메뉴 건너뛰기




Volumn 6, Issue , 2016, Pages

Erratum: Antibodies from multiple sclerosis patients preferentially recognize hyperglucosylated adhesin of non-typeable Haemophilus influenzae (Scientific Reports (2016) 6 (39430) DOI: 10.1038/srep39430);Antibodies from multiple sclerosis patients preferentially recognize hyperglucosylated adhesin of non-typeable Haemophilus influenzae

Author keywords

[No Author keywords available]

Indexed keywords

ADHESIN; ANTIBODY; ASPARAGINE; BACTERIAL ANTIGEN; GLYCOCONJUGATE; GLYCOPEPTIDE; OUTER MEMBRANE PROTEIN;

EID: 85007232679     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep44969     Document Type: Erratum
Times cited : (23)

References (52)
  • 1
    • 34548133584 scopus 로고    scopus 로고
    • Multiple sclerosis: A complicated picture of autoimmunity
    • McFarland, H. F. & Martin, R. Multiple sclerosis: a complicated picture of autoimmunity. Nat Immunol 8, 913-9 (2007).
    • (2007) Nat Immunol , vol.8 , pp. 913-919
    • McFarland, H.F.1    Martin, R.2
  • 3
    • 34247590137 scopus 로고    scopus 로고
    • Environmental risk factors for multiple sclerosis. Part I: The role of infection
    • Part II: Noninfectious factors. Ann Neurol 61, 504-13 (2007)
    • Ascherio, A. & Munger, K. L. Environmental risk factors for multiple sclerosis. Part I: the role of infection. Ann Neurol 61, 288-99 (2007), Part II: Noninfectious factors. Ann Neurol 61, 504-13 (2007).
    • (2007) Ann Neurol , vol.61 , pp. 288-299
    • Ascherio, A.1    Munger, K.L.2
  • 4
    • 84877296734 scopus 로고    scopus 로고
    • New findings and old controversies in the research of multiple sclerosis and its model experimental autoimmune encephalomyelitis
    • Aharoni, R. New findings and old controversies in the research of multiple sclerosis and its model experimental autoimmune encephalomyelitis. Expert Rev Clin Immunol 9, 423-40 (2013).
    • (2013) Expert Rev Clin Immunol , vol.9 , pp. 423-440
    • Aharoni, R.1
  • 5
    • 77954593393 scopus 로고    scopus 로고
    • Bacterial infections and the pathogenesis of autoimmune conditions
    • Sherbet, G. Bacterial Infections and the Pathogenesis of Autoimmune Conditions. Br J Med Pract 2, 6-13 (2009).
    • (2009) Br J Med Pract , vol.2 , pp. 6-13
    • Sherbet, G.1
  • 6
    • 57449091100 scopus 로고    scopus 로고
    • The role of infections in autoimmune disease
    • Ercolini, A. M. & Miller, S. D. The role of infections in autoimmune disease. Clin Exp Immunol 155, 1-15 (2009).
    • (2009) Clin Exp Immunol , vol.155 , pp. 1-15
    • Ercolini, A.M.1    Miller, S.D.2
  • 7
    • 84935704551 scopus 로고    scopus 로고
    • Antibody biomarkers in CNS demyelinating diseases - A long and winding road
    • Berger, T. & Reindl, M. Antibody biomarkers in CNS demyelinating diseases - a long and winding road. Eur J Neurol 22, 1162-8 (2015).
    • (2015) Eur J Neurol , vol.22 , pp. 1162-1168
    • Berger, T.1    Reindl, M.2
  • 8
    • 84915793365 scopus 로고    scopus 로고
    • Autoantibodies to non-myelin antigens as contributors to the pathogenesis of multiple sclerosis
    • Levin, M. C. et al. Autoantibodies to Non-myelin Antigens as Contributors to the Pathogenesis of Multiple Sclerosis. J Clin Cell Immunol 4 (2013).
    • (2013) J Clin Cell Immunol , vol.4
    • Levin, M.C.1
  • 9
    • 84908563903 scopus 로고    scopus 로고
    • Targets of the humoral autoimmune response in multiple sclerosis
    • Fraussen, J., Claes, N., de Bock, L. & Somers, V. Targets of the humoral autoimmune response in multiple sclerosis. Autoimmun Rev 13, 1126-37 (2014).
    • (2014) Autoimmun Rev , vol.13 , pp. 1126-1137
    • Fraussen, J.1    Claes, N.2    De Bock, L.3    Somers, V.4
  • 10
    • 80053300042 scopus 로고    scopus 로고
    • Antibodies to MOG are transient in childhood acute disseminated encephalomyelitis
    • Pröbstel, A. K. et al. Antibodies to MOG are transient in childhood acute disseminated encephalomyelitis. Neurology 77, 580-8 (2011).
    • (2011) Neurology , vol.77 , pp. 580-588
    • Pröbstel, A.K.1
  • 11
    • 84860720797 scopus 로고    scopus 로고
    • Glycoproteins as targets of autoantibodies in CNS inflammation: MOG and more
    • Mayer, M. C. & Meinl, E. Glycoproteins as targets of autoantibodies in CNS inflammation: MOG and more. Ther Adv Neurol Disord 5, 147-59 (2012).
    • (2012) Ther Adv Neurol Disord , vol.5 , pp. 147-159
    • Mayer, M.C.1    Meinl, E.2
  • 12
    • 84881368722 scopus 로고    scopus 로고
    • The spectrum of MOG autoantibody-associated demyelinating diseases
    • Reindl, M., Di Pauli, F., Rostásy, K. & Berger, T. The spectrum of MOG autoantibody-associated demyelinating diseases. Nat Rev Neurol 9, 455-61 (2013).
    • (2013) Nat Rev Neurol , vol.9 , pp. 455-461
    • Reindl, M.1    Di Pauli, F.2    Rostásy, K.3    Berger, T.4
  • 13
    • 0033579860 scopus 로고    scopus 로고
    • A synthetic glycopeptide of human myelin oligodendrocyte glycoprotein to detect antibody responses in multiple sclerosis and other neurological diseases
    • Mazzucco, S. et al. A synthetic glycopeptide of human myelin oligodendrocyte glycoprotein to detect antibody responses in multiple sclerosis and other neurological diseases. Bioorg Med Chem Lett 9, 167-72 (1999).
    • (1999) Bioorg Med Chem Lett , vol.9 , pp. 167-172
    • Mazzucco, S.1
  • 14
    • 22544448364 scopus 로고    scopus 로고
    • An N-glucosylated peptide detecting disease-specific autoantibodies, biomarkers of multiple sclerosis
    • Lolli, F. et al. An N-glucosylated peptide detecting disease-specific autoantibodies, biomarkers of multiple sclerosis. Proc Natl Acad Sci USA 102, 10273-8 (2005).
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 10273-10278
    • Lolli, F.1
  • 15
    • 24144443537 scopus 로고    scopus 로고
    • The glycopeptide CSF114(Glc) detects serum antibodies in multiple sclerosis
    • Lolli, F. et al. The glycopeptide CSF114(Glc) detects serum antibodies in multiple sclerosis. J Neuroimmunol 167, 131-7 (2005).
    • (2005) J Neuroimmunol , vol.167 , pp. 131-137
    • Lolli, F.1
  • 16
    • 84861544418 scopus 로고    scopus 로고
    • Glycopeptide-based antibody detection in multiple sclerosis by surface plasmon resonance
    • Real-Fernández, F. et al. Glycopeptide-based antibody detection in multiple sclerosis by surface plasmon resonance. Sensors (Basel) 12, 5596-607 (2012).
    • (2012) Sensors (Basel) , vol.12 , pp. 5596-5607
    • Real-Fernández, F.1
  • 17
    • 51849095900 scopus 로고    scopus 로고
    • Designed glycopeptides with different beta-turn types as synthetic probes for the detection of autoantibodies as biomarkers of multiple sclerosis
    • Carotenuto, A. et al. Designed glycopeptides with different beta-turn types as synthetic probes for the detection of autoantibodies as biomarkers of multiple sclerosis. J Med Chem 51, 5304-9 (2008).
    • (2008) J Med Chem , vol.51 , pp. 5304-5309
    • Carotenuto, A.1
  • 18
    • 0028222069 scopus 로고
    • Novel N-glycosylation in eukaryotes: Laminin contains the linkage unit betaglucosylasparagine
    • Schreiner, R., Schnabel, E. & Wieland, F. Novel N-glycosylation in eukaryotes: laminin contains the linkage unit betaglucosylasparagine. J Cell Biol 124, 1071-81 (1994).
    • (1994) J Cell Biol , vol.124 , pp. 1071-1081
    • Schreiner, R.1    Schnabel, E.2    Wieland, F.3
  • 19
    • 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 20, 1065-76 (2010).
    • (2010) Glycobiology , vol.20 , pp. 1065-1076
    • Calo, D.1    Kaminski, L.2    Eichler, J.3
  • 20
    • 0142028206 scopus 로고    scopus 로고
    • Is Devic's neuromyelitis optica a separate disease? A comparative study with multiple sclerosis
    • de Seze, J. et al. Is Devic's neuromyelitis optica a separate disease? A comparative study with multiple sclerosis. Mult Scler 9, 521-5 (2003)
    • (2003) Mult Scler , vol.9 , pp. 521-525
    • De Seze, J.1
  • 21
    • 55749088210 scopus 로고    scopus 로고
    • Antibody to aquaporin-4 in the long-term course of neuromyelitis optica
    • Jarius, S. et al. Antibody to aquaporin-4 in the long-term course of neuromyelitis optica. Brain 131, 3072-80 (2008)
    • (2008) Brain , vol.131 , pp. 3072-3080
    • Jarius, S.1
  • 22
    • 84930818143 scopus 로고    scopus 로고
    • Sugar coating: Bacterial protein glycosylation and host-microbe interactions
    • Tan, F. Y., Tang, C. M. & Exley, R. M. Sugar coating: bacterial protein glycosylation and host-microbe interactions. Trends Biochem Sci 40, 342-50 (2015).
    • (2015) Trends Biochem Sci , vol.40 , pp. 342-350
    • Tan, F.Y.1    Tang, C.M.2    Exley, R.M.3
  • 23
    • 0037673430 scopus 로고    scopus 로고
    • The Haemophilus influenzae HMW1 adhesin is glycosylated in a process that requires HMW1C and phosphoglucomutase, an enzyme involved in lipooligosaccharide biosynthesis
    • Grass, S. et al. The Haemophilus influenzae HMW1 adhesin is glycosylated in a process that requires HMW1C and phosphoglucomutase, an enzyme involved in lipooligosaccharide biosynthesis. Mol Microbiol 48, 737-51 (2003).
    • (2003) Mol Microbiol , vol.48 , pp. 737-751
    • Grass, S.1
  • 24
    • 54449094921 scopus 로고    scopus 로고
    • The Haemophilus influenzae HMW1 adhesin is a glycoprotein with an unusual N-linked carbohydrate modification
    • Gross, J. et al. The Haemophilus influenzae HMW1 adhesin is a glycoprotein with an unusual N-linked carbohydrate modification. J Biol Chem 283, 26010-5 (2008).
    • (2008) J Biol Chem , vol.283 , pp. 26010-26015
    • Gross, J.1
  • 25
    • 80055095714 scopus 로고    scopus 로고
    • Structural insights into the glycosyltransferase activity of the Actinobacillus pleuropneumoniae HMW1C-like protein
    • Kawai, F. et al. Structural insights into the glycosyltransferase activity of the Actinobacillus pleuropneumoniae HMW1C-like protein. J Biol Chem 286, 38546-57 (2011).
    • (2011) J Biol Chem , vol.286 , pp. 38546-38557
    • Kawai, F.1
  • 26
    • 84906875240 scopus 로고    scopus 로고
    • Substrate specificity of cytoplasmic N-glycosyltransferase
    • Naegeli, A. et al. Substrate specificity of cytoplasmic N-glycosyltransferase. J Biol Chem 289, 24521-32 (2014).
    • (2014) J Biol Chem , vol.289 , pp. 24521-24532
    • Naegeli, A.1
  • 27
    • 80053392394 scopus 로고    scopus 로고
    • Cytoplasmic N-glycosyltransferase of Actinobacillus pleuropneumoniae is an inverting enzyme and recognizes the NX(S/T) consensus sequence
    • Schwarz, F., Fan, Y. Y., Schubert, M. & Aebi, M. Cytoplasmic N-glycosyltransferase of Actinobacillus pleuropneumoniae is an inverting enzyme and recognizes the NX(S/T) consensus sequence. J Biol Chem 286, 35267-74 (2011).
    • (2011) J Biol Chem , vol.286 , pp. 35267-35274
    • Schwarz, F.1    Fan, Y.Y.2    Schubert, M.3    Aebi, M.4
  • 28
    • 78651248164 scopus 로고    scopus 로고
    • The Actinobacillus pleuropneumoniae HMW1C-like glycosyltransferase mediates N-linked glycosylation of the Haemophilus influenzae HMW1 adhesin
    • Choi, K. J., Grass, S., Paek, S. St, Geme, J. W. & Yeo, H. J. The Actinobacillus pleuropneumoniae HMW1C-like glycosyltransferase mediates N-linked glycosylation of the Haemophilus influenzae HMW1 adhesin. PLoS One 5, e15888 (2010).
    • (2010) PLoS One , vol.5 , pp. e15888
    • Choi, K.J.1    Grass, S.2    Paek, S.3    St Geme, J.W.4    Yeo, H.J.5
  • 29
    • 84925156346 scopus 로고    scopus 로고
    • The I-TASSER Suite: Protein structure and function prediction
    • Yang, J. et al. The I-TASSER Suite: protein structure and function prediction. Nat Methods 12, 7-8 (2015).
    • (2015) Nat Methods , vol.12 , pp. 7-8
    • Yang, J.1
  • 30
    • 39449115394 scopus 로고    scopus 로고
    • I-TASSER server for protein 3D structure prediction
    • Zhang, Y. I-TASSER server for protein 3D structure prediction. BMC Bioinformatics 9, 40 (2008).
    • (2008) BMC Bioinformatics , vol.9 , pp. 40
    • Zhang, Y.1
  • 31
    • 77954080496 scopus 로고    scopus 로고
    • The Haemophilus influenzae HMW1C protein is a glycosyltransferase that transfers hexose residues to asparagine sites in the HMW1 adhesin
    • Grass, S., Lichti, C. F., Townsend, R. R., Gross, J. & St Geme, J. W. The Haemophilus influenzae HMW1C protein is a glycosyltransferase that transfers hexose residues to asparagine sites in the HMW1 adhesin. PLoS Pathog 6, e1000919 (2010).
    • (2010) PLoS Pathog , vol.6 , pp. e1000919
    • Grass, S.1    Lichti, C.F.2    Townsend, R.R.3    Gross, J.4    St Geme, J.W.5
  • 32
    • 84896316200 scopus 로고    scopus 로고
    • Selection against glycosylation sites in potential target proteins of the general HMWC N-glycosyltransferase in Haemophilus influenzae
    • Gawthorne, J. A. et al. Selection against glycosylation sites in potential target proteins of the general HMWC N-glycosyltransferase in Haemophilus influenzae. Biochem Biophys Res Commun 445, 633-8 (2014).
    • (2014) Biochem Biophys Res Commun , vol.445 , pp. 633-638
    • Gawthorne, J.A.1
  • 33
    • 84893152008 scopus 로고    scopus 로고
    • Molecular analysis of an alternative N-glycosylation machinery by functional transfer from Actinobacillus pleuropneumoniae to Escherichia coli
    • Naegeli, A. et al. Molecular analysis of an alternative N-glycosylation machinery by functional transfer from Actinobacillus pleuropneumoniae to Escherichia coli. J Biol Chem 289, 2170-9 (2014).
    • (2014) J Biol Chem , vol.289 , pp. 2170-2179
    • Naegeli, A.1
  • 34
    • 33646027294 scopus 로고    scopus 로고
    • Engineering the E. Coli UDP-glucose synthesis pathway for oligosaccharide synthesis
    • Mao, Z., Shin, H. D. & Chen, R. R. Engineering the E. coli UDP-glucose synthesis pathway for oligosaccharide synthesis. Biotechnol Prog 22, 369-74 (2006).
    • (2006) Biotechnol Prog , vol.22 , pp. 369-374
    • Mao, Z.1    Shin, H.D.2    Chen, R.R.3
  • 35
    • 0023869530 scopus 로고
    • An inhibition enzyme immunoassay for estimating relative antibody affinity and affinity heterogeneity
    • Rath, S., Stanley, C. M. & Steward, M. W. An inhibition enzyme immunoassay for estimating relative antibody affinity and affinity heterogeneity. J Immunol Methods 106, 245-9 (1988).
    • (1988) J Immunol Methods , vol.106 , pp. 245-249
    • Rath, S.1    Stanley, C.M.2    Steward, M.W.3
  • 36
    • 80755139618 scopus 로고    scopus 로고
    • Distinct pathological patterns in relapsing-remitting and chronic models of experimental autoimmune enchephalomyelitis and the neuroprotective effect of glatiramer acetate
    • Aharoni, R. et al. Distinct pathological patterns in relapsing-remitting and chronic models of experimental autoimmune enchephalomyelitis and the neuroprotective effect of glatiramer acetate. J Autoimmun 37, 228-41 (2011).
    • (2011) J Autoimmun , vol.37 , pp. 228-241
    • Aharoni, R.1
  • 37
    • 33745243275 scopus 로고    scopus 로고
    • Bacterial glycoproteomics
    • Hitchen, P. G. & Dell, A. Bacterial glycoproteomics. Microbiology 152, 1575-80 (2006).
    • (2006) Microbiology , vol.152 , pp. 1575-1580
    • Hitchen, P.G.1    Dell, A.2
  • 38
    • 77957267813 scopus 로고    scopus 로고
    • Glycoproteomics: A powerful tool for characterizing the diverse glycoforms of bacterial pilins and flagellins
    • Hitchen, P. G. et al. Glycoproteomics: a powerful tool for characterizing the diverse glycoforms of bacterial pilins and flagellins. Biochem Soc Trans 38, 1307-13 (2010).
    • (2010) Biochem Soc Trans , vol.38 , pp. 1307-1313
    • Hitchen, P.G.1
  • 39
    • 60549092317 scopus 로고    scopus 로고
    • Bioanalytical tools for the discovery of eukaryotic glycoproteins applied to the analysis of bacterial glycoproteins
    • Balonova, L., Hernychova, L. & Bilkova, Z. Bioanalytical tools for the discovery of eukaryotic glycoproteins applied to the analysis of bacterial glycoproteins. Expert Rev Proteomics 6, 75-85 (2009).
    • (2009) Expert Rev Proteomics , vol.6 , pp. 75-85
    • Balonova, L.1    Hernychova, L.2    Bilkova, Z.3
  • 40
    • 77950672706 scopus 로고    scopus 로고
    • Multimethodological approach to identification of glycoproteins from the proteome of Francisella tularensis, an intracellular microorganism
    • Balonova, L. et al. Multimethodological approach to identification of glycoproteins from the proteome of Francisella tularensis, an intracellular microorganism. J Proteome Res 9, 1995-2005 (2010).
    • (2010) J Proteome Res , vol.9 , pp. 1995-2005
    • Balonova, L.1
  • 41
    • 0345059167 scopus 로고    scopus 로고
    • Sweet new world: Glycoproteins in bacterial pathogens
    • Schmidt, M. A., Riley, L. W. & Benz, I. Sweet new world: glycoproteins in bacterial pathogens. Trends Microbiol 11, 554-61 (2003).
    • (2003) Trends Microbiol , vol.11 , pp. 554-561
    • Schmidt, M.A.1    Riley, L.W.2    Benz, I.3
  • 42
    • 0034818302 scopus 로고    scopus 로고
    • Purification and structure elucidation of the N-acetylbacillosamine-containing polysaccharide from Bacillus licheniformis ATCC 9945
    • Schäffer, C. et al. Purification and structure elucidation of the N-acetylbacillosamine-containing polysaccharide from Bacillus licheniformis ATCC 9945. Eur J Biochem 268, 857-64 (2001).
    • (2001) Eur J Biochem , vol.268 , pp. 857-864
    • Schäffer, C.1
  • 43
    • 67349272331 scopus 로고    scopus 로고
    • Glycoproteomics: Past, present and future
    • Tissot, B. et al. Glycoproteomics: past, present and future. FEBS Lett 583, 1728-35 (2009).
    • (2009) FEBS Lett , vol.583 , pp. 1728-1735
    • Tissot, B.1
  • 44
    • 33845398313 scopus 로고    scopus 로고
    • Identification of labile UDP-ketosugars in Helicobacter pylori, Campylobacter jejuni and Pseudomonas aeruginosa: Key metabolites used to make glycan virulence factors
    • McNally, D. J. et al. Identification of labile UDP-ketosugars in Helicobacter pylori, Campylobacter jejuni and Pseudomonas aeruginosa: key metabolites used to make glycan virulence factors. Chembiochem 7, 1865-8 (2006).
    • (2006) Chembiochem , vol.7 , pp. 1865-1868
    • McNally, D.J.1
  • 45
    • 33748155285 scopus 로고    scopus 로고
    • Bacterial glycans: Key mediators of diverse host immune responses
    • Comstock, L. E. & Kasper, D. L. Bacterial glycans: key mediators of diverse host immune responses. Cell 126, 847-50 (2006).
    • (2006) Cell , vol.126 , pp. 847-850
    • Comstock, L.E.1    Kasper, D.L.2
  • 46
    • 34548028239 scopus 로고    scopus 로고
    • Campylobacter jejuni: Molecular biology and pathogenesis
    • Young, K. T., Davis, L. M. & Dirita, V. J. Campylobacter jejuni: molecular biology and pathogenesis. Nat Rev Microbiol 5, 665-79 (2007).
    • (2007) Nat Rev Microbiol , vol.5 , pp. 665-679
    • Young, K.T.1    Davis, L.M.2    Dirita, V.J.3
  • 47
    • 27644558148 scopus 로고    scopus 로고
    • Guillain-Barré syndrome
    • Hughes, R. A. & Cornblath, D. R. Guillain-Barré syndrome. Lancet 366, 1653-66 (2005).
    • (2005) Lancet , vol.366 , pp. 1653-1666
    • Hughes, R.A.1    Cornblath, D.R.2
  • 48
    • 3843114339 scopus 로고    scopus 로고
    • Carbohydrate mimicry between human ganglioside GM1 and Campylobacter jejuni lipooligosaccharide causes Guillain-Barre syndrome
    • Yuki, N. et al. Carbohydrate mimicry between human ganglioside GM1 and Campylobacter jejuni lipooligosaccharide causes Guillain-Barre syndrome. Proc Natl Acad Sci USA 101, 11404-9 (2004).
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 11404-11409
    • Yuki, N.1
  • 49
    • 85007223819 scopus 로고    scopus 로고
    • New type of encephalomyelitis responsive to trimethoprim/sulfamethoxazole treatment in Japan
    • Sakiyama, Y. et al. New type of encephalomyelitis responsive to trimethoprim/sulfamethoxazole treatment in Japan. Neurol Neuroimmunol Neuroinflamm 13, e143 (2015).
    • (2015) Neurol Neuroimmunol Neuroinflamm , vol.13 , pp. e143
    • Sakiyama, Y.1
  • 50
  • 51
    • 84964820947 scopus 로고    scopus 로고
    • Microbes and Alzheimer's diseases
    • Itzhaki, R. F. et al. Microbes and Alzheimer's Diseases. J Alzheimers Dis 51, 979-84 (2016).
    • (2016) J Alzheimers Dis , vol.51 , pp. 979-984
    • Itzhaki, R.F.1
  • 52
    • 79952501096 scopus 로고    scopus 로고
    • Diagnostic criteria for multiple sclerosis: 2010 revisions to the McDonald criteria
    • Polman, C. H. et al. Diagnostic criteria for multiple sclerosis: 2010 revisions to the McDonald criteria. Ann Neurol 69, 292-302 (2011).
    • (2011) Ann Neurol , vol.69 , pp. 292-302
    • Polman, C.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.