This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Vogel, U.
Right arrow Articles by Frosch, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Vogel, U.
Right arrow Articles by Frosch, M.

 Previous Article  |  Next Article 

Infection and Immunity, February 1999, p. 954-957, Vol. 67, No. 2
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Role of Lipopolysaccharide Sialylation in Serum Resistance of Serogroup B and C Meningococcal Disease Isolates

Ulrich Vogel,* Heike Claus, Gabriele Heinze, and Matthias Frosch

Institut für Hygiene und Mikrobiologie, Universität Würzburg, 97080 Würzburg, Germany

Received 10 August 1998/Returned for modification 25 September 1998/Accepted 17 November 1998

alpha -2,3-Sialyltransferase mutants of three genetically and phenotypically diverse Neisseria meningitidis strains were compared with regard to resistance to human serum and systemic spread in the infant rat. Lipopolysaccharide sialylation was found to be of minor importance for the resistance of serogroup B and C meningococcal disease isolates to complement attack.

* Corresponding author. Mailing address: Institut für Hygiene und Mikrobiologie, Universität Würzburg, Josef-Schneider-Str. 2, 97080 Würzburg, Germany. Phone: 49(931)201 3902. Fax: 49(931)201 3445. E-mail: uvogel{at}hygiene.uni-wuerzburg.de.

Infection and Immunity, February 1999, p. 954-957, Vol. 67, No. 2
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Maruvada, R., Prasadarao, N. V., Rubens, C. E. (2009). Acquisition of factor H by a novel surface protein on group B Streptococcus promotes complement degradation. FASEB J. 23: 3967-3977 [Abstract] [Full Text]  
  • Almagro-Moreno, S., Boyd, E. F. (2009). Sialic Acid Catabolism Confers a Competitive Advantage to Pathogenic Vibrio cholerae in the Mouse Intestine. Infect. Immun. 77: 3807-3816 [Abstract] [Full Text]  
  • Shaughnessy, J., Lewis, L. A., Jarva, H., Ram, S. (2009). Functional Comparison of the Binding of Factor H Short Consensus Repeat 6 (SCR 6) to Factor H Binding Protein from Neisseria meningitidis and the Binding of Factor H SCR 18 to 20 to Neisseria gonorrhoeae Porin. Infect. Immun. 77: 2094-2103 [Abstract] [Full Text]  
  • Lewis, L. A., Ram, S., Prasad, A., Gulati, S., Getzlaff, S., Blom, A. M., Vogel, U., Rice, P. A. (2008). Defining Targets for Complement Components C4b and C3b on the Pathogenic Neisseriae. Infect. Immun. 76: 339-350 [Abstract] [Full Text]  
  • Smith, H., Tang, C. M., Exley, R. M. (2007). Effect of Host Lactate on Gonococci and Meningococci: New Concepts on the Role of Metabolites in Pathogenicity. Infect. Immun. 75: 4190-4198 [Full Text]  
  • Madico, G., Ngampasutadol, J., Gulati, S., Vogel, U., Rice, P. A., Ram, S. (2007). Factor H Binding and Function in Sialylated Pathogenic Neisseriae is Influenced by Gonococcal, but Not Meningococcal, Porin. J. Immunol. 178: 4489-4497 [Abstract] [Full Text]  
  • Madico, G., Welsch, J. A., Lewis, L. A., McNaughton, A., Perlman, D. H., Costello, C. E., Ngampasutadol, J., Vogel, U., Granoff, D. M., Ram, S. (2006). The Meningococcal Vaccine Candidate GNA1870 Binds the Complement Regulatory Protein Factor H and Enhances Serum Resistance. J. Immunol. 177: 501-510 [Abstract] [Full Text]  
  • Packiam, M., Shell, D. M., Liu, S. V., Liu, Y.-B., McGee, D. J., Srivastava, R., Seal, S., Rest, R. F. (2006). Differential Expression and Transcriptional Analysis of the {alpha}-2,3-Sialyltransferase Gene in Pathogenic Neisseria spp.. Infect. Immun. 74: 2637-2650 [Abstract] [Full Text]  
  • Gulati, S., Cox, A., Lewis, L. A., Michael, F. St., Li, J., Boden, R., Ram, S., Rice, P. A. (2005). Enhanced Factor H Binding to Sialylated Gonococci Is Restricted to the Sialylated Lacto-N-Neotetraose Lipooligosaccharide Species: Implications for Serum Resistance and Evidence for a Bifunctional Lipooligosaccharide Sialyltransferase in Gonococci. Infect. Immun. 73: 7390-7397 [Abstract] [Full Text]  
  • Exley, R. M., Shaw, J., Mowe, E., Sun, Y.-h., West, N. P., Williamson, M., Botto, M., Smith, H., Tang, C. M. (2005). Available carbon source influences the resistance of Neisseria meningitidis against complement. JEM 201: 1637-1645 [Abstract] [Full Text]  
  • Jarva, H., Ram, S., Vogel, U., Blom, A. M., Meri, S. (2005). Binding of the Complement Inhibitor C4bp to Serogroup B Neisseria meningitidis. J. Immunol. 174: 6299-6307 [Abstract] [Full Text]  
  • Ram, S., Cox, A. D., Wright, J. C., Vogel, U., Getzlaff, S., Boden, R., Li, J., Plested, J. S., Meri, S., Gulati, S., Stein, D. C., Richards, J. C., Moxon, E. R., Rice, P. A. (2003). Neisserial Lipooligosaccharide Is a Target for Complement Component C4b: INNER CORE PHOSPHOETHANOLAMINE RESIDUES DEFINE C4b LINKAGE SPECIFICITY. J. Biol. Chem. 278: 50853-50862 [Abstract] [Full Text]  
  • Oyston, P.C. F., Prior, J.L., Kiljunen, S., Skurnik, M., Hill, J., Titball, R.W. (2003). Expression of heterologous O-antigen in Yersinia pestis KIM does not affect virulence by the intravenous route. J Med Microbiol 52: 289-294 [Abstract] [Full Text]  
  • Geoffroy, M.-C., Floquet, S., Metais, A., Nassif, X., Pelicic, V. (2003). Large-Scale Analysis of the Meningococcus Genome by Gene Disruption: Resistance to Complement-Mediated Lysis. Genome Res 13: 391-398 [Abstract] [Full Text]  
  • Shell, D. M., Chiles, L., Judd, R. C., Seal, S., Rest, R. F. (2002). The Neisseria Lipooligosaccharide-Specific {alpha}-2,3-Sialyltransferase Is a Surface-Exposed Outer Membrane Protein. Infect. Immun. 70: 3744-3751 [Abstract] [Full Text]  
  • Munster, A.-K., Weinhold, B., Gotza, B., Muhlenhoff, M., Frosch, M., Gerardy-Schahn, R. (2002). Nuclear Localization Signal of Murine CMP-Neu5Ac Synthetase Includes Residues Required for Both Nuclear Targeting and Enzymatic Activity. J. Biol. Chem. 277: 19688-19696 [Abstract] [Full Text]  
  • Unkmeir, A., Kammerer, U., Stade, A., Hubner, C., Haller, S., Kolb-Maurer, A., Frosch, M., Dietrich, G. (2002). Lipooligosaccharide and Polysaccharide Capsule: Virulence Factors of Neisseria meningitidis That Determine Meningococcal Interaction with Human Dendritic Cells. Infect. Immun. 70: 2454-2462 [Abstract] [Full Text]  
  • Brandtzaeg, P., Bjerre, A., Ovstebo, R., Brusletto, B., Joo, G. B., Kierulf, P. (2001). Invited review: Neisseria meningitidis lipopolysaccharides in human pathology. Innate Immunity 7: 401-420 [Abstract]  
  • van Deuren, M., Brandtzaeg, P., van der Meer, J. W. M. (2000). Update on Meningococcal Disease with Emphasis on Pathogenesis and Clinical Management. Clin. Microbiol. Rev. 13: 144-166 [Abstract] [Full Text]  
  • Dixon, G. L. J., Heyderman, R. S., Kotovicz, K., Jack, D. L., Andersen, S. R., Vogel, U., Frosch, M., Klein, N. (1999). Endothelial Adhesion Molecule Expression and Its Inhibition by Recombinant Bactericidal/Permeability-Increasing Protein Are Influenced by the Capsulation and Lipooligosaccharide Structure of Neisseria meningitidis. Infect. Immun. 67: 5626-5633 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»