메뉴 건너뛰기




Volumn 1, Issue 6, 2010, Pages 546-550

Campylobacter jejuni free oligosaccharides function and fate

Author keywords

Acetyltransferase; Campylobacter jejuni; Free oligosaccharides; Mass spectrometry; N linked protein glycosylation; Oligosaccharyltransferase; Osmolarity; Periplasmic glucans; Pglb; Pgld; Salt stress

Indexed keywords

ASPARAGINE; GLYCOPROTEIN; GUANINE NUCLEOTIDE BINDING PROTEIN; HYDROLASE; OLIGOSACCHARIDE; PHOSPHATE; PROTEIN FOS;

EID: 79251471744     PISSN: 21505594     EISSN: 21505608     Source Type: Journal    
DOI: 10.4161/viru.1.6.13801     Document Type: Article
Times cited : (17)

References (29)
  • 1
    • 0036173114 scopus 로고    scopus 로고
    • Cronshaw AD,Wren BW. Identification of N-acetylgalactosaminecontaining glycoproteins PEB3 and CgpA in Campylobacter jejuni
    • Linton D, Allan E, Karlyshev AV, Cronshaw AD,Wren BW. Identification of N-acetylgalactosaminecontaining glycoproteins PEB3 and CgpA in Campylobacter jejuni. Mol Microbiol 2002; 43:497-508.
    • (2002) Mol Microbiol , vol.43 , pp. 497-508
    • Linton, D.1    Allan, E.2    Karlyshev, A.V.3
  • 2
    • 0033024228 scopus 로고    scopus 로고
    • Evidence for a system of general protein glycosylation in Campylobacter jejuni
    • Szymanski CM, Yao R, Ewing CP, Trust TJ, Guerry P. Evidence for a system of general protein glycosylation in Campylobacter jejuni. Mol Microbiol 1999; 32:1022-30.
    • (1999) Mol Microbiol , vol.32 , pp. 1022-1030
    • Szymanski, C.M.1    Yao, R.2    Ewing, C.P.3    Trust, T.J.4    Guerry, P.5
  • 4
    • 0037044765 scopus 로고    scopus 로고
    • Structure of the N-linked glycan present on multiple glycoproteins in the Gram-negative bacterium, Campylobacter jejuni
    • Young NM, Brisson JR, Kelly J, Watson DC, Tessier L, Lanthier PH, et al. Structure of the N-linked glycan present on multiple glycoproteins in the Gram-negative bacterium, Campylobacter jejuni. J Biol Chem 2002; 277:42530-9.
    • (2002) J Biol Chem , vol.277 , pp. 42530-42539
    • Young, N.M.1    Brisson, J.R.2    Kelly, J.3    Watson, D.C.4    Tessier, L.5    Lanthier, P.H.6
  • 5
    • 33646564396 scopus 로고    scopus 로고
    • Definition of the bacterial N-glycosylation site consensus sequence
    • Kowarik M, Young NM, Numao S, Schulz BL, Hug I, Callewaert N, et al. Definition of the bacterial N-glycosylation site consensus sequence. EMBO J 2006; 25:1957-66.
    • (2006) EMBO J , vol.25 , pp. 1957-1966
    • Kowarik, M.1    Young, N.M.2    Numao, S.3    Schulz, B.L.4    Hug, I.5    Callewaert, N.6
  • 6
    • 77955433290 scopus 로고    scopus 로고
    • Protein glycosylation in Archaea: Sweet and extreme
    • Calo D, Kaminski L, Eichler J. Protein glycosylation in Archaea: Sweet and extreme. Glycobiology 2010; 20:1065-76.
    • (2010) Glycobiology , vol.20 , pp. 1065-1076
    • Calo, D.1    Kaminski, L.2    Eichler, J.3
  • 7
    • 33646892873 scopus 로고    scopus 로고
    • Asparagine-linked protein glycosylation: From eukaryotic to prokaryotic systems
    • Weerapana E, Imperiali B. Asparagine-linked protein glycosylation: From eukaryotic to prokaryotic systems. Glycobiology 2006; 16:91-101.
    • (2006) Glycobiology , vol.16 , pp. 91-101
    • Weerapana, E.1    Imperiali, B.2
  • 8
    • 33748505442 scopus 로고    scopus 로고
    • Mass spectrometry-based glycomics strategy for exploring N-linked glycosylation in eukaryotes and bacteria
    • Liu X, McNally DJ, Nothaft H, Szymanski CM, Brisson JR, Li J. Mass spectrometry-based glycomics strategy for exploring N-linked glycosylation in eukaryotes and bacteria. Anal Chem 2006; 78:6081-7.
    • (2006) Anal Chem , vol.78 , pp. 6081-6087
    • Liu, X.1    McNally, D.J.2    Nothaft, H.3    Szymanski, C.M.4    Brisson, J.R.5    Li, J.6
  • 9
    • 70349279995 scopus 로고    scopus 로고
    • Study of free oligosaccharides derived from the bacterial N-glycosylation pathway
    • Nothaft H, Liu X, McNally DJ, Li J, Szymanski CM. Study of free oligosaccharides derived from the bacterial N-glycosylation pathway. Proc Natl Acad Sci USA 2009; 106:15019-24.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 15019-15024
    • Nothaft, H.1    Liu, X.2    McNally, D.J.3    Li, J.4    Szymanski, C.M.5
  • 10
    • 77950861521 scopus 로고    scopus 로고
    • Comparative structural biology of Eubacterial and Archaeal oligosaccharyltransferases
    • Maita N, Nyirenda J, Igura M, Kamishikiryo J, Kohda D. Comparative structural biology of Eubacterial and Archaeal oligosaccharyltransferases. J Biol Chem 2010; 285:4941-50.
    • (2010) J Biol Chem , vol.285 , pp. 4941-4950
    • Maita, N.1    Nyirenda, J.2    Igura, M.3    Kamishikiryo, J.4    Kohda, D.5
  • 11
    • 38049051311 scopus 로고    scopus 로고
    • Structure-guided identification of a new catalytic motif of oligosaccharyltransferase
    • Igura M, Maita N, Kamishikiryo J, Yamada M, Obita T, Maenaka K, et al. Structure-guided identification of a new catalytic motif of oligosaccharyltransferase. EMBO J 2008; 27:234-43.
    • (2008) EMBO J , vol.27 , pp. 234-243
    • Igura, M.1    Maita, N.2    Kamishikiryo, J.3    Yamada, M.4    Obita, T.5    Maenaka, K.6
  • 12
    • 71049170514 scopus 로고    scopus 로고
    • Identification and quantification of glycoproteins using ion-pairing normal-phase liquid chromatography and mass spectrometry
    • Ding W, Nothaft H, Szymanski CM, Kelly J. Identification and quantification of glycoproteins using ion-pairing normal-phase liquid chromatography and mass spectrometry. Mol Cell Proteomics 2009; 8:2170-85.
    • (2009) Mol Cell Proteomics , vol.8 , pp. 2170-2185
    • Ding, W.1    Nothaft, H.2    Szymanski, C.M.3    Kelly, J.4
  • 13
    • 33645228374 scopus 로고    scopus 로고
    • Biosynthesis of the N-linked glycan in Campylobacter jejuni and addition onto protein through block transfer
    • Kelly J, Jarrell H, Millar L, Tessier L, Fiori LM, Lau PC, et al. Biosynthesis of the N-linked glycan in Campylobacter jejuni and addition onto protein through block transfer. J Bacteriol 2006; 188:2427-34.
    • (2006) J Bacteriol , vol.188 , pp. 2427-2434
    • Kelly, J.1    Jarrell, H.2    Millar, L.3    Tessier, L.4    Fiori, L.M.5    Lau, P.C.6
  • 14
    • 44449138388 scopus 로고    scopus 로고
    • Salt tolerance of Arabidopsis thaliana requires maturation of N-glycosylated proteins in the Golgi apparatus
    • Kang JS, Frank J, Kang CH, Kajiura H, Vikram M, Ueda A, et al. Salt tolerance of Arabidopsis thaliana requires maturation of N-glycosylated proteins in the Golgi apparatus. Proc Natl Acad Sci USA 2008;105:5933-8.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 5933-5938
    • Kang, J.S.1    Frank, J.2    Kang, C.H.3    Kajiura, H.4    Vikram, M.5    Ueda, A.6
  • 15
    • 36248931035 scopus 로고    scopus 로고
    • Haloferax volcanii AglB and AglD are involved in N-glycosylation of the S-layer glycoprotein and proper assembly of the surface layer
    • Abu-Qarn M, Yurist-Doutsch S, Giordano A, Trauner A, Morris HR, Hitchen P, et al. Haloferax volcanii AglB and AglD are involved in N-glycosylation of the S-layer glycoprotein and proper assembly of the surface layer. J Mol Biol 2007; 374:1224-36.
    • (2007) J Mol Biol , vol.374 , pp. 1224-1236
    • Abu-Qarn, M.1    Yurist-Doutsch, S.2    Giordano, A.3    Trauner, A.4    Morris, H.R.5    Hitchen, P.6
  • 16
    • 77949520592 scopus 로고    scopus 로고
    • Periplasmic glucans isolated from Proteobacteria
    • Lee S, Cho E, Jung S. Periplasmic glucans isolated from Proteobacteria. BMB Rep 2009; 42:769-75.
    • (2009) BMB Rep , vol.42 , pp. 769-775
    • Lee, S.1    Cho, E.2    Jung, S.3
  • 17
    • 0033014719 scopus 로고    scopus 로고
    • Osmosensing by bacteria: Signals and membrane-based sensors
    • Wood JM. Osmosensing by bacteria: signals and membrane-based sensors. Microbiol Mol Biol Rev 1999; 63:230-62.
    • (1999) Microbiol Mol Biol Rev , vol.63 , pp. 230-262
    • Wood, J.M.1
  • 19
    • 49049120373 scopus 로고    scopus 로고
    • Affinity-capture tandem mass spectrometric characterization of polyprenyl-linked oligosaccharides: Tool to study protein N-glycosylation pathways
    • Reid CW, Stupak J, Chen MM, Imperiali B, Li J, Szymanski CM. Affinity-capture tandem mass spectrometric characterization of polyprenyl-linked oligosaccharides: tool to study protein N-glycosylation pathways. Anal Chem 2008; 80:5468-75.
    • (2008) Anal Chem , vol.80 , pp. 5468-5475
    • Reid, C.W.1    Stupak, J.2    Chen, M.M.3    Imperiali, B.4    Li, J.5    Szymanski, C.M.6
  • 20
    • 70449885897 scopus 로고    scopus 로고
    • Analysis of bacterial lipid-linked oligosaccharide intermediates using porous graphitic carbon liquid chromatography-electrospray ionization mass spectrometry: Heterogeneity in the polyisoprenyl carrier revealed
    • Reid CW, Stupak J, Szymanski CM, Li J. Analysis of bacterial lipid-linked oligosaccharide intermediates using porous graphitic carbon liquid chromatography-electrospray ionization mass spectrometry: heterogeneity in the polyisoprenyl carrier revealed. Anal Chem 2009; 81:8472-8.
    • (2009) Anal Chem , vol.81 , pp. 8472-8478
    • Reid, C.W.1    Stupak, J.2    Szymanski, C.M.3    Li, J.4
  • 21
    • 50249166796 scopus 로고    scopus 로고
    • N-linked Protein Glycosylation in Campylobacter
    • Nachamkin I, Szymanski CM, Blaser MJ, Eds., 3rd Edition. Washington DC: ASM Press
    • Nothaft H, Amber S, Aebi M, Szymanski CM. N-linked Protein Glycosylation in Campylobacter. In: Nachamkin I, Szymanski CM, Blaser MJ, Eds. Campylobacter, 3rd Edition. Washington DC: ASM Press 2008; 447-69.
    • (2008) Campylobacter , pp. 447-469
    • Nothaft, H.1    Amber, S.2    Aebi, M.3    Szymanski, C.M.4
  • 22
    • 14544282378 scopus 로고    scopus 로고
    • Protein glycosylation in bacterial mucosal pathogens
    • Szymanski CM, Wren BW. Protein glycosylation in bacterial mucosal pathogens. Nat Rev Microbiol 2005; 3:225-37.
    • (2005) Nat Rev Microbiol , vol.3 , pp. 225-237
    • Szymanski, C.M.1    Wren, B.W.2
  • 23
    • 4544254484 scopus 로고    scopus 로고
    • N-linked protein glycosylation is required for full competence in Campylobacter jejuni 81-176
    • Larsen JC, Szymanski C, Guerry P. N-linked protein glycosylation is required for full competence in Campylobacter jejuni 81-176. J Bacteriol 2004; 186:6508-14.
    • (2004) J Bacteriol , vol.186 , pp. 6508-6514
    • Larsen, J.C.1    Szymanski, C.2    Guerry, P.3
  • 24
    • 0032414758 scopus 로고    scopus 로고
    • Stability of the Agrobacterium tumefaciens VirB10 protein is modulated by growth temperature and periplasmic osmoadaption
    • Banta LM, Bohne J, Lovejoy SD, Dostal K. Stability of the Agrobacterium tumefaciens VirB10 protein is modulated by growth temperature and periplasmic osmoadaption. J Bacteriol 1998; 180:6597-606.
    • (1998) J Bacteriol , vol.180 , pp. 6597-6606
    • Banta, L.M.1    Bohne, J.2    Lovejoy, S.D.3    Dostal, K.4
  • 25
    • 33947362939 scopus 로고    scopus 로고
    • Osmoregulation in the periplasm
    • Ehrmann M, ed., Washington DC: American Society for Microbiology
    • Bohin JP, Lacroix JM. Osmoregulation in the periplasm. In: Ehrmann M, ed. The Periplasm. Washington DC: American Society for Microbiology 2006; 325-41.
    • (2006) The Periplasm , pp. 325-341
    • Bohin, J.P.1    Lacroix, J.M.2
  • 26
    • 72749095395 scopus 로고    scopus 로고
    • N-glycosylated proteins and distinct lipooligosaccharide glycoforms of Campylobacter jejuni target the human C-type lectin receptor MGL
    • van Sorge NM, Bleumink NM, van Vliet SJ, Saeland E, van der Pol WL, van Kooyk Y, et al. N-glycosylated proteins and distinct lipooligosaccharide glycoforms of Campylobacter jejuni target the human C-type lectin receptor MGL. Cell Microbiol 2009; 11:1768-81.
    • (2009) Cell Microbiol , vol.11 , pp. 1768-1781
    • van Sorge, N.M.1    Bleumink, N.M.2    van Vliet, S.J.3    Saeland, E.4    van der Pol, W.L.5    van Kooyk, Y.6
  • 27
    • 77958099601 scopus 로고    scopus 로고
    • Protein glycosylation in bacteria-sweeter than ever
    • Nothaft H, Szymanski CM. Protein glycosylation in bacteria-sweeter than ever. Nat Rev Microbiol 2010; 8:765-78.
    • (2010) Nat Rev Microbiol , vol.8 , pp. 765-778
    • Nothaft, H.1    Szymanski, C.M.2
  • 28
    • 34548595384 scopus 로고    scopus 로고
    • Protein glycosylation in Campylobacter jejuni: Partial suppression of pglF by mutation of pseC
    • Guerry P, Ewing CP, Schoenhofen IC, Logan SM. Protein glycosylation in Campylobacter jejuni: partial suppression of pglF by mutation of pseC. J Bacteriol 2007; 189:6731-3.
    • (2007) J Bacteriol , vol.189 , pp. 6731-6733
    • Guerry, P.1    Ewing, C.P.2    Schoenhofen, I.C.3    Logan, S.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.