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Volumn 48, Issue 11, 2013, Pages 1199-1206

A combined mass spectrometry strategy for complete posttranslational modification mapping of Neisseria meningitidis major pilin

Author keywords

Accurate mass profiling; FT ICR; pathogenic Neisseria; Posttranslational Modification; type IV pili

Indexed keywords

ACCURATE MASS; FT-ICR; IV PILI; PATHOGENIC NEISSERIA; POST-TRANSLATIONAL MODIFICATIONS;

EID: 84888161922     PISSN: 10765174     EISSN: 10969888     Source Type: Journal    
DOI: 10.1002/jms.3262     Document Type: Article
Times cited : (12)

References (31)
  • 1
    • 84856100146 scopus 로고    scopus 로고
    • Vascular colonization by Neisseria meningitidis
    • K. Melican, G. Dumenil,. Vascular colonization by Neisseria meningitidis. Curr. Opin. Microbiol. 2012, 15, 50.
    • (2012) Curr. Opin. Microbiol. , vol.15 , pp. 50
    • Melican, K.1    Dumenil, G.2
  • 3
    • 5644295324 scopus 로고    scopus 로고
    • The molecular mechanisms used by Neisseria gonorrhoeae to initiate infection differ between men and women
    • J. L. Edwards, M. A. Apicella,. The molecular mechanisms used by Neisseria gonorrhoeae to initiate infection differ between men and women. Clin. Microbiol. Rev. 2004, 17, 965.
    • (2004) Clin. Microbiol. Rev. , vol.17 , pp. 965
    • Edwards, J.L.1    Apicella, M.A.2
  • 4
    • 0015589995 scopus 로고
    • Studies on gonococcus infection 4. Pili - Their role in attachment of gonococci to tissue-culture cells
    • J. Swanson,. Studies on gonococcus infection 4. Pili-their role in attachment of gonococci to tissue-culture cells. J. Exp. Med. 1973, 137, 571.
    • (1973) J. Exp. Med. , vol.137 , pp. 571
    • Swanson, J.1
  • 8
    • 0031695884 scopus 로고    scopus 로고
    • The phosphorylcholine epitope undergoes phase variation on a 43-kilodalton protein in Pseudomonas aeruginosa and on pili of Neisseria meningitidis and Neisseria gonorrhoeae
    • J. N. Weiser, J. B. Goldberg, N. Pan, L. Wilson, M. Virji,. The phosphorylcholine epitope undergoes phase variation on a 43-kilodalton protein in Pseudomonas aeruginosa and on pili of Neisseria meningitidis and Neisseria gonorrhoeae. Infect. Immun. 1998, 66, 4263.
    • (1998) Infect. Immun. , vol.66 , pp. 4263
    • Weiser, J.N.1    Goldberg, J.B.2    Pan, N.3    Wilson, L.4    Virji, M.5
  • 9
    • 33748792256 scopus 로고    scopus 로고
    • Neisseria gonorrhoeae type IV pili undergo multisite, hierarchical modifications with phosphoethanolamine and phosphocholine requiring an enzyme structurally related to lipopolysaccharide phosphoethanolamine transferases
    • F. E. Aas, W. Egge-Jacobsen, H. C. Winther-Larsen, C. Lovold, P. G. Hitchen, A. Dell, M. Koomey,. Neisseria gonorrhoeae type IV pili undergo multisite, hierarchical modifications with phosphoethanolamine and phosphocholine requiring an enzyme structurally related to lipopolysaccharide phosphoethanolamine transferases. J. Biol. Chem. 2006, 281, 27712.
    • (2006) J. Biol. Chem. , vol.281 , pp. 27712
    • Aas, F.E.1    Egge-Jacobsen, W.2    Winther-Larsen, H.C.3    Lovold, C.4    Hitchen, P.G.5    Dell, A.6    Koomey, M.7
  • 12
    • 0032905128 scopus 로고    scopus 로고
    • Crystallographic structure reveals phosphorylated pilin from Neisseria: Phosphoserine sites modify type IV pilus surface chemistry and fibre morphology
    • K. T. Forest, S. A. Dunham, M. Koomey, J. A. Tainer,. Crystallographic structure reveals phosphorylated pilin from Neisseria: phosphoserine sites modify type IV pilus surface chemistry and fibre morphology. Mol. Microbiol. 1999, 31, 743.
    • (1999) Mol. Microbiol. , vol.31 , pp. 743
    • Forest, K.T.1    Dunham, S.A.2    Koomey, M.3    Tainer, J.A.4
  • 15
    • 77952556110 scopus 로고    scopus 로고
    • Genetic, structural, and antigenic analyses of glycan diversity in the O-linked protein glycosylation systems of human neisseria species
    • B. Borud, F. E. Aas, A. Vik, H. C. Winther-Larsen, W. Egge-Jacobsen, M. Koomey,. Genetic, structural, and antigenic analyses of glycan diversity in the O-linked protein glycosylation systems of human neisseria species. J. Bacteriol. 2010, 192, 2816.
    • (2010) J. Bacteriol. , vol.192 , pp. 2816
    • Borud, B.1    Aas, F.E.2    Vik, A.3    Winther-Larsen, H.C.4    Egge-Jacobsen, W.5    Koomey, M.6
  • 16
    • 84878514516 scopus 로고    scopus 로고
    • Dual pili post-translational modifications synergize to mediate meningococcal adherence to platelet activating factor receptor on human airway cells
    • F. E. C. Jen, M. J. Warren, B. L. Schulz, P. M. Power, W. E. Swords, J. N. Weiser, M. A. Apicella, J. L. Edwards, M. P. Jennings,. Dual pili post-translational modifications synergize to mediate meningococcal adherence to platelet activating factor receptor on human airway cells. PLoS Pathog. 2013, 9, e1003377.
    • (2013) PLoS Pathog. , vol.9
    • Jen, F.E.C.1    Warren, M.J.2    Schulz, B.L.3    Power, P.M.4    Swords, W.E.5    Weiser, J.N.6    Apicella, M.A.7    Edwards, J.L.8    Jennings, M.P.9
  • 17
    • 63049088278 scopus 로고    scopus 로고
    • Pathogenic neisseriae: Surface modulation, pathogenesis and infection control
    • M. Virji,. Pathogenic neisseriae: surface modulation, pathogenesis and infection control. Nat. Rev. Microbiol. 2009, 7, 274.
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 274
    • Virji, M.1
  • 18
    • 80052301150 scopus 로고    scopus 로고
    • Protein glycosylation in infectious disease pathobiology and treatment
    • D. J. Vigerust,. Protein glycosylation in infectious disease pathobiology and treatment. Cent. Eur. J. Biol. 2011, 6, 802.
    • (2011) Cent. Eur. J. Biol. , vol.6 , pp. 802
    • Vigerust, D.J.1
  • 19
    • 79955980572 scopus 로고    scopus 로고
    • Neisseria gonorrhoeae pilin glycan contributes to CR3 activation during challenge of primary cervical epithelial cells
    • M. P. Jennings, F. E. C. Jen, L. F. Roddam, M. A. Apicella, J. L. Edwards,. Neisseria gonorrhoeae pilin glycan contributes to CR3 activation during challenge of primary cervical epithelial cells. Cell. Microbiol. 2011, 13, 885.
    • (2011) Cell. Microbiol. , vol.13 , pp. 885
    • Jennings, M.P.1    Jen, F.E.C.2    Roddam, L.F.3    Apicella, M.A.4    Edwards, J.L.5
  • 21
    • 84874625369 scopus 로고    scopus 로고
    • Proteoform: A single term describing protein complexity
    • L. M. Smith, N. L. Kelleher,. Proteoform: a single term describing protein complexity. Nat Meth 2013, 10, 186.
    • (2013) Nat Meth , vol.10 , pp. 186
    • Smith, L.M.1    Kelleher, N.L.2
  • 23
    • 12344272637 scopus 로고    scopus 로고
    • Type IV pilus biogenesis in Neisseria meningitidis: PilW is involved in a step occurring after pilus assembly, essential for fibre stability and function
    • E. Carbonnelle, S. Helaine, L. Prouvensier, X. Nassif, V. Pelicic,. Type IV pilus biogenesis in Neisseria meningitidis: PilW is involved in a step occurring after pilus assembly, essential for fibre stability and function. Mol. Microbiol. 2005, 55, 54.
    • (2005) Mol. Microbiol. , vol.55 , pp. 54
    • Carbonnelle, E.1    Helaine, S.2    Prouvensier, L.3    Nassif, X.4    Pelicic, V.5
  • 25
    • 0027528605 scopus 로고
    • A single bifunctional enzyme, PilD, catalyzes cleavage and N-methylation of proteins belonging to the type-IV pilin family
    • M. S. Strom, D. N. Nunn, S. Lory,. A single bifunctional enzyme, PilD, catalyzes cleavage and N-methylation of proteins belonging to the type-IV pilin family. Proc. Natl. Acad. Sci. U. S. A. 1993, 90, 2404.
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 2404
    • Strom, M.S.1    Nunn, D.N.2    Lory, S.3
  • 26
    • 83755168835 scopus 로고    scopus 로고
    • Ultrahigh resolution and full-length pilin structures with insights for filament assembly, pathogenic functions, and vaccine potential
    • S. Hartung, A. S. Arvai, T. Wood, S. Kolappan, D. S. Shin, L. Craig, J. A. Tainer,. Ultrahigh resolution and full-length pilin structures with insights for filament assembly, pathogenic functions, and vaccine potential. J. Biol. Chem. 2011, 286, 44254.
    • (2011) J. Biol. Chem. , vol.286 , pp. 44254
    • Hartung, S.1    Arvai, A.S.2    Wood, T.3    Kolappan, S.4    Shin, D.S.5    Craig, L.6    Tainer, J.A.7
  • 27
    • 0036882287 scopus 로고    scopus 로고
    • Protein disulfide bond determination by mass spectrometry
    • J. J. Gorman, T. P. Wallis, J. J. Pitt,. Protein disulfide bond determination by mass spectrometry. Mass Spectrom. Rev. 2002, 21, 183.
    • (2002) Mass Spectrom. Rev. , vol.21 , pp. 183
    • Gorman, J.J.1    Wallis, T.P.2    Pitt, J.J.3
  • 29
    • 14844331822 scopus 로고    scopus 로고
    • Beyond quantitative proteomics: Signal enhancement of the a(1) ion as a mass tag for peptide sequencing using dimethyl labeling
    • J. L. Hsu, S. Y. Huang, J. T. Shiea, W. Y. Huang, S. H. Chen,. Beyond quantitative proteomics: signal enhancement of the a(1) ion as a mass tag for peptide sequencing using dimethyl labeling. J. Proteome Res. 2005, 4, 101.
    • (2005) J. Proteome Res. , vol.4 , pp. 101
    • Hsu, J.L.1    Huang, S.Y.2    Shiea, J.T.3    Huang, W.Y.4    Chen, S.H.5
  • 30
    • 33748788003 scopus 로고    scopus 로고
    • Deamidation of -Asn-Gly- sequences during sample preparation for proteomics: Consequences for MALDI and HPLC-MALDI analysis
    • O. V. Krokhin, M. Antonovici, W. Ens, J. A. Wilkins, K. G. Standing,. Deamidation of -Asn-Gly- sequences during sample preparation for proteomics: consequences for MALDI and HPLC-MALDI analysis. Anal. Chem. 2006, 78, 6645.
    • (2006) Anal. Chem. , vol.78 , pp. 6645
    • Krokhin, O.V.1    Antonovici, M.2    Ens, W.3    Wilkins, J.A.4    Standing, K.G.5
  • 31
    • 2442589577 scopus 로고    scopus 로고
    • Type IV pilus structure and bacterial pathogenicity
    • L. Craig, M. E. Pique, J. A. Tainer,. Type IV pilus structure and bacterial pathogenicity. Nat. Rev. Microbiol. 2004, 2, 363.
    • (2004) Nat. Rev. Microbiol. , vol.2 , pp. 363
    • Craig, L.1    Pique, M.E.2    Tainer, J.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.