메뉴 건너뛰기




Volumn 203, Issue 10, 2006, Pages 2363-2375

A Leishmania amazonensis ZIP family iron transporter is essential for parasite replication within macrophage phagolysosomes

Author keywords

[No Author keywords available]

Indexed keywords

FERROPORTIN 1; MEMBRANE PROTEIN;

EID: 33749325014     PISSN: 00221007     EISSN: 00221007     Source Type: Journal    
DOI: 10.1084/jem.20060559     Document Type: Article
Times cited : (124)

References (56)
  • 1
    • 0033137082 scopus 로고    scopus 로고
    • The role of iron in protozoan and fungal infectious diseases
    • Weinberg, E.D. 1999. The role of iron in protozoan and fungal infectious diseases. J. Eukaryot. Microbiol. 46:231-238.
    • (1999) J. Eukaryot. Microbiol. , vol.46 , pp. 231-238
    • Weinberg, E.D.1
  • 3
    • 0034613681 scopus 로고    scopus 로고
    • Natural resistance to intracellular infections: Natural resistance-associated macrophage protein 1 (Nramp1) functions as a pH-dependent manganese transporter at the phagosomal membrane
    • Jabado, N., A. Jankowski, S. Dougaparsad, V. Picard, S. Grinstein, and P. Gros. 2000. Natural resistance to intracellular infections: natural resistance-associated macrophage protein 1 (Nramp1) functions as a pH-dependent manganese transporter at the phagosomal membrane. J. Exp. Med. 192:1237-1248.
    • (2000) J. Exp. Med. , vol.192 , pp. 1237-1248
    • Jabado, N.1    Jankowski, A.2    Dougaparsad, S.3    Picard, V.4    Grinstein, S.5    Gros, P.6
  • 4
    • 0035421993 scopus 로고    scopus 로고
    • Divalent-metal transport by NRAMP proteins at the interface of host-pathogen interactions
    • Forbes, J.R., and P. Gros. 2001. Divalent-metal transport by NRAMP proteins at the interface of host-pathogen interactions. Trends Microbiol. 9:397-403.
    • (2001) Trends Microbiol. , vol.9 , pp. 397-403
    • Forbes, J.R.1    Gros, P.2
  • 5
    • 0031455412 scopus 로고    scopus 로고
    • Cloning, characterization and overexpression of two iron superoxide dismutase cDNAs from Leishmania chagasi: Role in pathogenesis
    • Paramchuk, W.J., S.O. Ismail, A. Bhatia, and L. Gedamu. 1997. Cloning, characterization and overexpression of two iron superoxide dismutase cDNAs from Leishmania chagasi: role in pathogenesis. Mol. Biochem. Parasitol. 90:203-221.
    • (1997) Mol. Biochem. Parasitol. , vol.90 , pp. 203-221
    • Paramchuk, W.J.1    Ismail, S.O.2    Bhatia, A.3    Gedamu, L.4
  • 6
    • 0032171693 scopus 로고    scopus 로고
    • Iron uptake by parasitic protozoa
    • Wilson, M.E., and B.E. Britigan. 1998. Iron uptake by parasitic protozoa. Parasitol. Today. 14:348-353.
    • (1998) Parasitol. Today , vol.14 , pp. 348-353
    • Wilson, M.E.1    Britigan, B.E.2
  • 8
    • 0037184526 scopus 로고    scopus 로고
    • Mechanisms of cellular iron acquisition: Another iron in the fire
    • Kaplan, J. 2002. Mechanisms of cellular iron acquisition: another iron in the fire. Cell. 111:603-606.
    • (2002) Cell , vol.111 , pp. 603-606
    • Kaplan, J.1
  • 10
    • 0032477866 scopus 로고    scopus 로고
    • Nramp2 is mutated in the anemic Belgrade (b) rat: Evidence of a role for Nramp2 in endosomal iron transport
    • Fleming, M.D., M.A. Romano, M.A. Su, L.M. Garrick, M.D. Garrick, and N.C. Andrews. 1998. Nramp2 is mutated in the anemic Belgrade (b) rat: evidence of a role for Nramp2 in endosomal iron transport. Proc. Natl. Acad. Sci. USA. 95:1148-1153.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 1148-1153
    • Fleming, M.D.1    Romano, M.A.2    Su, M.A.3    Garrick, L.M.4    Garrick, M.D.5    Andrews, N.C.6
  • 11
    • 0027435537 scopus 로고
    • Iron uptake mechanisms of pathogenic bacteria
    • Wooldridge, K.G., and P.H. Williams. 1993. Iron uptake mechanisms of pathogenic bacteria. FEMS Microbiol. Rev. 12:325-348.
    • (1993) FEMS Microbiol. Rev. , vol.12 , pp. 325-348
    • Wooldridge, K.G.1    Williams, P.H.2
  • 12
    • 0028058934 scopus 로고
    • Acquisition of iron from transferrin and lactoferrin by the protozoan Leishmania chagasi
    • Wilson, M.E., R.W. Vorhies, K.A. Andersen, and B.E. Britigan. 1994. Acquisition of iron from transferrin and lactoferrin by the protozoan Leishmania chagasi. Infect. Immun. 62:3262-3269.
    • (1994) Infect. Immun. , vol.62 , pp. 3262-3269
    • Wilson, M.E.1    Vorhies, R.W.2    Andersen, K.A.3    Britigan, B.E.4
  • 13
    • 0028861990 scopus 로고
    • Transferrin-binding protein complex is the receptor for transferrin uptake in Trypanosoma brucei
    • Steverding, D., Y.D. Stierhof, H. Fuchs, R. Tauber, and P. Overath. 1995. Transferrin-binding protein complex is the receptor for transferrin uptake in Trypanosoma brucei. J. Cell Biol. 131:1173-1182.
    • (1995) J. Cell Biol. , vol.131 , pp. 1173-1182
    • Steverding, D.1    Stierhof, Y.D.2    Fuchs, H.3    Tauber, R.4    Overath, P.5
  • 14
    • 0031665621 scopus 로고    scopus 로고
    • Subverted transferrin trafficking in Leishmania-infected macrophages
    • Borges, V.M., M.A. Vannier-Santos, and W. de Souza. 1998. Subverted transferrin trafficking in Leishmania-infected macrophages. Parasitol. Res. 84:811-822.
    • (1998) Parasitol. Res. , vol.84 , pp. 811-822
    • Borges, V.M.1    Vannier-Santos, M.A.2    De Souza, W.3
  • 15
    • 0036525476 scopus 로고    scopus 로고
    • Leishmania chagasi: Uptake of iron bound to lactoferrin or transferrin requires an iron reductase
    • Wilson, M.E., T.S. Lewis, M.A. Miller, M.L. McCormick, and B.E. Britigan. 2002. Leishmania chagasi: uptake of iron bound to lactoferrin or transferrin requires an iron reductase. Exp. Parasitol. 100:196-207.
    • (2002) Exp. Parasitol. , vol.100 , pp. 196-207
    • Wilson, M.E.1    Lewis, T.S.2    Miller, M.A.3    McCormick, M.L.4    Britigan, B.E.5
  • 16
    • 0034192475 scopus 로고    scopus 로고
    • The ZIP family of metal transporters
    • Guerinot, M.L. 2000. The ZIP family of metal transporters. Biochim. Biophys. Acta. 1465:190-198.
    • (2000) Biochim. Biophys. Acta , vol.1465 , pp. 190-198
    • Guerinot, M.L.1
  • 17
    • 0034710975 scopus 로고    scopus 로고
    • Altered selectivity in an Arabidopsis metal transporter
    • Rogers, E.E., D.J. Eide, and M.L. Guerinot. 2000. Altered selectivity in an Arabidopsis metal transporter. Proc. Natl. Acad. Sci. USA. 97:12356-12360.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 12356-12360
    • Rogers, E.E.1    Eide, D.J.2    Guerinot, M.L.3
  • 19
    • 0035012676 scopus 로고    scopus 로고
    • Secretory and endocytic pathways converge in a dynamic endosomal system in a primitive protozoan
    • Ghedin, E., A. Debrabant, J.C. Engel, and D.M. Dwyer. 2001. Secretory and endocytic pathways converge in a dynamic endosomal system in a primitive protozoan. Traffic. 2:175-188.
    • (2001) Traffic , vol.2 , pp. 175-188
    • Ghedin, E.1    Debrabant, A.2    Engel, J.C.3    Dwyer, D.M.4
  • 20
    • 0035983847 scopus 로고    scopus 로고
    • Expression of the IRT1 metal transporter is controlled by metals at the levels of transcript and protein accumulation
    • Connolly, E.L., J.P. Fett, and M.L. Guerinot. 2002. Expression of the IRT1 metal transporter is controlled by metals at the levels of transcript and protein accumulation. Plant Cell. 14:1347-1357.
    • (2002) Plant Cell , vol.14 , pp. 1347-1357
    • Connolly, E.L.1    Fett, J.P.2    Guerinot, M.L.3
  • 21
    • 0028053806 scopus 로고
    • The FET4 gene encodes the low affinity Fe(II) transport protein of Saccharomyces cerevisiae
    • Dix, D.R., J.T. Bridgham, M.A. Broderius, C.A. Byersdorfer, and D.J. Eide. 1994. The FET4 gene encodes the low affinity Fe(II) transport protein of Saccharomyces cerevisiae. J. Biol. Chem. 269:26092-26099.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26092-26099
    • Dix, D.R.1    Bridgham, J.T.2    Broderius, M.A.3    Byersdorfer, C.A.4    Eide, D.J.5
  • 22
    • 0029891827 scopus 로고    scopus 로고
    • A novel iron-regulated metal transporter from plants identified by functional expression in yeast
    • Eide, D., M. Broderius, J. Fett, and M.L. Guerinot. 1996. A novel iron-regulated metal transporter from plants identified by functional expression in yeast. Proc. Natl. Acad. Sci. USA. 93:5624-5628.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 5624-5628
    • Eide, D.1    Broderius, M.2    Fett, J.3    Guerinot, M.L.4
  • 23
    • 0025903857 scopus 로고
    • Applications of high efficiency lithium acetate transformation of intact yeast cells using single-stranded nucleic acids as carrier
    • Gietz, R.D., and R.H. Schiestl. 1991. Applications of high efficiency lithium acetate transformation of intact yeast cells using single-stranded nucleic acids as carrier. Yeast. 7:253-263.
    • (1991) Yeast , vol.7 , pp. 253-263
    • Gietz, R.D.1    Schiestl, R.H.2
  • 24
    • 0036302227 scopus 로고    scopus 로고
    • Regulation of Saccharomyces cerevisiae FET4 by oxygen and iron
    • Jensen, L.T., and V.C. Culotta. 2002. Regulation of Saccharomyces cerevisiae FET4 by oxygen and iron. J. Mol. Biol. 318:251-260.
    • (2002) J. Mol. Biol. , vol.318 , pp. 251-260
    • Jensen, L.T.1    Culotta, V.C.2
  • 25
    • 19544385970 scopus 로고    scopus 로고
    • The 3A1-La monoclonal antibody reveals key features of Leishmania (L) amazonensis metacyclic promastigotes and inhibits procyclics attachment to the sand fly midgut
    • Pinto-da-Silva, L.H., P. Fampa, D.C. Soares, S.M. Oliveira, T. Souto-Padron, and E.M. Saraiva. 2005. The 3A1-La monoclonal antibody reveals key features of Leishmania (L) amazonensis metacyclic promastigotes and inhibits procyclics attachment to the sand fly midgut. Int. J. Parasitol. 35:757-764.
    • (2005) Int. J. Parasitol. , vol.35 , pp. 757-764
    • Pinto-da-Silva, L.H.1    Fampa, P.2    Soares, D.C.3    Oliveira, S.M.4    Souto-Padron, T.5    Saraiva, E.M.6
  • 27
    • 0033564656 scopus 로고    scopus 로고
    • Cellular and subcellular localization of the Nramp2 iron transporter in the intestinal brush border and regulation by dietary iron
    • Canonne-Hergaux, F., S. Gruenheid, P. Ponka, and P. Gros. 1999. Cellular and subcellular localization of the Nramp2 iron transporter in the intestinal brush border and regulation by dietary iron. Blood. 93:4406-4417.
    • (1999) Blood , vol.93 , pp. 4406-4417
    • Canonne-Hergaux, F.1    Gruenheid, S.2    Ponka, P.3    Gros, P.4
  • 28
    • 0343267840 scopus 로고    scopus 로고
    • Use of the green fluorescent protein as a marker in transfected Leishmania
    • Ha, D.S., J.K. Schwarz, S.J. Turco, and S.M. Beverley. 1996. Use of the green fluorescent protein as a marker in transfected Leishmania. Mol. Biochem. Parasitol. 77:57-64.
    • (1996) Mol. Biochem. Parasitol. , vol.77 , pp. 57-64
    • Ha, D.S.1    Schwarz, J.K.2    Turco, S.J.3    Beverley, S.M.4
  • 29
    • 0034532261 scopus 로고    scopus 로고
    • The immunologically protective P-4 antigen of Leishmania amastigotes. A developmentally regulated single strand-specific nuclease associated with the endoplasmic reticulum
    • Kar, S., L. Soong, M. Colmenares, K. Goldsmith-Pestana, and D. McMahon-Pratt. 2000. The immunologically protective P-4 antigen of Leishmania amastigotes. A developmentally regulated single strand-specific nuclease associated with the endoplasmic reticulum. J. Biol. Chem. 275:37789-37797.
    • (2000) J. Biol. Chem. , vol.275 , pp. 37789-37797
    • Kar, S.1    Soong, L.2    Colmenares, M.3    Goldsmith-Pestana, K.4    McMahon-Pratt, D.5
  • 30
    • 0031793544 scopus 로고    scopus 로고
    • The biogenesis and properties of the parasitophorous vacuoles that harbour Leishmania in murine macrophages
    • Antoine, J.C., E. Prina, T. Lang, and N. Courret. 1998. The biogenesis and properties of the parasitophorous vacuoles that harbour Leishmania in murine macrophages. Trends Microbiol. 6:392-401.
    • (1998) Trends Microbiol. , vol.6 , pp. 392-401
    • Antoine, J.C.1    Prina, E.2    Lang, T.3    Courret, N.4
  • 31
    • 0036591962 scopus 로고    scopus 로고
    • Biogenesis of Leishmania-harbouring parasitophorous vacuoles following phagocytosis of the metacyclic promastigote or amastigote stages of the parasites
    • Courret, N., C. Frehel, N. Gouhier, M. Pouchelet, E. Prina, P. Roux, and J.C. Antoine. 2002. Biogenesis of Leishmania-harbouring parasitophorous vacuoles following phagocytosis of the metacyclic promastigote or amastigote stages of the parasites. J. Cell Sci. 115:2303-2316.
    • (2002) J. Cell Sci. , vol.115 , pp. 2303-2316
    • Courret, N.1    Frehel, C.2    Gouhier, N.3    Pouchelet, M.4    Prina, E.5    Roux, P.6    Antoine, J.C.7
  • 32
    • 0029898541 scopus 로고    scopus 로고
    • Evidence from disruption of the lmcpb gene array of Leishmania mexicana that cysteine proteinases are virulence factors
    • Mottram, J.C., A.E. Souza, J.E. Hutchison, R. Carter, M.J. Frame, and G.H. Coombs. 1996. Evidence from disruption of the lmcpb gene array of Leishmania mexicana that cysteine proteinases are virulence factors. Proc. Natl. Acad. Sci. USA. 93:6008-6013.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 6008-6013
    • Mottram, J.C.1    Souza, A.E.2    Hutchison, J.E.3    Carter, R.4    Frame, M.J.5    Coombs, G.H.6
  • 33
    • 0032080107 scopus 로고    scopus 로고
    • A mitogen-activated protein (MAP) kinase homologue of Leishmania mexicana is essential for parasite survival in the infected host
    • Wiese, M. 1998. A mitogen-activated protein (MAP) kinase homologue of Leishmania mexicana is essential for parasite survival in the infected host. EMBO J. 17:2619-2628.
    • (1998) EMBO J. , vol.17 , pp. 2619-2628
    • Wiese, M.1
  • 34
    • 0034255342 scopus 로고    scopus 로고
    • Lipophosphoglycan is a virulence factor distinct from related glycoconjugates in the protozoan parasite Leishmania major
    • Spath, G.F., L. Epstein, B. Leader, S.M. Singer, H.A. Avila, S.J. Turco, and S.M. Beverley. 2000. Lipophosphoglycan is a virulence factor distinct from related glycoconjugates in the protozoan parasite Leishmania major. Proc. Natl. Acad. Sci. USA. 97:9258-9263.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 9258-9263
    • Spath, G.F.1    Epstein, L.2    Leader, B.3    Singer, S.M.4    Avila, H.A.5    Turco, S.J.6    Beverley, S.M.7
  • 35
    • 0036831673 scopus 로고    scopus 로고
    • The immunology of susceptibility and resistance to Leishmania major in mice
    • Sacks, D., and N. Noben-Trauth. 2002. The immunology of susceptibility and resistance to Leishmania major in mice. Nat. Rev. Immunol. 2:845-858.
    • (2002) Nat. Rev. Immunol. , vol.2 , pp. 845-858
    • Sacks, D.1    Noben-Trauth, N.2
  • 36
    • 0042322609 scopus 로고    scopus 로고
    • Persistence without pathology in phosphoglycan-deficient Leishmania major
    • Spath, G.F., L.F. Lye, H. Segawa, D.L. Sacks, S.J. Turco, and S.M. Beverley. 2003. Persistence without pathology in phosphoglycan-deficient Leishmania major. Science. 301:1241-1243.
    • (2003) Science , vol.301 , pp. 1241-1243
    • Spath, G.F.1    Lye, L.F.2    Segawa, H.3    Sacks, D.L.4    Turco, S.J.5    Beverley, S.M.6
  • 37
    • 4844223738 scopus 로고    scopus 로고
    • Does the Leishmania major paradigm of pathogenesis and protection hold for New World cutaneous leishmaniases or the visceral disease?
    • McMahon-Pratt, D., and J. Alexander. 2004. Does the Leishmania major paradigm of pathogenesis and protection hold for New World cutaneous leishmaniases or the visceral disease? Immunol. Rev. 201:206-224.
    • (2004) Immunol. Rev. , vol.201 , pp. 206-224
    • McMahon-Pratt, D.1    Alexander, J.2
  • 38
    • 0035983839 scopus 로고    scopus 로고
    • IRT1, an Arabidopsis transporter essential for iron uptake from the soil and for plant growth
    • Vert, G., N. Grotz, F. Dedaldechamp, F. Gaymard, M.L. Guerinot, J.F. Briat, and C. Curie. 2002. IRT1, an Arabidopsis transporter essential for iron uptake from the soil and for plant growth. Plant Cell. 14:1223-1233.
    • (2002) Plant Cell , vol.14 , pp. 1223-1233
    • Vert, G.1    Grotz, N.2    Dedaldechamp, F.3    Gaymard, F.4    Guerinot, M.L.5    Briat, J.F.6    Curie, C.7
  • 39
    • 0034680828 scopus 로고    scopus 로고
    • Nramp 2 (DCT1/DMT1) expressed at the plasma membrane transports iron and other divalent cations into a calcein-accessible cytoplasmic pool
    • Picard, V., G. Govoni, N. Jabado, and P. Gros. 2000. Nramp 2 (DCT1/DMT1) expressed at the plasma membrane transports iron and other divalent cations into a calcein-accessible cytoplasmic pool. J. Biol. Chem. 275:35738-35745.
    • (2000) J. Biol. Chem. , vol.275 , pp. 35738-35745
    • Picard, V.1    Govoni, G.2    Jabado, N.3    Gros, P.4
  • 40
    • 0031783138 scopus 로고    scopus 로고
    • Evidence for a link between iron metabolism and Nramp1 gene function in innate resistance against Mycobacterium avium
    • Gomes, M.S., and R. Appelberg. 1998. Evidence for a link between iron metabolism and Nramp1 gene function in innate resistance against Mycobacterium avium. Immunology. 95:165-168.
    • (1998) Immunology , vol.95 , pp. 165-168
    • Gomes, M.S.1    Appelberg, R.2
  • 41
    • 0033008432 scopus 로고    scopus 로고
    • Role of iron in Nramp1-mediated inhibition of mycobacterial growth
    • Zwilling, B.S., D.E. Kuhn, L. Wikoff, D. Brown, and W. Lafuse. 1999. Role of iron in Nramp1-mediated inhibition of mycobacterial growth. Infect. Immun. 67:1386-1392.
    • (1999) Infect. Immun. , vol.67 , pp. 1386-1392
    • Zwilling, B.S.1    Kuhn, D.E.2    Wikoff, L.3    Brown, D.4    Lafuse, W.5
  • 42
    • 0010412593 scopus 로고    scopus 로고
    • Differential iron transport into phagosomes isolated from the RAW264.7 macrophage cell lines transfected with Nramp1Gly169 or Nramp1Asp169
    • Kuhn, D.E., B.D. Baker, W.P. Lafuse, and B.S. Zwilling. 1999. Differential iron transport into phagosomes isolated from the RAW264.7 macrophage cell lines transfected with Nramp1Gly169 or Nramp1Asp169. J. Leukoc. Biol. 66:113-119.
    • (1999) J. Leukoc. Biol. , vol.66 , pp. 113-119
    • Kuhn, D.E.1    Baker, B.D.2    Lafuse, W.P.3    Zwilling, B.S.4
  • 44
    • 0029563799 scopus 로고
    • Glucose transport in amastigotes and promastigotes of Leishmania mexicana mexicana
    • Burchmore, R.J., and D.T. Hart. 1995. Glucose transport in amastigotes and promastigotes of Leishmania mexicana mexicana. Mol. Biochem. Parasitol. 74:77-86.
    • (1995) Mol. Biochem. Parasitol. , vol.74 , pp. 77-86
    • Burchmore, R.J.1    Hart, D.T.2
  • 45
    • 0344500607 scopus 로고    scopus 로고
    • Developmental regulation of proline transport in Leishmania donovani
    • Mazareb, S., Z.Y. Fu, and D. Zilberstein. 1999. Developmental regulation of proline transport in Leishmania donovani. Exp. Parasitol. 91:341-348.
    • (1999) Exp. Parasitol. , vol.91 , pp. 341-348
    • Mazareb, S.1    Fu, Z.Y.2    Zilberstein, D.3
  • 47
    • 0036853070 scopus 로고    scopus 로고
    • Evasion of innate immunity by parasitic protozoa
    • Sacks, D., and A. Sher. 2002. Evasion of innate immunity by parasitic protozoa. Nat. Immunol. 3:1041-1047.
    • (2002) Nat. Immunol. , vol.3 , pp. 1041-1047
    • Sacks, D.1    Sher, A.2
  • 48
    • 2542594797 scopus 로고    scopus 로고
    • Identification of a compensatory mutant (lpg2-REV) of Leishmania major able to survive as amastigotes within macrophages without LPG2-dependent glycoconjugates and its significance to virulence and immunization strategies
    • Spath, G.F., L.F. Lye, H. Segawa, S.J. Turco, and S.M. Beverley. 2004. Identification of a compensatory mutant (lpg2-REV) of Leishmania major able to survive as amastigotes within macrophages without LPG2-dependent glycoconjugates and its significance to virulence and immunization strategies. Infect. Immun. 72:3622-3627.
    • (2004) Infect. Immun. , vol.72 , pp. 3622-3627
    • Spath, G.F.1    Lye, L.F.2    Segawa, H.3    Turco, S.J.4    Beverley, S.M.5
  • 50
    • 0032983516 scopus 로고    scopus 로고
    • Presentation of the Leishmania antigen LACK by infected macrophages is dependent upon the virulence of the phagocytosed parasites
    • Courret, N., E. Prina, E. Mougneau, E.M. Saraiva, D.L. Sacks, N. Glaichenhaus, and J.C. Antoine. 1999. Presentation of the Leishmania antigen LACK by infected macrophages is dependent upon the virulence of the phagocytosed parasites. Eur. J. Immunol. 29:762-773.
    • (1999) Eur. J. Immunol. , vol.29 , pp. 762-773
    • Courret, N.1    Prina, E.2    Mougneau, E.3    Saraiva, E.M.4    Sacks, D.L.5    Glaichenhaus, N.6    Antoine, J.C.7
  • 51
    • 0028953840 scopus 로고
    • Yeast vectors for the controlled expression of heterologous proteins in different genetic backgrounds
    • Mumberg, D., R. Muller, and M. Funk. 1995. Yeast vectors for the controlled expression of heterologous proteins in different genetic backgrounds. Gene. 156:119-122.
    • (1995) Gene. , vol.156 , pp. 119-122
    • Mumberg, D.1    Muller, R.2    Funk, M.3
  • 54
    • 0028214438 scopus 로고
    • Induction of early-response genes KC and JE by mycobacterial lipoarabinomannans: Regulation of KC expression in murine macrophages by Lsh/Ity/Bcg (candidate Nramp)
    • Roach, T.I., D. Chatterjee, and J.M. Blackwell. 1994. Induction of early-response genes KC and JE by mycobacterial lipoarabinomannans: regulation of KC expression in murine macrophages by Lsh/Ity/Bcg (candidate Nramp). Infect. Immun. 62:1176-1184.
    • (1994) Infect. Immun. , vol.62 , pp. 1176-1184
    • Roach, T.I.1    Chatterjee, D.2    Blackwell, J.M.3
  • 55
    • 0035669096 scopus 로고    scopus 로고
    • A lipophosphoglycan-independent method for isolation of infective Leishmania metacyclic promastigotes by density gradient centrifugation
    • Spath, G.F., and S.M. Beverley. 2001. A lipophosphoglycan-independent method for isolation of infective Leishmania metacyclic promastigotes by density gradient centrifugation. Exp. Parasitol. 99:97-103.
    • (2001) Exp. Parasitol. , vol.99 , pp. 97-103
    • Spath, G.F.1    Beverley, S.M.2
  • 56
    • 23344449993 scopus 로고    scopus 로고
    • Conditions influencing the efficacy of vaccination with live organisms against Leishmania major infection
    • Tabbara, K.S., N.C. Peters, F. Afrin, S. Mendez, S. Bertholet, Y. Belkaid, and D.L. Sacks. 2005. Conditions influencing the efficacy of vaccination with live organisms against Leishmania major infection. Infect. Immun. 73:4714-4722.
    • (2005) Infect. Immun. , vol.73 , pp. 4714-4722
    • Tabbara, K.S.1    Peters, N.C.2    Afrin, F.3    Mendez, S.4    Bertholet, S.5    Belkaid, Y.6    Sacks, D.L.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.