 prophage from the spirochete Leptospira biflexa and characterization of its replication and partition functions
    • Bourhy, P., Frangeul, L., Couvé, E., Glaser, P., Saint, G.I., and Picardeau, M. (2005) Complete nucleotide sequence of the LE1 prophage from the spirochete Leptospira biflexa and characterization of its replication and partition functions. J Bacteriol 187: 3931-3940.
    • (2005) J Bacteriol , vol.187 , pp. 3931-3940
    • Bourhy, P.1    Frangeul, L.2    Couvé, E.3    Glaser, P.4    Saint, G.I.5    Picardeau, M.6
  • 9
    • 0141756140 scopus 로고    scopus 로고
    • Bacterial pathogenesis: exploiting cellular adherence
    • Boyle, E.C., and Finlay, B.B. (2003) Bacterial pathogenesis: exploiting cellular adherence. Curr Opin Cell Biol 15: 633-639.
    • (2003) Curr Opin Cell Biol , vol.15 , pp. 633-639
    • Boyle, E.C.1    Finlay, B.B.2
  • 10
    • 43549124764 scopus 로고    scopus 로고
    • Selection of the internal control gene for real-time quantitative RT-PCR assays in temperature treated Leptospira
    • Carrillo-Casas, E.M., Hernández-Castro, R., Suárez-Güemes, F., and De la Peña-Moctezuma, A. (2008) Selection of the internal control gene for real-time quantitative RT-PCR assays in temperature treated Leptospira. Curr Microbiol 56: 539-546.
    • (2008) Curr Microbiol , vol.56 , pp. 539-546
    • Carrillo-Casas, E.M.1    Hernández-Castro, R.2    Suárez-Güemes, F.3    De la Peña-Moctezuma, A.4
  • 11
    • 35748983212 scopus 로고    scopus 로고
    • Immunogenicity of the recombinant leptospiral putative outer membrane proteins as vaccine candidates
    • Chang, Y.F., Chen, C.S., Palaniappan, R.U., He, H., McDonough, S.P., and Barr, S.C. (2007) Immunogenicity of the recombinant leptospiral putative outer membrane proteins as vaccine candidates. Vaccine 25: 8190-8197.
    • (2007) Vaccine , vol.25 , pp. 8190-8197
    • Chang, Y.F.1    Chen, C.S.2    Palaniappan, R.U.3    He, H.4    McDonough, S.P.5    Barr, S.C.6
  • 12
    • 0035048706 scopus 로고    scopus 로고
    • Recombinant Mycobacterium tuberculosis protein associated with mammalian cell entry
    • Chitale, S., Ehrt, S., Kawamura, I., Fujimura, T., Shimono, N., Anand, N., etal. (2001) Recombinant Mycobacterium tuberculosis protein associated with mammalian cell entry. Cell Microbiol 3: 247-254.
    • (2001) Cell Microbiol , vol.3 , pp. 247-254
    • Chitale, S.1    Ehrt, S.2    Kawamura, I.3    Fujimura, T.4    Shimono, N.5    Anand, N.6
  • 13
    • 34248368916 scopus 로고    scopus 로고
    • Physiological osmotic induction of Leptospira interrogans adhesion: LigA and LigB bind extracellular matrix proteins and fibrinogen
    • Choy, H.A., Kelley, M.M., Chen, T.L., Moller, A.K., Matsunaga, J., and Haake, D.A. (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    Moller, A.K.4    Matsunaga, J.5    Haake, D.A.6
  • 14
    • 0019580428 scopus 로고
    • Studies on the interaction between macrophages and leptospires
    • Cinco, M., Banfi, E., and Soranzo, M.R. (1981) Studies on the interaction between macrophages and leptospires. J Gen Microbiol 4: 409-413.
    • (1981) J Gen Microbiol , vol.4 , pp. 409-413
    • Cinco, M.1    Banfi, E.2    Soranzo, M.R.3
  • 15
    • 0032508046 scopus 로고    scopus 로고
    • Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence
    • Cole, S.T., Brosch, R., Parkhill, J., Garnier, T., Churcher, C., Harris, D., etal. (1998) Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature 393: 537-544.
    • (1998) Nature , vol.393 , pp. 537-544
    • Cole, S.T.1    Brosch, R.2    Parkhill, J.3    Garnier, T.4    Churcher, C.5    Harris, D.6
  • 16
    • 57349178393 scopus 로고    scopus 로고
    • Targeted mutagenesis in pathogenic Leptospira species: disruption of the LigB gene does not affect virulence in animal models of leptospirosis
    • Croda, J., Figueira, C.P., Wunder, E.A., Santos, C.S., Reis, M.G., and Ko, A.I. (2008) Targeted mutagenesis in pathogenic Leptospira species: disruption of the LigB gene does not affect virulence in animal models of leptospirosis. Infect Immun 76: 5826-5833.
    • (2008) Infect Immun , vol.76 , pp. 5826-5833
    • Croda, J.1    Figueira, C.P.2    Wunder, E.A.3    Santos, C.S.4    Reis, M.G.5    Ko, A.I.6
  • 17
    • 68349115091 scopus 로고    scopus 로고
    • Leptospira interrogans stably infects zebrafish embryos, altering phagocyte behavior and homing to specific tissues
    • Davis, J.M., Haake, D.A., and Ramakrishnan, L. (2009) Leptospira interrogans stably infects zebrafish embryos, altering phagocyte behavior and homing to specific tissues. PLoS Negl Trop Dis 3: e463.
    • (2009) PLoS Negl Trop Dis , vol.3
    • Davis, J.M.1    Haake, D.A.2    Ramakrishnan, L.3
  • 18
    • 68249158537 scopus 로고    scopus 로고
    • Virus binding to a plasma membrane receptor triggers interleukin-1 alpha-mediated proinflammatory macrophage response in vivo
    • Dipaolo, N.C., Miao, E.A., Iwakura, Y., Murali, K.K., Aderem, A., Flavell, R.A., etal. (2009) Virus binding to a plasma membrane receptor triggers interleukin-1 alpha-mediated proinflammatory macrophage response in vivo. Immunity 31: 110-121.
    • (2009) Immunity , vol.31 , pp. 110-121
    • Dipaolo, N.C.1    Miao, E.A.2    Iwakura, Y.3    Murali, K.K.4    Aderem, A.5    Flavell, R.A.6
  • 19
    • 60149089675 scopus 로고    scopus 로고
    • Characterization of the ompL1 gene of pathogenic Leptospira species in China and cross-immunogenicity of the OmpL1 protein
    • Dong, H.Y., Hu, Y., Xue, F., Sun, D., Ojcius, D.M., Mao, Y.F., etal. (2008) Characterization of the ompL1 gene of pathogenic Leptospira species in China and cross-immunogenicity of the OmpL1 protein. BMC Microbiol 8: 223-235.
    • (2008) BMC Microbiol , vol.8 , pp. 223-235
    • Dong, H.Y.1    Hu, Y.2    Xue, F.3    Sun, D.4    Ojcius, D.M.5    Mao, Y.F.6
  • 20
    • 34547628246 scopus 로고    scopus 로고
    • Regulated degradation of the HIV-1 Vpu protein through a betaTrCP-independent pathway limits the release of viral particles
    • Estrabaud, E., Le, R.E., Lopez-Vergès, S., Morel, M., Belaïdouni, N., Benarous, R., etal. (2007) Regulated degradation of the HIV-1 Vpu protein through a betaTrCP-independent pathway limits the release of viral particles. PLoS Pathog 3: e104.
    • (2007) PLoS Pathog , vol.3
    • Estrabaud, E.1    Le, R.E.2    Lopez-Vergès, S.3    Morel, M.4    Belaïdouni, N.5    Benarous, R.6
  • 21
    • 77957582069 scopus 로고    scopus 로고
    • Leptospira as an emerging pathogen: a review of its biology, pathogenesis and host immune responses
    • Evangelista, K.V., and Coburn, J. (2010) Leptospira as an emerging pathogen: a review of its biology, pathogenesis and host immune responses. Future Microbiol 5: 1413-1425.
    • (2010) Future Microbiol , vol.5 , pp. 1413-1425
    • Evangelista, K.V.1    Coburn, J.2
  • 23
    • 0032815631 scopus 로고    scopus 로고
    • Disruption of the mycobacterial cell entry gene of Mycobacterium bovis BCG results in a mutant that exhibits a reduced invasiveness for epithelial cells
    • Flesselles, B., Anand, N.N., Remani, J., Loosmore, S.M., and Klein, M.H. (1999) Disruption of the mycobacterial cell entry gene of Mycobacterium bovis BCG results in a mutant that exhibits a reduced invasiveness for epithelial cells. FEMS Microbiol Lett 177: 237-242.
    • (1999) FEMS Microbiol Lett , vol.177 , pp. 237-242
    • Flesselles, B.1    Anand, N.N.2    Remani, J.3    Loosmore, S.M.4    Klein, M.H.5
  • 24
    • 33644761790 scopus 로고    scopus 로고
    • A mycobacterial operon essential for virulence in vivo and invasion and intracellular persistence in macrophages
    • Gao, L.Y., Pak, M., Kish, R., Kajihara, K., and Brown, E.J. (2006) A mycobacterial operon essential for virulence in vivo and invasion and intracellular persistence in macrophages. Infect Immun 74: 1757-1767.
    • (2006) Infect Immun , vol.74 , pp. 1757-1767
    • Gao, L.Y.1    Pak, M.2    Kish, R.3    Kajihara, K.4    Brown, E.J.5
  • 25
    • 38349134847 scopus 로고    scopus 로고
    • Integrin alphaVbeta3 binds to the RGD motif of glycoprotein B of Kaposi's sarcoma-associated herpesvirus and functions as an RGD-dependent entry receptor
    • Garrigues, H.J., Rubinchikova, Y.E., Dipersio, C.M., and Rose, T.M. (2008) Integrin alphaVbeta3 binds to the RGD motif of glycoprotein B of Kaposi's sarcoma-associated herpesvirus and functions as an RGD-dependent entry receptor. J Virol 82: 1570-1580.
    • (2008) J Virol , vol.82 , pp. 1570-1580
    • Garrigues, H.J.1    Rubinchikova, Y.E.2    Dipersio, C.M.3    Rose, T.M.4
  • 27
    • 46249119468 scopus 로고    scopus 로고
    • In LipL32, the major leptospiral lipoprotein, the C terminus is the primary immunogenic domain and mediates interaction with collagen IV and plasma fibronectin
    • Hauk, P., Macedo, F., Romero, E.C., Vasconcellos, S.A., Morais, Z.M., Barbosa, A.S., etal. (2008) In LipL32, the major leptospiral lipoprotein, the C terminus is the primary immunogenic domain and mediates interaction with collagen IV and plasma fibronectin. Infect Immun 76: 2642-2650.
    • (2008) Infect Immun , vol.76 , pp. 2642-2650
    • Hauk, P.1    Macedo, F.2    Romero, E.C.3    Vasconcellos, S.A.4    Morais, Z.M.5    Barbosa, A.S.6
  • 28
    • 84860389021 scopus 로고    scopus 로고
    • Europe's neglected infections of poverty
    • Hotez, P.J., and Gurwith, M. (2011) Europe's neglected infections of poverty. Int J Infect Dis 15: e611-e619.
    • (2011) Int J Infect Dis , vol.15
    • Hotez, P.J.1    Gurwith, M.2
  • 29
    • 0033920740 scopus 로고    scopus 로고
    • Signaling and invasin-promoted uptake via integrin receptors
    • Isberg, R.R., Hamburger, Z., and Dersch, P. (2000) Signaling and invasin-promoted uptake via integrin receptors. Microbes Infect 2: 793-801.
    • (2000) Microbes Infect , vol.2 , pp. 793-801
    • Isberg, R.R.1    Hamburger, Z.2    Dersch, P.3
  • 30
    • 60549093565 scopus 로고    scopus 로고
    • Leptospira interrogans induces apoptosis in macrophages via caspase-8- and caspase-3-dependent pathways
    • Jin, D.D., Ojcius, D.M., Sun, D., Dong, H.Y., Luo, Y.H., Mao, Y.F., etal. (2009) Leptospira interrogans induces apoptosis in macrophages via caspase-8- and caspase-3-dependent pathways. Infect Immun 77: 799-809.
    • (2009) Infect Immun , vol.77 , pp. 799-809
    • Jin, D.D.1    Ojcius, D.M.2    Sun, D.3    Dong, H.Y.4    Luo, Y.H.5    Mao, Y.F.6
  • 32
    • 70349269503 scopus 로고    scopus 로고
    • Leptospira: the dawn of the molecular genetics era for an emerging zoonotic pathogen
    • Ko, A.I., Goarant, C., and Picardeau, M. (2009) Leptospira: the dawn of the molecular genetics era for an emerging zoonotic pathogen. Nat Rev Microbiol 7: 736-747.
    • (2009) Nat Rev Microbiol , vol.7 , pp. 736-747
    • Ko, A.I.1    Goarant, C.2    Picardeau, M.3
  • 33
    • 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., Hoffmann, I., Laran-Chich, M.P., Nassif, X., Couraud, P.O., and Bourdoulous, S. (2005) 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 118: 3805-3816.
    • (2005) J Cell Sci , vol.118 , pp. 3805-3816
    • Lambotin, M.1    Hoffmann, I.2    Laran-Chich, M.P.3    Nassif, X.4    Couraud, P.O.5    Bourdoulous, S.6
  • 34
    • 33644973069 scopus 로고    scopus 로고
    • Quantifying the specific binding between West Nile virus envelope domain III protein and the cellular receptor alphaVbeta3 integrin
    • Lee, J.W., Chu, J.J., and Ng, M.L. (2006) Quantifying the specific binding between West Nile virus envelope domain III protein and the cellular receptor alphaVbeta3 integrin. J Biol Chem 281: 1352-1360.
    • (2006) J Biol Chem , vol.281 , pp. 1352-1360
    • Lee, J.W.1    Chu, J.J.2    Ng, M.L.3
  • 35
  • 36
    • 36849009713 scopus 로고    scopus 로고
    • Comparison of invasion of fibroblasts and macrophages by high- and low-virulence Leptospira strains: colonization of the host-cell nucleus and induction of necrosis by the virulent strain
    • Li, L.W., Ojcius, D.M., and Yan, J. (2007) Comparison of invasion of fibroblasts and macrophages by high- and low-virulence Leptospira strains: colonization of the host-cell nucleus and induction of necrosis by the virulent strain. Arch Microbiol 188: 591-598.
    • (2007) Arch Microbiol , vol.188 , pp. 591-598
    • Li, L.W.1    Ojcius, D.M.2    Yan, J.3
  • 37
    • 77952357124 scopus 로고    scopus 로고
    • Replication or death: distinct fates of pathogenic Leptospira strain Lai within macrophages of human or mouse origin
    • Li, S.J., Ojcius, D.M., Liao, S.M., Li, L.W., Xue, F., Dong, H.Y., etal. (2010) Replication or death: distinct fates of pathogenic Leptospira strain Lai within macrophages of human or mouse origin. Innate Immun 16: 80-92.
    • (2010) Innate Immun , vol.16 , pp. 80-92
    • Li, S.J.1    Ojcius, D.M.2    Liao, S.M.3    Li, L.W.4    Xue, F.5    Dong, H.Y.6
  • 38
    • 67749102258 scopus 로고    scopus 로고
    • Repeated domains of Leptospira immunoglobulin-like proteins interact with elastin and tropoelastin
    • Lin, Y.P., Lee, D.W., McDonough, S.P., Nicholson, L.K., Sharma, Y., and Chang, Y.F. (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    Chang, Y.F.6
  • 39
    • 36149000178 scopus 로고    scopus 로고
    • Pathogenesis of leptospirosis: interaction of Leptospira interrogans with in vitro cultured mammalian cells
    • Liu, Y.Y., Zheng, W., Li, L.W., Mao, Y.F., and Yan, J. (2007) Pathogenesis of leptospirosis: interaction of Leptospira interrogans with in vitro cultured mammalian cells. Med Microbiol Immunol 196: 233-239.
    • (2007) Med Microbiol Immunol , vol.196 , pp. 233-239
    • Liu, Y.Y.1    Zheng, W.2    Li, L.W.3    Mao, Y.F.4    Yan, J.5
  • 40
    • 70649088857 scopus 로고    scopus 로고
    • Protein typing of major outer membrane lipoproteins from Chinese pathogenic Leptospira spp. and characterization of their immunogenicity
    • Luo, D.J., Xue, F., Ojcius, D.M., Zhao, J.F., Mao, Y.F., and Li, L.W. (2010) Protein typing of major outer membrane lipoproteins from Chinese pathogenic Leptospira spp. and characterization of their immunogenicity. Vaccine 28: 243-255.
    • (2010) Vaccine , vol.28 , pp. 243-255
    • Luo, D.J.1    Xue, F.2    Ojcius, D.M.3    Zhao, J.F.4    Mao, Y.F.5    Li, L.W.6
  • 43
    • 0031035320 scopus 로고    scopus 로고
    • Invasion of Vero cells and induction of apoptosis in macrophages by pathogenic Leptospira interrogans are correlated with virulence
    • Merien, F., Baranton, G., and Perolat, P. (1997) Invasion of Vero cells and induction of apoptosis in macrophages by pathogenic Leptospira interrogans are correlated with virulence. Infect Immun 65: 729-738.
    • (1997) Infect Immun , vol.65 , pp. 729-738
    • Merien, F.1    Baranton, G.2    Perolat, P.3
  • 44
    • 31944448737 scopus 로고    scopus 로고
    • Intracellular survival of Shigella
    • Ogawa, M., and Sasakawa, C. (2006) Intracellular survival of Shigella. Cell Microbiol 8: 177-184.
    • (2006) Cell Microbiol , vol.8 , pp. 177-184
    • Ogawa, M.1    Sasakawa, C.2
  • 46
    • 0036581160 scopus 로고    scopus 로고
    • Relative expression software tool (REST) for group-wise comparison and statistical analysis of relative expression results in real-time PCR
    • Pfaffl, M.W., Horgan, G.W., and Dempfle, L. (2002) Relative expression software tool (REST) for group-wise comparison and statistical analysis of relative expression results in real-time PCR. Nucleic Acids Res 30: e36.
    • (2002) Nucleic Acids Res , vol.30
    • Pfaffl, M.W.1    Horgan, G.W.2    Dempfle, L.3
  • 47
    • 0035050686 scopus 로고    scopus 로고
    • First evidence for gene replacement in Leptospira spp. inactivation of L. biflexa flaB results in non-motile mutants deficient in endoflagella
    • Picardeau, M., Brenot, A., and Saint, G.I. (2001) First evidence for gene replacement in Leptospira spp. inactivation of L. biflexa flaB results in non-motile mutants deficient in endoflagella. Mol Microbiol 40: 189-199.
    • (2001) Mol Microbiol , vol.40 , pp. 189-199
    • Picardeau, M.1    Brenot, A.2    Saint, G.I.3
  • 48
    • 78149244223 scopus 로고    scopus 로고
    • The OmpL37 surface-exposed protein is expressed by pathogenic Leptospira during infection and binds skin and vascular elastin
    • Pinne, M., Choy, H.A., and Haake, D.A. (2010) The OmpL37 surface-exposed protein is expressed by pathogenic Leptospira during infection and binds skin and vascular elastin. PLoS Negl Trop Dis 4: e815.
    • (2010) PLoS Negl Trop Dis , vol.4
    • Pinne, M.1    Choy, H.A.2    Haake, D.A.3
  • 49
    • 0033833451 scopus 로고    scopus 로고
    • Overview of the epidemiology, microbiology, and pathogenesis of Leptospira spp. in humans
    • Plank, R., and Dean, D. (2000) Overview of the epidemiology, microbiology, and pathogenesis of Leptospira spp. in humans. Microbes Infect 2: 1265-1276.
    • (2000) Microbes Infect , vol.2 , pp. 1265-1276
    • Plank, R.1    Dean, D.2
  • 50
    • 0037464546 scopus 로고    scopus 로고
    • Unique physiological and pathogenic features of Leptospira interrogans revealed by whole-genome sequencing
    • Ren, S.X., Fu, G., Jiang, X.G., Zeng, R., Miao, Y.G., Xu, H., etal. (2003) Unique physiological and pathogenic features of Leptospira interrogans revealed by whole-genome sequencing. Nature 422: 888-893.
    • (2003) Nature , vol.422 , pp. 888-893
    • Ren, S.X.1    Fu, G.2    Jiang, X.G.3    Zeng, R.4    Miao, Y.G.5    Xu, H.6
  • 52
    • 0030780833 scopus 로고    scopus 로고
    • Interaction of Yersinia enterocolitica with macrophages leads to macrophage cell death through apoptosis
    • Ruckdeschel, K., Roggenkamp, A., Lafont, V., Mangeat, P., Heesemann, J., and Rouot, B. (1997) Interaction of Yersinia enterocolitica with macrophages leads to macrophage cell death through apoptosis. Infect Immun 65: 4813-4821.
    • (1997) Infect Immun , vol.65 , pp. 4813-4821
    • Ruckdeschel, K.1    Roggenkamp, A.2    Lafont, V.3    Mangeat, P.4    Heesemann, J.5    Rouot, B.6
  • 53
    • 0029775681 scopus 로고    scopus 로고
    • RGD and other recognition sequences for integrins
    • Ruoslahti, E. (1996) RGD and other recognition sequences for integrins. Annu Rev Cell Dev Biol 12: 697-715.
    • (1996) Annu Rev Cell Dev Biol , vol.12 , pp. 697-715
    • Ruoslahti, E.1
  • 54
    • 0033819182 scopus 로고    scopus 로고
    • The LE1 bacteriophage replicates as a plasmid within Leptospira biflexa: construction of an L. biflexa-Escherichia coli shuttle vector
    • Saint Giron, I., Bourhy, P., Ottone, C., Picardeau, M., Yelton, D., Hendrix, R.W., etal. (2000) The LE1 bacteriophage replicates as a plasmid within Leptospira biflexa: construction of an L. biflexa-Escherichia coli shuttle vector. J Bacteriol 182: 5700-5705.
    • (2000) J Bacteriol , vol.182 , pp. 5700-5705
    • Saint Giron, I.1    Bourhy, P.2    Ottone, C.3    Picardeau, M.4    Yelton, D.5    Hendrix, R.W.6
  • 55
    • 67649771331 scopus 로고    scopus 로고
    • Molecular basis of the recognition of nephronectin by integrin alpha8beta1
    • Sato, Y., Uemura, T., Morimitsu, K., Sato, N.R., Manabe, R., Takagi, J., etal. (2009) Molecular basis of the recognition of nephronectin by integrin alpha8beta1. J Biol Chem 284: 14524-14536.
    • (2009) J Biol Chem , vol.284 , pp. 14524-14536
    • Sato, Y.1    Uemura, T.2    Morimitsu, K.3    Sato, N.R.4    Manabe, R.5    Takagi, J.6
  • 56
    • 70350007203 scopus 로고    scopus 로고
    • Leptospirosis research: fast, easy and reliable enumeration of mobile leptospires
    • Schreier, S., Triampo, W., Doungchawee, G., Triampo, D., and Chadsuthi, S. (2009) Leptospirosis research: fast, easy and reliable enumeration of mobile leptospires. Biol Res 42: 5-12.
    • (2009) Biol Res , vol.42 , pp. 5-12
    • Schreier, S.1    Triampo, W.2    Doungchawee, G.3    Triampo, D.4    Chadsuthi, S.5
  • 57
    • 38949205260 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis strains disrupted in mce3 and mce4 operons are attenuated in mice
    • Senaratne, R.H., Sidders, B., Sequeira, P., Saunders, G., Dunphy, K., Marjanovic, O., etal. (2008) Mycobacterium tuberculosis strains disrupted in mce3 and mce4 operons are attenuated in mice. J Med Microbiol 57: 164-170.
    • (2008) J Med Microbiol , vol.57 , pp. 164-170
    • Senaratne, R.H.1    Sidders, B.2    Sequeira, P.3    Saunders, G.4    Dunphy, K.5    Marjanovic, O.6
  • 58
    • 36048965750 scopus 로고    scopus 로고
    • The role of the activated macrophage in clearing Listeria monocytogenes infection
    • Shaughnessy, L.M., and Swanson, J.A. (2007) The role of the activated macrophage in clearing Listeria monocytogenes infection. Front Biosci 12: 2683-2692.
    • (2007) Front Biosci , vol.12 , pp. 2683-2692
    • Shaughnessy, L.M.1    Swanson, J.A.2
  • 59
    • 34748850660 scopus 로고    scopus 로고
    • Internalization by HeLa cells of latex beads coated with mammalian cell entry (Mce) proteins encoded by the mce3 operon of Mycobacterium tuberculosis
    • Sherief, E.S., Suhail, A., Abu, S.M., Raja, A.A., and Dimitrolos, K. (2007) Internalization by HeLa cells of latex beads coated with mammalian cell entry (Mce) proteins encoded by the mce3 operon of Mycobacterium tuberculosis. J Med Microbiol 56: 1145-1151.
    • (2007) J Med Microbiol , vol.56 , pp. 1145-1151
    • Sherief, E.S.1    Suhail, A.2    Abu, S.M.3    Raja, A.A.4    Dimitrolos, K.5
  • 60
    • 43149110212 scopus 로고    scopus 로고
    • Leptospira interrogans endostatin-like outer membrane proteins bind host fibronectin, laminin and regulators of complement
    • Stevenson, B., Choy, H.A., Pinne, M., Rotondi, M.L., Miller, M.C., Demoll, E., etal. (2007) Leptospira interrogans endostatin-like outer membrane proteins bind host fibronectin, laminin and regulators of complement. PLoS ONE 2: e1188.
    • (2007) PLoS ONE , vol.2
    • Stevenson, B.1    Choy, H.A.2    Pinne, M.3    Rotondi, M.L.4    Miller, M.C.5    Demoll, E.6
  • 61
    • 0033524449 scopus 로고    scopus 로고
    • A natural variant of the cysteine protease virulence factor of group A streptococcus with an arginine-glycine-aspartic acid (RGD) motif preferentially binds human integrins alphavbeta3 and alphaIIbbeta3
    • Stockbauer, K.E., Magoun, L., Liu, M., Burns, E.H., Gubba, S., Renish, S., etal. (1999) A natural variant of the cysteine protease virulence factor of group A streptococcus with an arginine-glycine-aspartic acid (RGD) motif preferentially binds human integrins alphavbeta3 and alphaIIbbeta3. Proc Natl Acad Sci USA 96: 242-247.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 242-247
    • Stockbauer, K.E.1    Magoun, L.2    Liu, M.3    Burns, E.H.4    Gubba, S.5    Renish, S.6
  • 62
    • 3042557983 scopus 로고    scopus 로고
    • Structural basis for ligand recognition by RGD (Arg-Gly-Asp) dependent integrins
    • Takagi, J. (2004) Structural basis for ligand recognition by RGD (Arg-Gly-Asp) dependent integrins. Biochem Soc Trans 32: 403-406.
    • (2004) Biochem Soc Trans , vol.32 , pp. 403-406
    • Takagi, J.1
  • 63
    • 80054112939 scopus 로고    scopus 로고
    • Characteristic features of intracellular pathogenic Leptospira in infected murine macrophages
    • Toma, C., Okura, N., Takayama, C., and Suzuki, T. (2011) Characteristic features of intracellular pathogenic Leptospira in infected murine macrophages. Cell Microbiol 13: 1783-1792.
    • (2011) Cell Microbiol , vol.13 , pp. 1783-1792
    • Toma, C.1    Okura, N.2    Takayama, C.3    Suzuki, T.4
  • 64
    • 0036216769 scopus 로고    scopus 로고
    • Phagocytosis of microbes: complexity in action
    • Underhill, D.M., and Ozinsky, A. (2002) Phagocytosis of microbes: complexity in action. Annu Rev Immunol 20: 825-852.
    • (2002) Annu Rev Immunol , vol.20 , pp. 825-852
    • Underhill, D.M.1    Ozinsky, A.2
  • 65
    • 77951239052 scopus 로고    scopus 로고
    • Leptospiral endostatin-like protein A (LenA) is a bacterial cell-surface receptor for human plasminogen
    • Verma, A., Brissette, C.A., Bowman, A.A., Shah, S.T., Zipfel, P.F., and Stevenson, B. (2010) Leptospiral endostatin-like protein A (LenA) 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    Stevenson, B.6
  • 66
    • 33644790664 scopus 로고    scopus 로고
    • Synthetic RGD-containing alpha-helical coiled coil peptides promote integrin-dependent cell adhesion
    • Villard, V., Kalyuzhniy, O., Riccio, O., Potekhin, S., Melnik, T.N., Kajava, A.V., etal. (2006) Synthetic RGD-containing alpha-helical coiled coil peptides promote integrin-dependent cell adhesion. J Pept Sci 12: 206-212.
    • (2006) J Pept Sci , vol.12 , pp. 206-212
    • Villard, V.1    Kalyuzhniy, O.2    Riccio, O.3    Potekhin, S.4    Melnik, T.N.5    Kajava, A.V.6
  • 67
    • 0021710445 scopus 로고
    • Role of specific antibody in interaction of leptospires with human monocytes and monocyte-derived macrophages
    • Wang, B., Sullivan, J.A., Sullivan, G.W., and Mandell, G.L. (1984) Role of specific antibody in interaction of leptospires with human monocytes and monocyte-derived macrophages. Infect Immun 46: 809-813.
    • (1984) Infect Immun , vol.46 , pp. 809-813
    • Wang, B.1    Sullivan, J.A.2    Sullivan, G.W.3    Mandell, G.L.4
  • 69
    • 0034775391 scopus 로고    scopus 로고
    • Yersinia enterocolitica invasin triggers phagocytosis via beta1 integrins, CDC42Hs and WASp in macrophages
    • Wiedemann, A., Linder, S., Grassl, G., Albert, M., Autenrieth, I., and Aepfelbacher, M. (2001) Yersinia enterocolitica invasin triggers phagocytosis via beta1 integrins, CDC42Hs and WASp in macrophages. Cell Microbiol 3: 693-702.
    • (2001) Cell Microbiol , vol.3 , pp. 693-702
    • Wiedemann, A.1    Linder, S.2    Grassl, G.3    Albert, M.4    Autenrieth, I.5    Aepfelbacher, M.6
  • 70
    • 2942637333 scopus 로고    scopus 로고
    • Integrin alpha v beta 6 is an RGD-dependent receptor for coxsackievirus A9
    • Williams, C.H., Kajander, T., Hyypia, T., Jackson, T., Sheppard, D., and Stanway, G. (2004) Integrin alpha v beta 6 is an RGD-dependent receptor for coxsackievirus A9. J Virol 78: 6967-6973.
    • (2004) J Virol , vol.78 , pp. 6967-6973
    • Williams, C.H.1    Kajander, T.2    Hyypia, T.3    Jackson, T.4    Sheppard, D.5    Stanway, G.6
  • 71
    • 78449242700 scopus 로고    scopus 로고
    • Transcriptional responses of Leptospira interrogans to host innate immunity: Significant changes in metabolism, oxygen tolerance, and outer membrane
    • Xue, F., Dong, H.Y., Wu, J.Y., Wu, Z.W., Hu, W.L., Sun, A.H., etal. (2010) Transcriptional responses of Leptospira interrogans to host innate immunity: Significant changes in metabolism, oxygen tolerance, and outer membrane. PLoS Negl Trop Dis 4: e857.
    • (2010) PLoS Negl Trop Dis , vol.4
    • Xue, F.1    Dong, H.Y.2    Wu, J.Y.3    Wu, Z.W.4    Hu, W.L.5    Sun, A.H.6


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