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Volumn 135, Issue 2, 2004, Pages 225-229

The mitochondrial ribosome of the protozoan Acanthamoeba castellanii is the target for macrolide antibiotics

Author keywords

Acanthamoeba; Drug resistance; Macrolide; Mitochondria; Protein synthesis inhibitors; Ribosomal RNA

Indexed keywords

MACROLIDE; CLARITHROMYCIN; GENTAMICIN; HYGROMYCIN B;

EID: 1942446017     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molbiopara.2004.02.004     Document Type: Article
Times cited : (10)

References (39)
  • 1
    • 0023922697 scopus 로고
    • Azithromycin, a macrolide antibiotic with potent activity against Toxoplasma gondii
    • Araujo F.G., Guptill D.R., Remington J.S. Azithromycin, a macrolide antibiotic with potent activity against Toxoplasma gondii. Antimicrob Agents Chemother. 32:1988;755-757.
    • (1988) Antimicrob Agents Chemother , vol.32 , pp. 755-757
    • Araujo, F.G.1    Guptill, D.R.2    Remington, J.S.3
  • 2
    • 0024588809 scopus 로고
    • Susceptibility of Giardia lamblia to aminoglycoside protein synthesis inhibitors: Correlation with rRNA structure
    • Edlind T.D. Susceptibility of Giardia lamblia to aminoglycoside protein synthesis inhibitors: correlation with rRNA structure. Antimicrob Agents Chemother. 33:1989;484-488.
    • (1989) Antimicrob Agents Chemother , vol.33 , pp. 484-488
    • Edlind, T.D.1
  • 3
    • 0029156099 scopus 로고
    • Effects of azithromycin on malariometric indices in the Gambia
    • Sadiq S.T., Glasgow K.W., Drakeley C.J.et al. Effects of azithromycin on malariometric indices in The Gambia. Lancet. 346:1995;881-882.
    • (1995) Lancet , vol.346 , pp. 881-882
    • Sadiq, S.T.1    Glasgow, K.W.2    Drakeley, C.J.3
  • 4
    • 0031823634 scopus 로고    scopus 로고
    • Paromomycin and geneticin inhibit intracellular Cryptosporidium parvum without trafficking through the host cell cytoplasm: Implications for drug delivery
    • Griffiths J.K., Balakrishnan R., Widmer G., Tzipori S. Paromomycin and geneticin inhibit intracellular Cryptosporidium parvum without trafficking through the host cell cytoplasm: implications for drug delivery. Infect. Immun. 66:1998;3874-3883.
    • (1998) Infect. Immun. , vol.66 , pp. 3874-3883
    • Griffiths, J.K.1    Balakrishnan, R.2    Widmer, G.3    Tzipori, S.4
  • 5
    • 0031030313 scopus 로고    scopus 로고
    • Inhibition of Plasmodium falciparum protein synthesis. Targeting the plastid-like organelle with thiostrepton
    • McConkey G.A., Rogers M.J., McCutchan T.F. Inhibition of Plasmodium falciparum protein synthesis. Targeting the plastid-like organelle with thiostrepton. J. Biol. Chem. 272:1997;2046-2049.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2046-2049
    • McConkey, G.A.1    Rogers, M.J.2    McCutchan, T.F.3
  • 6
    • 0031917769 scopus 로고    scopus 로고
    • The antibiotic micrococcin is a potent inhibitor of growth and protein synthesis in the malaria parasite
    • Rogers M.J., Cundliffe E., McCutchan T.F. The antibiotic micrococcin is a potent inhibitor of growth and protein synthesis in the malaria parasite. Antimicrob Agents Chemother. 42:1998;715-716.
    • (1998) Antimicrob Agents Chemother , vol.42 , pp. 715-716
    • Rogers, M.J.1    Cundliffe, E.2    McCutchan, T.F.3
  • 9
    • 0034776893 scopus 로고    scopus 로고
    • Anti-toxoplasmosis drugs
    • Derouin F. Anti-toxoplasmosis drugs. Curr. Opin. Invest. Drugs. 2:2001;1368-1374.
    • (2001) Curr. Opin. Invest. Drugs , vol.2 , pp. 1368-1374
    • Derouin, F.1
  • 10
    • 0036747490 scopus 로고    scopus 로고
    • Activity of azithromycin against Leishmania major in vitro and in vivo
    • Krolewiecki A., Leon S., Scott P., Abraham D. Activity of azithromycin against Leishmania major in vitro and in vivo. Am. J. Trop Med. Hyg. 67:2002;273-277.
    • (2002) Am. J. Trop Med. Hyg. , vol.67 , pp. 273-277
    • Krolewiecki, A.1    Leon, S.2    Scott, P.3    Abraham, D.4
  • 11
    • 0028832133 scopus 로고
    • Inhibition of cytoplasmic and organellar protein synthesis in Toxoplasma gondii. Implications for the target of macrolide antibiotics
    • Beckers C.J., Roos D.S., Donald R.G.et al. Inhibition of cytoplasmic and organellar protein synthesis in Toxoplasma gondii. Implications for the target of macrolide antibiotics. J. Clin. Invest. 95:1995;367-376.
    • (1995) J. Clin. Invest. , vol.95 , pp. 367-376
    • Beckers, C.J.1    Roos, D.S.2    Donald, R.G.3
  • 12
    • 0031444101 scopus 로고    scopus 로고
    • A plastid organelle as a drug target in apicomplexan parasites
    • Fichera M.E., Roos D.S. A plastid organelle as a drug target in apicomplexan parasites. Nature. 390:1997;407-409.
    • (1997) Nature , vol.390 , pp. 407-409
    • Fichera, M.E.1    Roos, D.S.2
  • 14
    • 0032815207 scopus 로고    scopus 로고
    • Apicomplexan plastids as drug targets
    • McFadden G.I., Roos D.S. Apicomplexan plastids as drug targets. Trends Microbiol. 7:1999;328-333.
    • (1999) Trends Microbiol. , vol.7 , pp. 328-333
    • McFadden, G.I.1    Roos, D.S.2
  • 15
    • 0032988608 scopus 로고    scopus 로고
    • The apicoplast as a potential therapeutic target in Toxoplasma and other apicomplexan parasites: Some additional thoughts
    • Roos D.S. The apicoplast as a potential therapeutic target in Toxoplasma and other apicomplexan parasites: some additional thoughts. Parasitol Today. 15:1999;41.
    • (1999) Parasitol Today , vol.15 , pp. 41
    • Roos, D.S.1
  • 16
    • 0036227773 scopus 로고    scopus 로고
    • An rRNA mutation identifies the apicoplast as the target for clindamycin in Toxoplasma gondii
    • Camps M., Arrizabalaga G., Boothroyd J. An rRNA mutation identifies the apicoplast as the target for clindamycin in Toxoplasma gondii. Mol. Microbiol. 43:2002;1309-1318.
    • (2002) Mol. Microbiol. , vol.43 , pp. 1309-1318
    • Camps, M.1    Arrizabalaga, G.2    Boothroyd, J.3
  • 17
    • 0022624064 scopus 로고
    • Effects of mitochondrial inhibitors on intraerythrocytic Plasmodium falciparum in in vitro cultures
    • Ginsburg H., Divo A.A., Geary T.G., Boland M.T., Jensen J.B. Effects of mitochondrial inhibitors on intraerythrocytic Plasmodium falciparum in in vitro cultures. J. Protozool. 33:1986;121-125.
    • (1986) J. Protozool. , vol.33 , pp. 121-125
    • Ginsburg, H.1    Divo, A.A.2    Geary, T.G.3    Boland, M.T.4    Jensen, J.B.5
  • 19
    • 0037181479 scopus 로고    scopus 로고
    • Inhibition of mitochondrial and plastid activity of Plasmodium falciparum by minocycline
    • Lin Q., Katakura K., Suzuki M. Inhibition of mitochondrial and plastid activity of Plasmodium falciparum by minocycline. FEBS Lett. 515:2002;71-74.
    • (2002) FEBS Lett , vol.515 , pp. 71-74
    • Lin, Q.1    Katakura, K.2    Suzuki, M.3
  • 20
    • 0024424033 scopus 로고
    • Mutations in 16S ribosomal RNA disrupt antibiotic-RNA interactions
    • De Stasio E.A., Moazed D., Noller H.F., Dahlberg A.E. Mutations in 16S ribosomal RNA disrupt antibiotic-RNA interactions. EMBO J. 8:1989;1213-1216.
    • (1989) EMBO J. , vol.8 , pp. 1213-1216
    • De Stasio, E.A.1    Moazed, D.2    Noller, H.F.3    Dahlberg, A.E.4
  • 21
    • 0027248565 scopus 로고
    • Erythromycin binding is reduced in ribosomes with conformational alterations in the 23S rRNA peptidyl transferase loop
    • Douthwaite S., Aagaard C. Erythromycin binding is reduced in ribosomes with conformational alterations in the 23S rRNA peptidyl transferase loop. J. Mol. Biol. 232:1993;725-731.
    • (1993) J. Mol. Biol. , vol.232 , pp. 725-731
    • Douthwaite, S.1    Aagaard, C.2
  • 22
    • 0024746937 scopus 로고
    • Antibiotic resistance mutations in the chloroplast 16S and 23S rRNA genes of Chlamydomonas reinhardtii: Correlation of genetic and physical maps of the chloroplast genome
    • Harris E.H., Burkhart B.D., Gillham N.W., Boynton J.E. Antibiotic resistance mutations in the chloroplast 16S and 23S rRNA genes of Chlamydomonas reinhardtii: correlation of genetic and physical maps of the chloroplast genome. Genetics. 123:1989;281-292.
    • (1989) Genetics , vol.123 , pp. 281-292
    • Harris, E.H.1    Burkhart, B.D.2    Gillham, N.W.3    Boynton, J.E.4
  • 23
    • 0031802176 scopus 로고    scopus 로고
    • A single 16S ribosomal RNA substitution is responsible for resistance to amikacin and other 2-deoxystreptamine aminoglycosides in Mycobacterium abscessus and Mycobacterium chelonae
    • Prammananan T., Sander P., Brown B.A.et al. A single 16S ribosomal RNA substitution is responsible for resistance to amikacin and other 2-deoxystreptamine aminoglycosides in Mycobacterium abscessus and Mycobacterium chelonae. J. Infect. Dis. 177:1998;1573-1581.
    • (1998) J. Infect. Dis. , vol.177 , pp. 1573-1581
    • Prammananan, T.1    Sander, P.2    Brown, B.A.3
  • 25
    • 0029800114 scopus 로고    scopus 로고
    • Introducing mutations into a chromosomal rRNA gene using a genetically modified eubacterial host with a single rRNA operon
    • Sander P., Prammananan T., Bottger E.C. Introducing mutations into a chromosomal rRNA gene using a genetically modified eubacterial host with a single rRNA operon. Mol. Microbiol. 22:1996;841-848.
    • (1996) Mol. Microbiol. , vol.22 , pp. 841-848
    • Sander, P.1    Prammananan, T.2    Bottger, E.C.3
  • 26
    • 0031879814 scopus 로고    scopus 로고
    • Site-specific mutations in the 23S rRNA gene of Helicobacter pylori confer two types of resistance to macrolide-lincosamide-streptogramin B antibiotics
    • Wang G., Taylor D.E. Site-specific mutations in the 23S rRNA gene of Helicobacter pylori confer two types of resistance to macrolide-lincosamide- streptogramin B antibiotics. Antimicrob Agents Chemother. 42:1998;1952-1958.
    • (1998) Antimicrob Agents Chemother , vol.42 , pp. 1952-1958
    • Wang, G.1    Taylor, D.E.2
  • 27
    • 0035032997 scopus 로고    scopus 로고
    • Structural basis for selectivity and toxicity of ribosomal antibiotics
    • Bottger E.C., Springer B., Prammananan T., Kidan Y., Sander P. Structural basis for selectivity and toxicity of ribosomal antibiotics. EMBO Rep. 2:2001;318-323.
    • (2001) EMBO Rep. , vol.2 , pp. 318-323
    • Bottger, E.C.1    Springer, B.2    Prammananan, T.3    Kidan, Y.4    Sander, P.5
  • 28
    • 0028924641 scopus 로고
    • Fine structure of the peptidyl transferase centre on 23S-like rRNAs deduced from chemical probin of antibiotic-ribosome complexes
    • Rodriguez-Fonseca C., Amils R., Garrett R.A. Fine structure of the peptidyl transferase centre on 23S-like rRNAs deduced from chemical probin of antibiotic-ribosome complexes. J. Mol. Biol. 247:1995;224-235.
    • (1995) J. Mol. Biol. , vol.247 , pp. 224-235
    • Rodriguez-Fonseca, C.1    Amils, R.2    Garrett, R.A.3
  • 30
    • 0037398448 scopus 로고    scopus 로고
    • Acanthamoeba spp. as agents of disease in humans
    • Marciano-Cabral F., Cabral G. Acanthamoeba spp. as agents of disease in humans. Clin. Microbiol. Rev. 16:2003;273-307.
    • (2003) Clin. Microbiol. Rev. , vol.16 , pp. 273-307
    • Marciano-Cabral, F.1    Cabral, G.2
  • 31
    • 0037251969 scopus 로고    scopus 로고
    • Garrity GM and others. The Ribosomal Database Project (RDP-II): Previewing a new autoaligner that allows regular updates and the new prokaryotic taxonomy
    • Cole J.R., Chai B., Marsh T.L.et al. Garrity GM and others. The Ribosomal Database Project (RDP-II): previewing a new autoaligner that allows regular updates and the new prokaryotic taxonomy. Nucleic Acids Res. 31:2003;442-443.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 442-443
    • Cole, J.R.1    Chai, B.2    Marsh, T.L.3
  • 32
    • 0002051540 scopus 로고    scopus 로고
    • BioEdit: A user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT
    • Hall T.A. BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT. Nucleic Acids Symp Ser. 41:1999;95-98.
    • (1999) Nucleic Acids Symp Ser , vol.41 , pp. 95-98
    • Hall, T.A.1
  • 33
    • 0018624480 scopus 로고
    • Growth, reproduction, and differentiation in Acanthamoeba
    • Byers T.J. Growth, reproduction, and differentiation in Acanthamoeba. Int. Rev. Cytol. 61:1979;283-338.
    • (1979) Int. Rev. Cytol. , vol.61 , pp. 283-338
    • Byers, T.J.1
  • 34
    • 0018962602 scopus 로고
    • Differentiation promoting factors induced in Acanthamoeba by inhibitors of mitochondrial macromolecule synthesis
    • Akins R.A., Byers T.J. Differentiation promoting factors induced in Acanthamoeba by inhibitors of mitochondrial macromolecule synthesis. Dev. Biol. 78:1980;126-140.
    • (1980) Dev. Biol. , vol.78 , pp. 126-140
    • Akins, R.A.1    Byers, T.J.2
  • 35
    • 0032978275 scopus 로고    scopus 로고
    • RecA-mediated gene conversion and aminoglycoside resistance in strains heterozygous for rRNA
    • Prammananan T., Sander P., Springer B., Bottger E.C. RecA-mediated gene conversion and aminoglycoside resistance in strains heterozygous for rRNA. Antimicrob Agents Chemother. 43:1999;447-453.
    • (1999) Antimicrob Agents Chemother , vol.43 , pp. 447-453
    • Prammananan, T.1    Sander, P.2    Springer, B.3    Bottger, E.C.4
  • 36
    • 1842409545 scopus 로고    scopus 로고
    • Molecular diagnosis of bacterial endocarditis by broad-range PCR amplification and direct sequencing
    • Goldenberger D., Kunzli A., Vogt P., Zbinden R., Altwegg M. Molecular diagnosis of bacterial endocarditis by broad-range PCR amplification and direct sequencing. J. Clin. Microbiol. 35:1997;2733-2739.
    • (1997) J. Clin. Microbiol. , vol.35 , pp. 2733-2739
    • Goldenberger, D.1    Kunzli, A.2    Vogt, P.3    Zbinden, R.4    Altwegg, M.5
  • 37
    • 0014532519 scopus 로고
    • The fine structure of Acanthamoeba castellanii (Neff strain). II. Encystment
    • Bowers B., Korn E.D. The fine structure of Acanthamoeba castellanii (Neff strain). II. Encystment. J. Cell Biol. 41:1969;786-805.
    • (1969) J. Cell Biol. , vol.41 , pp. 786-805
    • Bowers, B.1    Korn, E.D.2
  • 38
    • 0030693282 scopus 로고    scopus 로고
    • Reevaluation of the effect of lysoyzme on Escherichia coli employing ultrarapid freezing followed by cryoelectronmicroscopy or freeze substitution
    • Wild P., Gabrieli A., Schraner E.M.et al. Reevaluation of the effect of lysoyzme on Escherichia coli employing ultrarapid freezing followed by cryoelectronmicroscopy or freeze substitution. Microsc Res. Tech. 39:1997;297-304.
    • (1997) Microsc Res. Tech. , vol.39 , pp. 297-304
    • Wild, P.1    Gabrieli, A.2    Schraner, E.M.3
  • 39
    • 0035873242 scopus 로고    scopus 로고
    • Enhanced resolution of membranes in cultured cells by cryoimmobilization and freeze-substitution
    • Wild P., Schraner E., Adler H., Humbel B. Enhanced resolution of membranes in cultured cells by cryoimmobilization and freeze-substitution. Microsc Res. Tech. 53:2001;313-321.
    • (2001) Microsc Res. Tech. , vol.53 , pp. 313-321
    • Wild, P.1    Schraner, E.2    Adler, H.3    Humbel, B.4


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