메뉴 건너뛰기




Volumn 114, Issue 3 SPEC. ISS., 2005, Pages 256-265

Modulation of phagolysosome biogenesis by the lipophosphoglycan of Leishmania

Author keywords

Glycolipids; Leishmania; Macrophage; Phagocytosis; Virulence

Indexed keywords

F ACTIN; GLYCOCONJUGATE; GLYCOLIPID; LIPOPHOSPHOGLYCAN;

EID: 13844267783     PISSN: 15216616     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.clim.2004.07.018     Document Type: Article
Times cited : (53)

References (88)
  • 1
    • 0024390249 scopus 로고
    • Metacyclogenesis in Leishmania promastigotes
    • D.L. Sacks Metacyclogenesis in Leishmania promastigotes Exp. Parasitol. 69 1989 100 103
    • (1989) Exp. Parasitol. , vol.69 , pp. 100-103
    • Sacks, D.L.1
  • 2
    • 0017311847 scopus 로고
    • Multiplication of a human parasite (Leishmania donovani) in phagolysosomes of hamster macrophages in vitro
    • K.P. Chang, and D.M. Dwyer Multiplication of a human parasite (Leishmania donovani) in phagolysosomes of hamster macrophages in vitro Science 193 1976 678 680
    • (1976) Science , vol.193 , pp. 678-680
    • Chang, K.P.1    Dwyer, D.M.2
  • 3
    • 0016754011 scopus 로고
    • Fusion of host cell secondary lysosomes with the parasitophorous vacuoles of Leishmania mexicana-infected macrophages
    • J. Alexander, and K. Vickerman Fusion of host cell secondary lysosomes with the parasitophorous vacuoles of Leishmania mexicana-infected macrophages J. Protozool. 22 1975 502 508
    • (1975) J. Protozool. , vol.22 , pp. 502-508
    • Alexander, J.1    Vickerman, K.2
  • 4
    • 0026533657 scopus 로고
    • The interaction of Leishmania species with macrophages
    • J. Alexander, and D.G. Russell The interaction of Leishmania species with macrophages Adv. Parasitol. 31 1992 175 254
    • (1992) Adv. Parasitol. , vol.31 , pp. 175-254
    • Alexander, J.1    Russell, D.G.2
  • 5
    • 0032852260 scopus 로고    scopus 로고
    • Glycoconjugates in Leishmania infectivity
    • A. Descoteaux, and S.J. Turco Glycoconjugates in Leishmania infectivity Biochim. Biophys. Acta 1455 1999 341 352
    • (1999) Biochim. Biophys. Acta , vol.1455 , pp. 341-352
    • Descoteaux, A.1    Turco, S.J.2
  • 7
    • 0026746610 scopus 로고
    • The lipophosphoglycan of Leishmania parasites
    • S.J. Turco, and A. Descoteaux The lipophosphoglycan of Leishmania parasites Annu. Rev. Microbiol. 46 1992 65 94
    • (1992) Annu. Rev. Microbiol. , vol.46 , pp. 65-94
    • Turco, S.J.1    Descoteaux, A.2
  • 8
    • 0036063277 scopus 로고    scopus 로고
    • Functional aspects of the Leishmania donovani lipophosphoglycan during macrophage infection
    • A. Descoteaux, and S.J. Turco Functional aspects of the Leishmania donovani lipophosphoglycan during macrophage infection Microbes Infect. 4 2002 975 981
    • (2002) Microbes Infect. , vol.4 , pp. 975-981
    • Descoteaux, A.1    Turco, S.J.2
  • 9
    • 0035048929 scopus 로고    scopus 로고
    • Leishmania-sand fly interactions controlling species-specific vector competence
    • D.L. Sacks Leishmania-sand fly interactions controlling species-specific vector competence Cell. Microbiol. 3 2001 189 196
    • (2001) Cell. Microbiol. , vol.3 , pp. 189-196
    • Sacks, D.L.1
  • 10
    • 0023898688 scopus 로고
    • Complement binding by two developmental stages of Leishmania major promastigotes varying in expression of a surface lipophosphoglycan
    • S.M. Puentes, D.L. Sacks, R.P. da Silva, and K.A. Joiner Complement binding by two developmental stages of Leishmania major promastigotes varying in expression of a surface lipophosphoglycan J. Exp. Med. 167 1988 887 902
    • (1988) J. Exp. Med. , vol.167 , pp. 887-902
    • Puentes, S.M.1    Sacks, D.L.2    Da Silva, R.P.3    Joiner, K.A.4
  • 11
    • 0026057059 scopus 로고
    • Expression of a stage-specific lipophosphoglycan in Leishmania major amastigotes
    • S.J. Turco, and D.L. Sacks Expression of a stage-specific lipophosphoglycan in Leishmania major amastigotes Mol. Biochem. Parasitol. 45 1991 91 99
    • (1991) Mol. Biochem. Parasitol. , vol.45 , pp. 91-99
    • Turco, S.J.1    Sacks, D.L.2
  • 12
    • 0027312698 scopus 로고
    • The structure of Leishmania major amastigote lipophosphoglycan
    • S.F. Moody, E. Handman, M.J. McConville, and A. Bacic The structure of Leishmania major amastigote lipophosphoglycan J. Biol. Chem. 268 1993 18457 18466
    • (1993) J. Biol. Chem. , vol.268 , pp. 18457-18466
    • Moody, S.F.1    Handman, E.2    McConville, M.J.3    Bacic, A.4
  • 14
    • 0027971162 scopus 로고
    • O- and N-glycosylation of the Leishmania mexicana-secreted acid phosphatase. Characterization of a new class of phosphoserine-linked glycans
    • T. Ilg, P. Overath, M.A. Ferguson, T. Rutherford, D.G. Campbell, and M.J. McConville O- and N-glycosylation of the Leishmania mexicana-secreted acid phosphatase. Characterization of a new class of phosphoserine-linked glycans J. Biol. Chem. 269 1994 24073 24081
    • (1994) J. Biol. Chem. , vol.269 , pp. 24073-24081
    • Ilg, T.1    Overath, P.2    Ferguson, M.A.3    Rutherford, T.4    Campbell, D.G.5    McConville, M.J.6
  • 15
    • 0032577451 scopus 로고    scopus 로고
    • Stage-specific proteophosphoglycan from Leishmania mexicana amastigotes. Structural characterization of novel mono-, di-, and triphosphorylated phosphodiester-linked oligosaccharides
    • T. Ilg, D. Craik, G. Currie, G. Multhaup, and A. Bacic Stage-specific proteophosphoglycan from Leishmania mexicana amastigotes. Structural characterization of novel mono-, di-, and triphosphorylated phosphodiester- linked oligosaccharides J. Biol. Chem. 273 1998 13509 13523
    • (1998) J. Biol. Chem. , vol.273 , pp. 13509-13523
    • Ilg, T.1    Craik, D.2    Currie, G.3    Multhaup, G.4    Bacic, A.5
  • 16
    • 0033615693 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel repeat-containing Leishmania major gene, ppg1, that encodes a membrane-associated form of proteophosphoglycan with a putative glycosylphosphatidylinositol anchor
    • T. Ilg, J. Montgomery, Y.D. Stierhof, and E. Handman Molecular cloning and characterization of a novel repeat-containing Leishmania major gene, ppg1, that encodes a membrane-associated form of proteophosphoglycan with a putative glycosylphosphatidylinositol anchor J. Biol. Chem. 274 1999 31410 31420
    • (1999) J. Biol. Chem. , vol.274 , pp. 31410-31420
    • Ilg, T.1    Montgomery, J.2    Stierhof, Y.D.3    Handman, E.4
  • 17
    • 0027257177 scopus 로고
    • The structure, biosynthesis and function of glycosylated phosphatidylinositols in the parasitic protozoa and higher eukaryotes
    • M.J. McConville, and M.A. Ferguson The structure, biosynthesis and function of glycosylated phosphatidylinositols in the parasitic protozoa and higher eukaryotes Biochem. J. 294 1993 305 324
    • (1993) Biochem. J. , vol.294 , pp. 305-324
    • McConville, M.J.1    Ferguson, M.A.2
  • 18
    • 0027268692 scopus 로고
    • The glycoinositol phospholipids of Leishmania mexicana promastigotes. Evidence for the presence of three distinct pathways of glycolipid biosynthesis
    • M.J. McConville, T.A. Collidge, M.A. Ferguson, and P. Schneider The glycoinositol phospholipids of Leishmania mexicana promastigotes. Evidence for the presence of three distinct pathways of glycolipid biosynthesis J. Biol. Chem. 268 1993 15595 15604
    • (1993) J. Biol. Chem. , vol.268 , pp. 15595-15604
    • McConville, M.J.1    Collidge, T.A.2    Ferguson, M.A.3    Schneider, P.4
  • 19
    • 0034776373 scopus 로고    scopus 로고
    • Molecular aspects of parasite-vector and vector-host interactions in leishmaniasis
    • D. Sacks, and S. Kamhawi Molecular aspects of parasite-vector and vector-host interactions in leishmaniasis Annu. Rev. Microbiol. 55 2001 453 483
    • (2001) Annu. Rev. Microbiol. , vol.55 , pp. 453-483
    • Sacks, D.1    Kamhawi, S.2
  • 20
    • 0022413168 scopus 로고
    • The mouse macrophage receptor for C3bi (CR3) is a major mechanism in the phagocytosis of Leishmania promastigotes
    • D.M. Mosser, and P.J. Edelson The mouse macrophage receptor for C3bi (CR3) is a major mechanism in the phagocytosis of Leishmania promastigotes J. Immunol. 135 1985 2785 2789
    • (1985) J. Immunol. , vol.135 , pp. 2785-2789
    • Mosser, D.M.1    Edelson, P.J.2
  • 21
    • 0043180475 scopus 로고    scopus 로고
    • The role(s) of lipophosphoglycan (LPG) in the establishment of Leishmania major infections in mammalian hosts
    • G.F. Spath, L.A. Garraway, S.J. Turco, and S.M. Beverley The role(s) of lipophosphoglycan (LPG) in the establishment of Leishmania major infections in mammalian hosts Proc. Natl Acad. Sci. U. S. A. 100 2003 9536 9541
    • (2003) Proc. Natl Acad. Sci. U. S. A. , vol.100 , pp. 9536-9541
    • Spath, G.F.1    Garraway, L.A.2    Turco, S.J.3    Beverley, S.M.4
  • 22
    • 0028121975 scopus 로고
    • Recognition of the major cell surface glycoconjugates of Leishmania parasites by the human serum mannan-binding protein
    • P.J. Green, T. Feizi, M.S. Stoll, S. Thiel, A. Prescott, and M.J. McConville Recognition of the major cell surface glycoconjugates of Leishmania parasites by the human serum mannan-binding protein Mol. Biochem. Parasitol. 66 1994 319 328
    • (1994) Mol. Biochem. Parasitol. , vol.66 , pp. 319-328
    • Green, P.J.1    Feizi, T.2    Stoll, M.S.3    Thiel, S.4    Prescott, A.5    McConville, M.J.6
  • 23
    • 0029931163 scopus 로고    scopus 로고
    • C-reactive protein binds to a novel ligand on Leishmania donovani and increases uptake into human macrophages
    • F.J. Culley, R.A. Harris, P.M. Kaye, K.P. McAdam, and J.G. Raynes C-reactive protein binds to a novel ligand on Leishmania donovani and increases uptake into human macrophages J. Immunol. 156 1996 4691 4696
    • (1996) J. Immunol. , vol.156 , pp. 4691-4696
    • Culley, F.J.1    Harris, R.A.2    Kaye, P.M.3    McAdam, K.P.4    Raynes, J.G.5
  • 24
    • 0035003815 scopus 로고    scopus 로고
    • Is lipophosphoglycan a virulence factor? a surprising diversity between Leishmania species
    • S.J. Turco, G.F. Spath, and S.M. Beverley Is lipophosphoglycan a virulence factor? A surprising diversity between Leishmania species Trends Parasitol. 17 2001 223 226
    • (2001) Trends Parasitol. , vol.17 , pp. 223-226
    • Turco, S.J.1    Spath, G.F.2    Beverley, S.M.3
  • 25
    • 0034595204 scopus 로고    scopus 로고
    • Lipophosphoglycan is not required for infection of macrophages or mice by Leishmania mexicana
    • T. Ilg Lipophosphoglycan is not required for infection of macrophages or mice by Leishmania mexicana EMBO J. 19 2000 1953 1962
    • (2000) EMBO J. , vol.19 , pp. 1953-1962
    • Ilg, T.1
  • 27
    • 0042322609 scopus 로고    scopus 로고
    • Persistence without pathology in phosphoglycan-deficient Leishmania major
    • G.F. Spath, L.F. Lye, H. Segawa, D.L. Sacks, S.J. Turco, and S.M. Beverley Persistence without pathology in phosphoglycan-deficient Leishmania major Science 301 2003 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
  • 28
    • 0025215801 scopus 로고
    • Requirement of lipophosphoglycan for intracellular survival of Leishmania donovani within human monocytes
    • T.B. McNeely, and S.J. Turco Requirement of lipophosphoglycan for intracellular survival of Leishmania donovani within human monocytes J. Immunol. 144 1990 2745 2750
    • (1990) J. Immunol. , vol.144 , pp. 2745-2750
    • McNeely, T.B.1    Turco, S.J.2
  • 29
    • 0035895960 scopus 로고    scopus 로고
    • Phosphoglycan repeat-deficient Leishmania mexicana parasites remain infectious to macrophages and mice
    • T. Ilg, M. Demar, and D. Harbecke Phosphoglycan repeat-deficient Leishmania mexicana parasites remain infectious to macrophages and mice J. Biol. Chem. 276 2001 4988 4997
    • (2001) J. Biol. Chem. , vol.276 , pp. 4988-4997
    • Ilg, T.1    Demar, M.2    Harbecke, D.3
  • 30
    • 0033046220 scopus 로고    scopus 로고
    • Mechanisms of phagocytosis in macrophages
    • A. Aderem, and D.M. Underhill Mechanisms of phagocytosis in macrophages Annu. Rev. Immunol. 17 1999 593 623
    • (1999) Annu. Rev. Immunol. , vol.17 , pp. 593-623
    • Aderem, A.1    Underhill, D.M.2
  • 32
    • 0033559901 scopus 로고    scopus 로고
    • Phagosomes are fully competent antigen-processing organelles that mediate the formation of peptide:class II MHC complexes
    • L. Ramachandra, R. Song, and C.V. Harding Phagosomes are fully competent antigen-processing organelles that mediate the formation of peptide:class II MHC complexes J. Immunol. 162 1999 3263 3272
    • (1999) J. Immunol. , vol.162 , pp. 3263-3272
    • Ramachandra, L.1    Song, R.2    Harding, C.V.3
  • 34
    • 0027672713 scopus 로고
    • Leishmania-macrophage interactions: Multiple receptors, multiple ligands and diverse cellular responses
    • D.M. Mosser, and L.A. Rosenthal Leishmania-macrophage interactions: multiple receptors, multiple ligands and diverse cellular responses Semin. Cell Biol. 4 1993 315 322
    • (1993) Semin. Cell Biol. , vol.4 , pp. 315-322
    • Mosser, D.M.1    Rosenthal, L.A.2
  • 35
    • 0026673841 scopus 로고
    • Inhibition of macrophage protein kinase C-mediated protein phosphorylation by Leishmania donovani lipophosphoglycan
    • A. Descoteaux, G. Matlashewski, and S.J. Turco Inhibition of macrophage protein kinase C-mediated protein phosphorylation by Leishmania donovani lipophosphoglycan J. Immunol. 149 1992 3008 3015
    • (1992) J. Immunol. , vol.149 , pp. 3008-3015
    • Descoteaux, A.1    Matlashewski, G.2    Turco, S.J.3
  • 36
    • 0021080912 scopus 로고
    • Receptors for C3b and C3bi promote phagocytosis but not the release of toxic oxygen from human phagocytes
    • S.D. Wright, and S.C. Silverstein Receptors for C3b and C3bi promote phagocytosis but not the release of toxic oxygen from human phagocytes J. Exp. Med. 158 1983 2016 2023
    • (1983) J. Exp. Med. , vol.158 , pp. 2016-2023
    • Wright, S.D.1    Silverstein, S.C.2
  • 38
    • 0033847256 scopus 로고    scopus 로고
    • Leishmania donovani promastigotes evade the activation of mitogen-activated protein kinases p38, c-Jun N-terminal kinase, and extracellular signal-regulated kinase-1/2 during infection of naive macrophages
    • C. Privé, and A. Descoteaux Leishmania donovani promastigotes evade the activation of mitogen-activated protein kinases p38, c-Jun N-terminal kinase, and extracellular signal-regulated kinase-1/2 during infection of naive macrophages Eur. J. Immunol. 30 2000 2235 2244
    • (2000) Eur. J. Immunol. , vol.30 , pp. 2235-2244
    • Privé, C.1    Descoteaux, A.2
  • 39
    • 0028106942 scopus 로고
    • Altered cell signaling and mononuclear phagocyte deactivation during intracellular infection
    • N.E. Reiner Altered cell signaling and mononuclear phagocyte deactivation during intracellular infection Immunol. Today 15 1994 374 381
    • (1994) Immunol. Today , vol.15 , pp. 374-381
    • Reiner, N.E.1
  • 40
    • 0036853070 scopus 로고    scopus 로고
    • Evasion of innate immunity by parasitic protozoa
    • D. Sacks, and A. Sher Evasion of innate immunity by parasitic protozoa Nat. Immunol. 3 2002 1041 1047
    • (2002) Nat. Immunol. , vol.3 , pp. 1041-1047
    • Sacks, D.1    Sher, A.2
  • 41
    • 0027494552 scopus 로고
    • The lipophosphoglycan of Leishmania and macrophage protein kinase C
    • A. Descoteaux, and S.J. Turco The lipophosphoglycan of Leishmania and macrophage protein kinase C Parasitol. Today 9 1993 468 471
    • (1993) Parasitol. Today , vol.9 , pp. 468-471
    • Descoteaux, A.1    Turco, S.J.2
  • 42
    • 0033840213 scopus 로고    scopus 로고
    • Exploitation of host cell signaling machinery: Activation of macrophage phosphotyrosine phosphatases as a novel mechanism of molecular microbial pathogenesis
    • D. Nandan, K.L. Knutson, R. Lo, and N.E. Reiner Exploitation of host cell signaling machinery: activation of macrophage phosphotyrosine phosphatases as a novel mechanism of molecular microbial pathogenesis J. Leukoc. Biol. 67 2000 464 470
    • (2000) J. Leukoc. Biol. , vol.67 , pp. 464-470
    • Nandan, D.1    Knutson, K.L.2    Lo, R.3    Reiner, N.E.4
  • 43
    • 0023667646 scopus 로고
    • Inhibition of protein kinase C activity by the Leishmania donovani lipophosphoglycan
    • T.B. McNeely, and S.J. Turco Inhibition of protein kinase C activity by the Leishmania donovani lipophosphoglycan Biochem. Biophys. Res. Commun. 148 1987 653 657
    • (1987) Biochem. Biophys. Res. Commun. , vol.148 , pp. 653-657
    • McNeely, T.B.1    Turco, S.J.2
  • 44
    • 0024512492 scopus 로고
    • Inhibitory effects on protein kinase C activity by lipophosphoglycan fragments and glycosylphosphatidylinositol antigens of the protozoan parasite Leishmania
    • T.B. McNeely, G. Rosen, M.V. Londner, and S.J. Turco Inhibitory effects on protein kinase C activity by lipophosphoglycan fragments and glycosylphosphatidylinositol antigens of the protozoan parasite Leishmania Biochem. J. 259 1989 601 604
    • (1989) Biochem. J. , vol.259 , pp. 601-604
    • McNeely, T.B.1    Rosen, G.2    Londner, M.V.3    Turco, S.J.4
  • 45
    • 0025667811 scopus 로고
    • Effect of glycolipids of Leishmania parasites on human monocyte activity. Inhibition by lipophosphoglycan
    • S. Frankenburg, V. Leibovici, N. Mansbach, S.J. Turco, and G. Rosen Effect of glycolipids of Leishmania parasites on human monocyte activity. Inhibition by lipophosphoglycan J. Immunol. 145 1990 4284 4289
    • (1990) J. Immunol. , vol.145 , pp. 4284-4289
    • Frankenburg, S.1    Leibovici, V.2    Mansbach, N.3    Turco, S.J.4    Rosen, G.5
  • 46
    • 0025849761 scopus 로고
    • Leishmania donovani lipophosphoglycan selectively inhibits signal transduction in macrophages
    • A. Descoteaux, S.J. Turco, D.L. Sacks, and G. Matlashewski Leishmania donovani lipophosphoglycan selectively inhibits signal transduction in macrophages J. Immunol. 146 1991 2747 2753
    • (1991) J. Immunol. , vol.146 , pp. 2747-2753
    • Descoteaux, A.1    Turco, S.J.2    Sacks, D.L.3    Matlashewski, G.4
  • 47
    • 0029966229 scopus 로고    scopus 로고
    • Transbilayer inhibition of protein kinase C by the lipophosphoglycan from Leishmania donovani
    • J.R. Giorgione, S.J. Turco, and R.M. Epand Transbilayer inhibition of protein kinase C by the lipophosphoglycan from Leishmania donovani Proc. Natl Acad. Sci. U. S. A. 93 1996 11634 11639
    • (1996) Proc. Natl Acad. Sci. U. S. A. , vol.93 , pp. 11634-11639
    • Giorgione, J.R.1    Turco, S.J.2    Epand, R.M.3
  • 48
    • 0035067475 scopus 로고    scopus 로고
    • Phagocytosis and the actin cytoskeleton
    • R.C. May, and L.M. Machesky Phagocytosis and the actin cytoskeleton J. Cell Sci. 114 2001 1061 1077
    • (2001) J. Cell Sci. , vol.114 , pp. 1061-1077
    • May, R.C.1    MacHesky, L.M.2
  • 50
    • 0032753490 scopus 로고    scopus 로고
    • Modular components of phagocytosis
    • S. Greenberg Modular components of phagocytosis J. Leukoc. Biol. 66 1999 712 717
    • (1999) J. Leukoc. Biol. , vol.66 , pp. 712-717
    • Greenberg, S.1
  • 52
    • 0033555931 scopus 로고    scopus 로고
    • A requirement for phosphatidylinositol 3-kinase in pseudopod extension
    • D. Cox, C.C. Tseng, G. Bjekic, and S. Greenberg A requirement for phosphatidylinositol 3-kinase in pseudopod extension J. Biol. Chem. 274 1999 1240 1247
    • (1999) J. Biol. Chem. , vol.274 , pp. 1240-1247
    • Cox, D.1    Tseng, C.C.2    Bjekic, G.3    Greenberg, S.4
  • 53
    • 0036112263 scopus 로고    scopus 로고
    • A microbial strategy to multiply in macrophages: The pregnant pause
    • M.S. Swanson, E. Fernandez-Moreira, and E. Fernandez-Moreia A microbial strategy to multiply in macrophages: the pregnant pause Traffic 3 2002 170 177
    • (2002) Traffic , vol.3 , pp. 170-177
    • Swanson, M.S.1    Fernandez-Moreira, E.2    Fernandez-Moreia, E.3
  • 55
    • 0029162389 scopus 로고
    • A role for MARCKS, the alpha isozyme of protein kinase C and myosin I in zymosan phagocytosis by macrophages
    • L.H. Allen, and A. Aderem A role for MARCKS, the alpha isozyme of protein kinase C and myosin I in zymosan phagocytosis by macrophages J. Exp. Med. 182 1995 829 840
    • (1995) J. Exp. Med. , vol.182 , pp. 829-840
    • Allen, L.H.1    Aderem, A.2
  • 56
    • 0033756894 scopus 로고    scopus 로고
    • Rab5 regulates the kiss and run fusion between phagosomes and endosomes and the acquisition of phagosome leishmanicidal properties in RAW 264.7 macrophages
    • S. Duclos, R. Diez, J. Garin, B. Papadopoulou, A. Descoteaux, H. Stenmark, and M. Desjardins Rab5 regulates the kiss and run fusion between phagosomes and endosomes and the acquisition of phagosome leishmanicidal properties in RAW 264.7 macrophages J. Cell Sci. 113 2000 3531 3541
    • (2000) J. Cell Sci. , vol.113 , pp. 3531-3541
    • Duclos, S.1    Diez, R.2    Garin, J.3    Papadopoulou, B.4    Descoteaux, A.5    Stenmark, H.6    Desjardins, M.7
  • 58
    • 0028328732 scopus 로고
    • Biogenesis of phagolysosomes proceeds through a sequential series of interactions with the endocytic apparatus
    • M. Desjardins, L.A. Huber, R.G. Parton, and G. Griffiths Biogenesis of phagolysosomes proceeds through a sequential series of interactions with the endocytic apparatus J. Cell Biol. 124 1994 677 688
    • (1994) J. Cell Biol. , vol.124 , pp. 677-688
    • Desjardins, M.1    Huber, L.A.2    Parton, R.G.3    Griffiths, G.4
  • 59
    • 0028958289 scopus 로고
    • Biogenesis of phagolysosomes: The kiss and run hypothesis
    • M. Desjardins Biogenesis of phagolysosomes: the kiss and run hypothesis Trends Cell Biol. 5 1995 183 186
    • (1995) Trends Cell Biol. , vol.5 , pp. 183-186
    • Desjardins, M.1
  • 60
    • 0031005660 scopus 로고    scopus 로고
    • Inhibition of phagolysosomal biogenesis by the Leishmania lipophosphoglycan
    • M. Desjardins, and A. Descoteaux Inhibition of phagolysosomal biogenesis by the Leishmania lipophosphoglycan J. Exp. Med. 185 1997 2061 2068
    • (1997) J. Exp. Med. , vol.185 , pp. 2061-2068
    • Desjardins, M.1    Descoteaux, A.2
  • 61
    • 0033157106 scopus 로고    scopus 로고
    • Impaired recruitment of the small GTPase rab7 correlates with the inhibition of phagosome maturation by Leishmania donovani promastigotes
    • S. Scianimanico, M. Desrosiers, J.-F. Dermine, S. Méresse, A. Descoteaux, and M. Desjardins Impaired recruitment of the small GTPase rab7 correlates with the inhibition of phagosome maturation by Leishmania donovani promastigotes Cell. Microbiol. 1 1999 19 32
    • (1999) Cell. Microbiol. , vol.1 , pp. 19-32
    • Scianimanico, S.1    Desrosiers, M.2    Dermine, J.-F.3    Méresse, S.4    Descoteaux, A.5    Desjardins, M.6
  • 62
    • 0034935414 scopus 로고    scopus 로고
    • Leishmania donovani lipophosphoglycan causes periphagosomal actin accumulation: Correlation with impaired translocation of PKCa and defective phagosome maturation
    • Å. Holm, K. Tejle, K.E. Magnusson, A. Descoteaux, and B. Rasmusson Leishmania donovani lipophosphoglycan causes periphagosomal actin accumulation: correlation with impaired translocation of PKCa and defective phagosome maturation Cell. Microbiol. 3 2001 439 447
    • (2001) Cell. Microbiol. , vol.3 , pp. 439-447
    • Holm, Å.1    Tejle, K.2    Magnusson, K.E.3    Descoteaux, A.4    Rasmusson, B.5
  • 63
    • 0025066836 scopus 로고
    • Expression of a repeating phosphorylated disaccharide lipophosphoglycan epitope on the surface of macrophages infected with Leishmania donovani
    • D.L. Tolson, S.J. Turco, and T.W. Pearson Expression of a repeating phosphorylated disaccharide lipophosphoglycan epitope on the surface of macrophages infected with Leishmania donovani Infect. Immun. 58 1990 3500 3507
    • (1990) Infect. Immun. , vol.58 , pp. 3500-3507
    • Tolson, D.L.1    Turco, S.J.2    Pearson, T.W.3
  • 64
    • 0028921104 scopus 로고
    • Potent inhibition of viral fusion by the lipophosphoglycan of Leishmania donovani
    • L. Miao, A. Stafford, S. Nir, S.J. Turco, T.D. Flanagan, and R.M. Epand Potent inhibition of viral fusion by the lipophosphoglycan of Leishmania donovani Biochemistry 34 1995 4676 4683
    • (1995) Biochemistry , vol.34 , pp. 4676-4683
    • Miao, L.1    Stafford, A.2    Nir, S.3    Turco, S.J.4    Flanagan, T.D.5    Epand, R.M.6
  • 65
    • 0032421354 scopus 로고    scopus 로고
    • Functions of lipid rafts in biological membranes
    • D.A. Brown, and E. London Functions of lipid rafts in biological membranes Annu. Rev. Cell Dev. Biol. 14 1998 111 136
    • (1998) Annu. Rev. Cell Dev. Biol. , vol.14 , pp. 111-136
    • Brown, D.A.1    London, E.2
  • 66
    • 0034676288 scopus 로고    scopus 로고
    • Microbial pathogenesis: Lipid rafts as pathogen portals
    • C.M. Rosenberger, J.H. Brumell, and B.B. Finlay Microbial pathogenesis: lipid rafts as pathogen portals Curr. Biol. 10 2000 R823 R825
    • (2000) Curr. Biol. , vol.10
    • Rosenberger, C.M.1    Brumell, J.H.2    Finlay, B.B.3
  • 68
    • 0036591962 scopus 로고    scopus 로고
    • Biogenesis of Leishmania-harbouring parasitophorous vacuoles following phagocytosis of the metacyclic promastigote or amastigote stages of the parasites
    • N. Courret, C. Frehel, N. Gouhier, M. Pouchelet, E. Prina, P. Roux, and J.C. Antoine Biogenesis of Leishmania-harbouring parasitophorous vacuoles following phagocytosis of the metacyclic promastigote or amastigote stages of the parasites J. Cell Sci. 115 2002 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
  • 69
    • 0031793544 scopus 로고    scopus 로고
    • The biogenesis and properties of the parasitophorous vacuoles that harbour Leishmania in murine macrophages
    • J.C. Antoine, E. Prina, T. Lang, and N. Courret The biogenesis and properties of the parasitophorous vacuoles that harbour Leishmania in murine macrophages Trends Microbiol. 6 1998 392 401
    • (1998) Trends Microbiol. , vol.6 , pp. 392-401
    • Antoine, J.C.1    Prina, E.2    Lang, T.3    Courret, N.4
  • 70
    • 0034085602 scopus 로고    scopus 로고
    • Leishmania promastigotes require lipophosphoglycan to actively modulate the fusion properties of phagosomes at an early step of phagocytosis
    • J.-F. Dermine, S. Scianimanico, C. Privé, A. Descoteaux, and M. Desjardins Leishmania promastigotes require lipophosphoglycan to actively modulate the fusion properties of phagosomes at an early step of phagocytosis Cell. Microbiol. 2 2000 115 126
    • (2000) Cell. Microbiol. , vol.2 , pp. 115-126
    • Dermine, J.-F.1    Scianimanico, S.2    Privé, C.3    Descoteaux, A.4    Desjardins, M.5
  • 71
    • 0033553440 scopus 로고    scopus 로고
    • A coat protein on phagosomes involved in the intracellular survival of mycobacteria
    • G. Ferrari, H. Langen, M. Naito, and J. Pieters A coat protein on phagosomes involved in the intracellular survival of mycobacteria Cell 97 1999 435 447
    • (1999) Cell , vol.97 , pp. 435-447
    • Ferrari, G.1    Langen, H.2    Naito, M.3    Pieters, J.4
  • 72
    • 0034306013 scopus 로고    scopus 로고
    • Function of Rho family proteins in actin dynamics during phagocytosis and engulfment
    • G. Chimini, and P. Chavrier Function of Rho family proteins in actin dynamics during phagocytosis and engulfment Nat. Cell Biol. 2 2000 E191 E196
    • (2000) Nat. Cell Biol. , vol.2
    • Chimini, G.1    Chavrier, P.2
  • 73
    • 0038523856 scopus 로고    scopus 로고
    • Regulation of endocytic traffic by Rho GTPases
    • B. Qualmann, and H. Mellor Regulation of endocytic traffic by Rho GTPases Biochem. J. 371 2003 233 241
    • (2003) Biochem. J. , vol.371 , pp. 233-241
    • Qualmann, B.1    Mellor, H.2
  • 74
    • 0032573378 scopus 로고    scopus 로고
    • Identification of two distinct mechanisms of phagocytosis controlled by different Rho GTPases
    • E. Caron, and A. Hall Identification of two distinct mechanisms of phagocytosis controlled by different Rho GTPases Science 282 1998 1717 1721
    • (1998) Science , vol.282 , pp. 1717-1721
    • Caron, E.1    Hall, A.2
  • 75
    • 0032493491 scopus 로고    scopus 로고
    • A requirement for ARF6 in Fcgamma receptor-mediated phagocytosis in macrophages
    • Q. Zhang, D. Cox, C.C. Tseng, J.G. Donaldson, and S. Greenberg A requirement for ARF6 in Fcgamma receptor-mediated phagocytosis in macrophages J. Biol. Chem. 273 1998 19977 19981
    • (1998) J. Biol. Chem. , vol.273 , pp. 19977-19981
    • Zhang, Q.1    Cox, D.2    Tseng, C.C.3    Donaldson, J.G.4    Greenberg, S.5
  • 76
    • 0037477712 scopus 로고    scopus 로고
    • ADP ribosylation factor 6 is activated and controls membrane delivery during phagocytosis in macrophages
    • F. Niedergang, E. Colucci-Guyon, T. Dubois, G. Raposo, and P. Chavrier ADP ribosylation factor 6 is activated and controls membrane delivery during phagocytosis in macrophages J. Cell Biol. 161 2003 1143 1150
    • (2003) J. Cell Biol. , vol.161 , pp. 1143-1150
    • Niedergang, F.1    Colucci-Guyon, E.2    Dubois, T.3    Raposo, G.4    Chavrier, P.5
  • 77
    • 0036070631 scopus 로고    scopus 로고
    • Opsonization modulates Rac-1 activation during cell entry by Leishmania amazonensis
    • J. Morehead, I. Coppens, and N.W. Andrews Opsonization modulates Rac-1 activation during cell entry by Leishmania amazonensis Infect. Immun. 70 2002 4571 4580
    • (2002) Infect. Immun. , vol.70 , pp. 4571-4580
    • Morehead, J.1    Coppens, I.2    Andrews, N.W.3
  • 78
    • 0037103252 scopus 로고    scopus 로고
    • Complement receptor 3 (CD11b/CD18) mediates type I and type II phagocytosis during nonopsonic and opsonic phagocytosis, respectively
    • V. Le Cabec, S. Carreno, A. Moisand, C. Bordier, and I. Maridonneau-Parini Complement receptor 3 (CD11b/CD18) mediates type I and type II phagocytosis during nonopsonic and opsonic phagocytosis, respectively J. Immunol. 169 2002 2003 2009
    • (2002) J. Immunol. , vol.169 , pp. 2003-2009
    • Le Cabec, V.1    Carreno, S.2    Moisand, A.3    Bordier, C.4    Maridonneau-Parini, I.5
  • 79
    • 0033790639 scopus 로고    scopus 로고
    • Involvement of the Arp2/3 complex in phagocytosis mediated by FcgammaR or CR3
    • R.C. May, E. Caron, A. Hall, and L.M. Machesky Involvement of the Arp2/3 complex in phagocytosis mediated by FcgammaR or CR3 Nat. Cell Biol. 2 2000 246 248
    • (2000) Nat. Cell Biol. , vol.2 , pp. 246-248
    • May, R.C.1    Caron, E.2    Hall, A.3    MacHesky, L.M.4
  • 81
    • 0037143448 scopus 로고    scopus 로고
    • Rho-kinase and myosin-II control phagocytic cup formation during CR, but not FcgammaR, phagocytosis
    • I.M. Olazabal, E. Caron, R.C. May, K. Schilling, D.A. Knecht, and L.M. Machesky Rho-kinase and myosin-II control phagocytic cup formation during CR, but not FcgammaR, phagocytosis Curr. Biol. 12 2002 1413 1418
    • (2002) Curr. Biol. , vol.12 , pp. 1413-1418
    • Olazabal, I.M.1    Caron, E.2    May, R.C.3    Schilling, K.4    Knecht, D.A.5    MacHesky, L.M.6
  • 82
    • 0036632356 scopus 로고    scopus 로고
    • The role of protein kinase C in the transient association of p57, a coronin family actin-binding protein, with phagosomes
    • S. Itoh, K. Suzuki, J. Nishihata, M. Iwasa, T. Oku, S. Nakajin, W.M. Nauseef, and S. Toyoshima The role of protein kinase C in the transient association of p57, a coronin family actin-binding protein, with phagosomes Biol. Pharm. Bull. 25 2002 837 844
    • (2002) Biol. Pharm. Bull. , vol.25 , pp. 837-844
    • Itoh, S.1    Suzuki, K.2    Nishihata, J.3    Iwasa, M.4    Oku, T.5    Nakajin, S.6    Nauseef, W.M.7    Toyoshima, S.8
  • 83
    • 0028909477 scopus 로고
    • Protein kinase C regulates MARCKS cycling between the plasma membrane and lysosomes in fibroblasts
    • L.A. Allen, and A. Aderem Protein kinase C regulates MARCKS cycling between the plasma membrane and lysosomes in fibroblasts EMBO J. 14 1995 1109 1120
    • (1995) EMBO J. , vol.14 , pp. 1109-1120
    • Allen, L.A.1    Aderem, A.2
  • 86
    • 0033679768 scopus 로고    scopus 로고
    • Amphiphysin IIm, a novel amphiphysin II isoform, is required for macrophage phagocytosis
    • E.S. Gold, N.S. Morrissette, D.M. Underhill, J. Guo, M. Bassetti, and A. Aderem Amphiphysin IIm, a novel amphiphysin II isoform, is required for macrophage phagocytosis Immunity 12 2000 285 292
    • (2000) Immunity , vol.12 , pp. 285-292
    • Gold, E.S.1    Morrissette, N.S.2    Underhill, D.M.3    Guo, J.4    Bassetti, M.5    Aderem, A.6
  • 88
    • 0033790751 scopus 로고    scopus 로고
    • Subversion of a young phagosome: The survival strategies of intracellular pathogens
    • S. Duclos, and M. Desjardins Subversion of a young phagosome: the survival strategies of intracellular pathogens Cell. Microbiol. 2 2000 365 377
    • (2000) Cell. Microbiol. , vol.2 , pp. 365-377
    • Duclos, S.1    Desjardins, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.