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Volumn 15, Issue 16, 2015, Pages 2733-2745

Comprehensive mapping of O-glycosylation in flagellin from Campylobacter jejuni 11168: A multienzyme differential ion mobility mass spectrometry approach

Author keywords

Campylobacter jejuni 11168; Flagellin A; Glycoproteomics; Glycosylation; LC FAIMS MS MS; Proteinase K; Trypsin

Indexed keywords

FLAGELLIN; PROTEINASE K; TRYPSIN; PEPTIDE FRAGMENT;

EID: 84938598488     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201400533     Document Type: Article
Times cited : (30)

References (26)
  • 1
    • 34250830856 scopus 로고    scopus 로고
    • Campylobacters as zoonotic pathogens: a food production perspective
    • Humphrey, T., O'Brien, S., Madsen, M., Campylobacters as zoonotic pathogens: a food production perspective. Int. J. Food Microbiol. 2007, 117, 237-257.
    • (2007) Int. J. Food Microbiol. , vol.117 , pp. 237-257
    • Humphrey, T.1    O'Brien, S.2    Madsen, M.3
  • 3
    • 84861802711 scopus 로고    scopus 로고
    • Public health burden due to infections by verocytotoxin-producing Escherichia coli (VTEC) and Campylobacter spp. as estimated by cost of illness and different approaches to model disability-adjusted life years
    • Toljander, J., Dovarn, A., Andersson, Y., Ivarsson, S., Lindqvist, R., Public health burden due to infections by verocytotoxin-producing Escherichia coli (VTEC) and Campylobacter spp. as estimated by cost of illness and different approaches to model disability-adjusted life years. Scand. J. Public Health 2012, 40, 294-302.
    • (2012) Scand. J. Public Health , vol.40 , pp. 294-302
    • Toljander, J.1    Dovarn, A.2    Andersson, Y.3    Ivarsson, S.4    Lindqvist, R.5
  • 4
    • 0041766677 scopus 로고    scopus 로고
    • Guillain-Barre syndrome associated with Campylobacter jejuni infection in England, 2000-2001
    • Tam, C. C., Rodrigues, L. C., O'Brien, S. J., Guillain-Barre syndrome associated with Campylobacter jejuni infection in England, 2000-2001. Clin. Infect. Dis. 2003, 37, 307-310.
    • (2003) Clin. Infect. Dis. , vol.37 , pp. 307-310
    • Tam, C.C.1    Rodrigues, L.C.2    O'Brien, S.J.3
  • 5
    • 0027234632 scopus 로고
    • Colonization of chicks by motility mutants of Campylobacter jejuni demonstrates the importance of flagellin A expression
    • Wassenaar, T. M., vander Zeijst, B. A., Ayling, R., Newell, D. G., Colonization of chicks by motility mutants of Campylobacter jejuni demonstrates the importance of flagellin A expression. J. Gen. Microbiol. 1993, 139, 1171-1175.
    • (1993) J. Gen. Microbiol. , vol.139 , pp. 1171-1175
    • Wassenaar, T.M.1    van der Zeijst, B.A.2    Ayling, R.3    Newell, D.G.4
  • 6
    • 0027287847 scopus 로고
    • Role of Campylobacter jejuni flagella as colonization factors for three-day-old chicks: analysis with flagellar mutants
    • Nachamkin, I., Yang, X. H., Stern, N. J., Role of Campylobacter jejuni flagella as colonization factors for three-day-old chicks: analysis with flagellar mutants. Appl. Environ. Microbiol. 1993, 59, 1269-1273.
    • (1993) Appl. Environ. Microbiol. , vol.59 , pp. 1269-1273
    • Nachamkin, I.1    Yang, X.H.2    Stern, N.J.3
  • 8
    • 84906938225 scopus 로고    scopus 로고
    • Flagellar biosynthesis exerts temporal regulation of secretion of specific Campylobacter jejuni colonization and virulence determinants
    • Barrero-Tobon, A. M., Hendrixson, D. R., Flagellar biosynthesis exerts temporal regulation of secretion of specific Campylobacter jejuni colonization and virulence determinants. Mol. Microbiol. 2014, 93, 957-974.
    • (2014) Mol. Microbiol. , vol.93 , pp. 957-974
    • Barrero-Tobon, A.M.1    Hendrixson, D.R.2
  • 9
    • 0030712233 scopus 로고    scopus 로고
    • Nonlipopolysaccharide surface antigens of Campylobacter species
    • Guerry, P., Nonlipopolysaccharide surface antigens of Campylobacter species. J. Infect. Dis. 1997, 176, S122-S124.
    • (1997) J. Infect. Dis. , vol.176 , pp. S122-S124
    • Guerry, P.1
  • 10
    • 33746104102 scopus 로고    scopus 로고
    • Phase-variable surface structures are required for infection of Campylobacter jejuni by bacteriophages
    • Coward, C., Grant, A. J., Swift, C., Philp, J. et al., Phase-variable surface structures are required for infection of Campylobacter jejuni by bacteriophages. Appl. Environ. Microbiol. 2006, 72, 4638-4647.
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 4638-4647
    • Coward, C.1    Grant, A.J.2    Swift, C.3    Philp, J.4
  • 11
    • 84919343020 scopus 로고    scopus 로고
    • A receptor binding protein of Campylobacter jejuni bacteriophage NCTC 12673 recognizes flagellin glycosylated with acetamidino-modified pseudaminic acid
    • Javed, M. A., vanAlphen, L. B., Sacher, J., Ding, W. et al., A receptor binding protein of Campylobacter jejuni bacteriophage NCTC 12673 recognizes flagellin glycosylated with acetamidino-modified pseudaminic acid. Mol. Microbiol. 2015, 95, 101-115.
    • (2015) Mol. Microbiol. , vol.95 , pp. 101-115
    • Javed, M.A.1    van Alphen, L.B.2    Sacher, J.3    Ding, W.4
  • 12
    • 0037674764 scopus 로고    scopus 로고
    • Campylobacter-a tale of two protein glycosylation systems
    • Szymanski, C. M., Logan, S. M., Linton, D., Wren, B. W., Campylobacter-a tale of two protein glycosylation systems. Trends Microbiol. 2003, 11, 233-238.
    • (2003) Trends Microbiol. , vol.11 , pp. 233-238
    • Szymanski, C.M.1    Logan, S.M.2    Linton, D.3    Wren, B.W.4
  • 13
    • 0035860764 scopus 로고    scopus 로고
    • Identification of the carbohydrate moieties and glycosylation motifs in Campylobacter jejuni flagellin
    • Thibault, P., Logan, S. M., Kelly, J. F., Brisson, J. R. et al., Identification of the carbohydrate moieties and glycosylation motifs in Campylobacter jejuni flagellin. J. Biol. Chem. 2001, 276, 34862-34870.
    • (2001) J. Biol. Chem. , vol.276 , pp. 34862-34870
    • Thibault, P.1    Logan, S.M.2    Kelly, J.F.3    Brisson, J.R.4
  • 14
    • 70350445517 scopus 로고    scopus 로고
    • Functional characterization of flagellin glycosylation in Campylobacter jejuni 81-176
    • Ewing, C. P., Andreishcheva, E., Guerry, P., Functional characterization of flagellin glycosylation in Campylobacter jejuni 81-176. J. Bacteriol. 2009, 191, 7086-7093.
    • (2009) J. Bacteriol. , vol.191 , pp. 7086-7093
    • Ewing, C.P.1    Andreishcheva, E.2    Guerry, P.3
  • 15
    • 79952424076 scopus 로고    scopus 로고
    • Novel glycosylation sites localized in Campylobacter jejuni flagellin FlaA by liquid chromatography electron capture dissociation tandem mass spectrometry
    • Zampronio, C. G., Blackwell, G., Penn, C. W., Cooper, H. J., Novel glycosylation sites localized in Campylobacter jejuni flagellin FlaA by liquid chromatography electron capture dissociation tandem mass spectrometry. J. Proteome Res. 2011, 10, 1238-1245.
    • (2011) J. Proteome Res. , vol.10 , pp. 1238-1245
    • Zampronio, C.G.1    Blackwell, G.2    Penn, C.W.3    Cooper, H.J.4
  • 16
    • 0035860764 scopus 로고    scopus 로고
    • Identification of the carbohydrate moieties and glycosylation motifs in Campylobacter jejuni flagellin
    • Thibault, P., Logan, S. M., Kelly, J. F., Brisson, J. R. et al., Identification of the carbohydrate moieties and glycosylation motifs in Campylobacter jejuni flagellin. J. Biol. Chem. 2001, 276, 34862-34870.
    • (2001) J. Biol. Chem. , vol.276 , pp. 34862-34870
    • Thibault, P.1    Logan, S.M.2    Kelly, J.F.3    Brisson, J.R.4
  • 17
    • 34347231618 scopus 로고    scopus 로고
    • Targeted metabolomics analysis of Campylobacter coli VC167 reveals legionaminic acid derivatives as novel flagellar glycans
    • McNally, D. J., Aubry, A. J., Hui, J. P. M., Khieu, N. H. et al., Targeted metabolomics analysis of Campylobacter coli VC167 reveals legionaminic acid derivatives as novel flagellar glycans. J. Biol. Chem. 2007, 282, 144463-144475.
    • (2007) J. Biol. Chem. , vol.282 , pp. 144463-144475
    • McNally, D.J.1    Aubry, A.J.2    Hui, J.P.M.3    Khieu, N.H.4
  • 18
    • 79952424076 scopus 로고    scopus 로고
    • Novel glycosylation sites localized in Campylobacter jejuni flagellin FlaA by liquid chromatography ECD tandem mass spectrometry
    • Zampronio, C. G., Blackwell, G., Penn, C. W., Cooper, H. J., Novel glycosylation sites localized in Campylobacter jejuni flagellin FlaA by liquid chromatography ECD tandem mass spectrometry. J. Proteome Res. 2011, 10, 1238-1245.
    • (2011) J. Proteome Res. , vol.10 , pp. 1238-1245
    • Zampronio, C.G.1    Blackwell, G.2    Penn, C.W.3    Cooper, H.J.4
  • 19
    • 58849107677 scopus 로고    scopus 로고
    • Identification of novel carbohydrate modifications in Campylobacter jejuni 11168 flagellin using metabolomics-based approaches
    • Logan, S. M., Hui, J. P. M., Vinogradov, E., Aubry, A. J. et al., Identification of novel carbohydrate modifications in Campylobacter jejuni 11168 flagellin using metabolomics-based approaches. FEBS J. 2009, 276, 1014-1023.
    • (2009) FEBS J. , vol.276 , pp. 1014-1023
    • Logan, S.M.1    Hui, J.P.M.2    Vinogradov, E.3    Aubry, A.J.4
  • 21
    • 14944367556 scopus 로고    scopus 로고
    • Characterization of gel-separated glycoproteins using two-step proteolytic digestion combined with sequential microcolumns and mass spectrometry
    • Larsen, M. R., Hojrup, P., Roepstorff, P., Characterization of gel-separated glycoproteins using two-step proteolytic digestion combined with sequential microcolumns and mass spectrometry. Mol. Cell. Proteomics 2005, 4, 107-119.
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 107-119
    • Larsen, M.R.1    Hojrup, P.2    Roepstorff, P.3
  • 22
    • 77950834205 scopus 로고    scopus 로고
    • Protein glycosylation analysis by HILIC-LC-MS of proteinase K-generated N- and O-glycopeptides
    • Zauner, G., Koeleman, C. A. M., Deelder, A. M., Wuhrer, M., Protein glycosylation analysis by HILIC-LC-MS of proteinase K-generated N- and O-glycopeptides. J. Sep. Sci. 2010, 33, 903-910.
    • (2010) J. Sep. Sci. , vol.33 , pp. 903-910
    • Zauner, G.1    Koeleman, C.A.M.2    Deelder, A.M.3    Wuhrer, M.4
  • 24
    • 67650364357 scopus 로고    scopus 로고
    • Enhanced sensitivity in proteomics experiments using FAIMS coupled with a hybrid linear ion trap/orbitrap mass spectrometer
    • Saba, J., Bonneil, E., Pomies, C., Eng, K., Thibault, P., Enhanced sensitivity in proteomics experiments using FAIMS coupled with a hybrid linear ion trap/orbitrap mass spectrometer. J. Proteome Res. 2009, 8, 3355-3366.
    • (2009) J. Proteome Res. , vol.8 , pp. 3355-3366
    • Saba, J.1    Bonneil, E.2    Pomies, C.3    Eng, K.4    Thibault, P.5
  • 25
    • 84859840487 scopus 로고    scopus 로고
    • Nanospray FAIMS fractionation provides significant increases in proteome coverage of unfractionated complex protein digests
    • Swearingen, K. E., Hoopmann, M. R., Johnson, R. S., Saleem, R. A. et al., Nanospray FAIMS fractionation provides significant increases in proteome coverage of unfractionated complex protein digests. Mol. Cell Proteomics 2011, 11, doi: 10.1074/mcp.M111.014985.
    • (2011) Mol. Cell Proteomics , vol.11
    • Swearingen, K.E.1    Hoopmann, M.R.2    Johnson, R.S.3    Saleem, R.A.4
  • 26
    • 84857872572 scopus 로고    scopus 로고
    • The separation and identification of isomeric glycopeptides by high field symmetric waveform ion mobility spectrometry
    • Creese, A. J., Cooper, H. J., The separation and identification of isomeric glycopeptides by high field symmetric waveform ion mobility spectrometry. Anal. Chem. 2012, 84, 2597-2601.
    • (2012) Anal. Chem. , vol.84 , pp. 2597-2601
    • Creese, A.J.1    Cooper, H.J.2


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