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Volumn 7, Issue 8, 2008, Pages 1344-1351

Dolichyl-phosphate-glucose is used to make O-glycans on glycoproteins of Trichomonas vaginalis

Author keywords

[No Author keywords available]

Indexed keywords

DOLICHOL D GLUCOSYLMONOPHOSPHATE; DOLICHOL PHOSPHATE MANNOSE; DOLICHOL-D-GLUCOSYLMONOPHOSPHATE; DOLICHYL PHOSPHATE BETA D MANNOSYLTRANSFERASE; DOLICHYL-PHOSPHATE BETA-D-MANNOSYLTRANSFERASE; GLUCOSYLTRANSFERASE; GLYCOPROTEIN; ISOPRENOID PHOSPHATE SUGAR; MANNOSYLTRANSFERASE; POLYSACCHARIDE;

EID: 48949094091     PISSN: 15359778     EISSN: None     Source Type: Journal    
DOI: 10.1128/EC.00061-08     Document Type: Article
Times cited : (11)

References (35)
  • 3
    • 27744522582 scopus 로고    scopus 로고
    • Trichomonas vaginalis lipophosphoglycan mutants have reduced adherence and cytotoxicity to human ectocervical cells
    • Bastida-Corcuera, F. D., C. Y. Okumura, A. Colocoussi, and P. J. Jonson. 2005. Trichomonas vaginalis lipophosphoglycan mutants have reduced adherence and cytotoxicity to human ectocervical cells. Eukaryot. Cell 4:1951-1958.
    • (2005) Eukaryot. Cell , vol.4 , pp. 1951-1958
    • Bastida-Corcuera, F.D.1    Okumura, C.Y.2    Colocoussi, A.3    Jonson, P.J.4
  • 4
    • 33846528971 scopus 로고    scopus 로고
    • Draft genome sequence of the sexually transmitted pathogen Trichomonas vaginalis
    • Carlton, J. M., R. P. Hirt, J. C. Silva, A. L. Delcher, M. Schatz, Q. Zhao, et al. 2007. Draft genome sequence of the sexually transmitted pathogen Trichomonas vaginalis. Science 315:207-212.
    • (2007) Science , vol.315 , pp. 207-212
    • Carlton, J.M.1    Hirt, R.P.2    Silva, J.C.3    Delcher, A.L.4    Schatz, M.5    Zhao, Q.6
  • 5
    • 0036310976 scopus 로고    scopus 로고
    • Methods for cultivation of luminal parasitic protists of clinical importance
    • Clark, C. G., and L. S. Diamond. 2002. Methods for cultivation of luminal parasitic protists of clinical importance. Clin. Microbiol. Rev. 15:329-341.
    • (2002) Clin. Microbiol. Rev , vol.15 , pp. 329-341
    • Clark, C.G.1    Diamond, L.S.2
  • 6
    • 0033179512 scopus 로고    scopus 로고
    • Active isoprenoid pathway in the intra-erythrocytic stages of Plasmodium falciparum: Presence of dolichols of 11 and 12 isoprene units
    • Couto, A. C., E. A. Kimura, V. J. Peres, M. L. Uhrig, and A. M. Katzin. 1999. Active isoprenoid pathway in the intra-erythrocytic stages of Plasmodium falciparum: presence of dolichols of 11 and 12 isoprene units. Biochem. J. 341:629-637.
    • (1999) Biochem. J , vol.341 , pp. 629-637
    • Couto, A.C.1    Kimura, E.A.2    Peres, V.J.3    Uhrig, M.L.4    Katzin, A.M.5
  • 7
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: Multiple sequence alignment with high accuracy and high throughput
    • Edgar, R. C. 2004. MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res. 32:1792-1797.
    • (2004) Nucleic Acids Res , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 8
    • 33749263019 scopus 로고    scopus 로고
    • Trichomonas vaginalis lipophosphoglycan triggers a selective upregulation of cytokines by human female reproductive tract epithelial cells
    • Fichorova, R. N., R. T. Trifonova, R. O. Gilbert, C. E. Costello, G. R. Hayes, J. J. Lucas, and B. N. Singh. 2006. Trichomonas vaginalis lipophosphoglycan triggers a selective upregulation of cytokines by human female reproductive tract epithelial cells. Infect. Immun. 74:5773-5779.
    • (2006) Infect. Immun , vol.74 , pp. 5773-5779
    • Fichorova, R.N.1    Trifonova, R.T.2    Gilbert, R.O.3    Costello, C.E.4    Hayes, G.R.5    Lucas, J.J.6    Singh, B.N.7
  • 9
    • 0027968807 scopus 로고
    • Isolation of the ALG5 locus encoding the UDP-glucose:dolichyl-phosphate glucosyltransferase from Saccharomyces cerevisiae
    • Heesen, S., L. Lehle, A. Weissmann, and M. Aebi. 1994. Isolation of the ALG5 locus encoding the UDP-glucose:dolichyl-phosphate glucosyltransferase from Saccharomyces cerevisiae. Eur. J. Biochem. 224:71-79.
    • (1994) Eur. J. Biochem , vol.224 , pp. 71-79
    • Heesen, S.1    Lehle, L.2    Weissmann, A.3    Aebi, M.4
  • 10
    • 3943059566 scopus 로고    scopus 로고
    • Roles of N-linked glycans in the endoplasmic reticulum
    • Helenius, A., and M. Aebi. 2004. Roles of N-linked glycans in the endoplasmic reticulum. Annu. Rev. Biochem. 73:1019-1049.
    • (2004) Annu. Rev. Biochem , vol.73 , pp. 1019-1049
    • Helenius, A.1    Aebi, M.2
  • 11
    • 0021067823 scopus 로고
    • Yeast mutants deficient in protein glycosylation
    • Huffaker, T., and P. W. Robbins. 1983. Yeast mutants deficient in protein glycosylation. Proc. Natl. Acad. Sci. USA 80:7466-7470.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 7466-7470
    • Huffaker, T.1    Robbins, P.W.2
  • 12
    • 0026691182 scopus 로고
    • The rapid generation of mutation data matrices from protein sequences
    • Jones, D. T., W. R. Taylor, and J. M. Thornton. 1992. The rapid generation of mutation data matrices from protein sequences. Comput. Appl. Biosci. 8:275-282.
    • (1992) Comput. Appl. Biosci , vol.8 , pp. 275-282
    • Jones, D.T.1    Taylor, W.R.2    Thornton, J.M.3
  • 13
    • 2142657817 scopus 로고    scopus 로고
    • A combined transmembrane topology and signal peptide prediction method
    • Käll, L., A. Krogh, and E. L. L. Sonnhammer. 2004. A combined transmembrane topology and signal peptide prediction method. J. Mol. Biol. 338:1027-1036.
    • (2004) J. Mol. Biol , vol.338 , pp. 1027-1036
    • Käll, L.1    Krogh, A.2    Sonnhammer, E.L.L.3
  • 14
    • 33744953962 scopus 로고    scopus 로고
    • Dodecaprenyl phosphate-galacturonic acid as a donor substrate for lipopolysaccharide core glycosylation in Rhizobium leguminosarum
    • Kanjilal-Kolar, S., and C. R. Raetz. 2006. Dodecaprenyl phosphate-galacturonic acid as a donor substrate for lipopolysaccharide core glycosylation in Rhizobium leguminosarum. J. Biol. Chem. 281:12879-12887.
    • (2006) J. Biol. Chem , vol.281 , pp. 12879-12887
    • Kanjilal-Kolar, S.1    Raetz, C.R.2
  • 15
    • 33645103490 scopus 로고    scopus 로고
    • An evolving view of the eukaryotic oligosaccharyltransferase
    • Kelleher, D. J., and R. Gilmore. 2006, An evolving view of the eukaryotic oligosaccharyltransferase. Glycobiology 16:47R-62R.
    • (2006) Glycobiology , vol.16
    • Kelleher, D.J.1    Gilmore, R.2
  • 16
    • 33644934032 scopus 로고    scopus 로고
    • Manipulation of prenyl chain length determination mechanism of cis-prenyltransferases
    • Kharel, Y., S. Takahashi, S. Yamashita, and T. Koyama. 2006. Manipulation of prenyl chain length determination mechanism of cis-prenyltransferases. FEBS J. 273:647-657.
    • (2006) FEBS J , vol.273 , pp. 647-657
    • Kharel, Y.1    Takahashi, S.2    Yamashita, S.3    Koyama, T.4
  • 17
    • 0033020387 scopus 로고    scopus 로고
    • Overexpression of the Saccharomyces cerevisiae mannosylphosphodolichol synthase-encoding gene in Trichoderma reesei results in an increased level of protein secretion and abnormal cell ultrastructure
    • Kruszewska, J. S., A. H. Butterweck, W. Kurzatkowski, A. Migdalski, C. P. Kubicek, and G. Palamarczyk. 1999. Overexpression of the Saccharomyces cerevisiae mannosylphosphodolichol synthase-encoding gene in Trichoderma reesei results in an increased level of protein secretion and abnormal cell ultrastructure. Appl. Environ. Microbiol. 65:2382-2387.
    • (1999) Appl. Environ. Microbiol , vol.65 , pp. 2382-2387
    • Kruszewska, J.S.1    Butterweck, A.H.2    Kurzatkowski, W.3    Migdalski, A.4    Kubicek, C.P.5    Palamarczyk, G.6
  • 18
    • 36448991500 scopus 로고    scopus 로고
    • Larkin, M. A, G. Blackshields, N. P. Brown, R. Chenna, P. A. McGettigan, H. McWilliam, F. Valentin, I. M. Wallace, A. Wilm, R. Lopez, J. D. Thompson, T. J. Gibson, and D. G. Higgins. 2007. Clustal W and Clustal X version 2.0. Bioinformatics 23:2947-2948
    • Larkin, M. A., G. Blackshields, N. P. Brown, R. Chenna, P. A. McGettigan, H. McWilliam, F. Valentin, I. M. Wallace, A. Wilm, R. Lopez, J. D. Thompson, T. J. Gibson, and D. G. Higgins. 2007. Clustal W and Clustal X version 2.0. Bioinformatics 23:2947-2948.
  • 19
    • 0026043234 scopus 로고
    • The mevalonate pathway in the bloodstream form of Trypanosoma brucei. Identification of dolichols containing 11 and 12 isoprene residues
    • Low, P., G. Dallner, S. Mayor, S. Cohen, B. T. Chait, and A. K. Menon. 1991. The mevalonate pathway in the bloodstream form of Trypanosoma brucei. Identification of dolichols containing 11 and 12 isoprene residues. J. Biol. Chem. 266:19250-19257.
    • (1991) J. Biol. Chem , vol.266 , pp. 19250-19257
    • Low, P.1    Dallner, G.2    Mayor, S.3    Cohen, S.4    Chait, B.T.5    Menon, A.K.6
  • 20
    • 0347635516 scopus 로고    scopus 로고
    • Demonstration of mammalian protein O-mannosyltransferase activity: Coexpression of POMT1 and POMT2 required for enzymatic activity
    • Manya, H., A. Chiba, A. Yoshida, X. Wang, Y. Chiba, Y. Jigami, R. Margolis, and T. Endo. 2004. Demonstration of mammalian protein O-mannosyltransferase activity: coexpression of POMT1 and POMT2 required for enzymatic activity. Proc. Natl. Acad. Sci. USA 101:500-505.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 500-505
    • Manya, H.1    Chiba, A.2    Yoshida, A.3    Wang, X.4    Chiba, Y.5    Jigami, Y.6    Margolis, R.7    Endo, T.8
  • 22
    • 0036730252 scopus 로고    scopus 로고
    • Common origin and evolution of glycosyltransferases using Dol-P-monosaccharides as donor substrate
    • Oriol, R., I. Martinez-Duncker, I. Chantret, R. Mollicone, and P. Codogno. 2002. Common origin and evolution of glycosyltransferases using Dol-P-monosaccharides as donor substrate. Mol. Biol. Evol. 19:1451-1463.
    • (2002) Mol. Biol. Evol , vol.19 , pp. 1451-1463
    • Oriol, R.1    Martinez-Duncker, I.2    Chantret, I.3    Mollicone, R.4    Codogno, P.5
  • 23
    • 0024297293 scopus 로고
    • Cloning and sequ encing of the yeast gene for dolichol phosphate mannose synthase, an essential protein
    • Orlean, P., C. Albright, and P. W. Robbins. 1988. Cloning and sequ encing of the yeast gene for dolichol phosphate mannose synthase, an essential protein. J. Biol. Chem. 263:17499-17507.
    • (1988) J. Biol. Chem , vol.263 , pp. 17499-17507
    • Orlean, P.1    Albright, C.2    Robbins, P.W.3
  • 24
    • 34248227584 scopus 로고    scopus 로고
    • Thematic review series: Lipid posttranslational modifications. GPI anchoring of protein in yeast and mammalian cells, or: how we learned to stop worrying and love glycophospholipids
    • Orlean, P., and A. K. Menon. 2007. Thematic review series: lipid posttranslational modifications. GPI anchoring of protein in yeast and mammalian cells, or: how we learned to stop worrying and love glycophospholipids. J. Lipid Res. 48:993-1011.
    • (2007) J. Lipid Res , vol.48 , pp. 993-1011
    • Orlean, P.1    Menon, A.K.2
  • 25
    • 13444281918 scopus 로고    scopus 로고
    • The diversity of protist and fungal dolichol-linked precursors to Asn-linked glycans likely results from secondary loss of sets of glycosyltransferases
    • Samuelson, J., S. Banerjee, P. Magnelli, J. Cui, D. J. Kelleher, R. Gilmore, and P. W. Robbins. 2005. The diversity of protist and fungal dolichol-linked precursors to Asn-linked glycans likely results from secondary loss of sets of glycosyltransferases. Proc. Natl. Acad. Sci. USA 102:1548-1553.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 1548-1553
    • Samuelson, J.1    Banerjee, S.2    Magnelli, P.3    Cui, J.4    Kelleher, D.J.5    Gilmore, R.6    Robbins, P.W.7
  • 26
    • 0028465445 scopus 로고
    • SUC1 and SUC2: Two sucrose transporters from Arabidopsis thaliana; expression and characterization in baker's yeast and identification of the histidine-tagged protein
    • Sauer, N., and J. Stolz. 1994. SUC1 and SUC2: two sucrose transporters from Arabidopsis thaliana; expression and characterization in baker's yeast and identification of the histidine-tagged protein. Plant J. 6:67-77.
    • (1994) Plant J , vol.6 , pp. 67-77
    • Sauer, N.1    Stolz, J.2
  • 27
    • 0036205377 scopus 로고    scopus 로고
    • TREE-PUZZLE: Maximum likelihood phylogenetic analysis using quartets and parallel computing
    • Schmidt, H. A., K. Strimmer, M. Vingron, and A. von Haeseler. 2002. TREE-PUZZLE: maximum likelihood phylogenetic analysis using quartets and parallel computing. Bioinformatics 18:502-504.
    • (2002) Bioinformatics , vol.18 , pp. 502-504
    • Schmidt, H.A.1    Strimmer, K.2    Vingron, M.3    von Haeseler, A.4
  • 29
    • 0027463719 scopus 로고
    • Lipophosphoglycan-like glycoconjugate of Trichomonas foetus and Trichomonas vaginalis
    • Singh, B. N. 1993. Lipophosphoglycan-like glycoconjugate of Trichomonas foetus and Trichomonas vaginalis. Mol. Biochem. Parasitol. 57:281-294.
    • (1993) Mol. Biochem. Parasitol , vol.57 , pp. 281-294
    • Singh, B.N.1
  • 30
    • 0021267941 scopus 로고
    • Enzymatic glucosylation of dolichol monophosphate and transfer of glucose from isolated dolichyl-D-glucosyl phosphate to ceramides by BHK-21 cell microsomes
    • Suzuki, Y., C. P. Ecker, and H. A. Blough. 1984. Enzymatic glucosylation of dolichol monophosphate and transfer of glucose from isolated dolichyl-D-glucosyl phosphate to ceramides by BHK-21 cell microsomes. Eur. J. Biochem. 143:447-453.
    • (1984) Eur. J. Biochem , vol.143 , pp. 447-453
    • Suzuki, Y.1    Ecker, C.P.2    Blough, H.A.3
  • 31
    • 22044458610 scopus 로고    scopus 로고
    • Polyisoprenoids: Structure, biosynthesis and function
    • Swiezewska, E., and W. Danikiewicz. 2005. Polyisoprenoids: structure, biosynthesis and function. Prog. Lipid Res. 44:235-258.
    • (2005) Prog. Lipid Res , vol.44 , pp. 235-258
    • Swiezewska, E.1    Danikiewicz, W.2
  • 32
    • 0030994977 scopus 로고    scopus 로고
    • Polyprenol formation in the yeast Saccharomyces cerevisiae: Effect of farnesyl diphosphate synthase overexpression
    • Szkopinska, A., K. Grabinska, D. Delourme, F. Karst, J. Rytka, and G. Palamarczyk. 1997. Polyprenol formation in the yeast Saccharomyces cerevisiae: effect of farnesyl diphosphate synthase overexpression. J. Lipid Res. 38:962-968.
    • (1997) J. Lipid Res , vol.38 , pp. 962-968
    • Szkopinska, A.1    Grabinska, K.2    Delourme, D.3    Karst, F.4    Rytka, J.5    Palamarczyk, G.6
  • 35
    • 21244433591 scopus 로고    scopus 로고
    • Protein O-mannosylation is crucial for cell wall integrity, septation and viability in fission yeast
    • Willer, T., M. Brandle, M. Sipiczki, and S. Strahl. 2005. Protein O-mannosylation is crucial for cell wall integrity, septation and viability in fission yeast. Mol. Microbiol. 57:156-170.
    • (2005) Mol. Microbiol , vol.57 , pp. 156-170
    • Willer, T.1    Brandle, M.2    Sipiczki, M.3    Strahl, S.4


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