This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplemental material
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 Allen, S.
Right arrow Articles by Apicella, M. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Allen, S.
Right arrow Articles by Apicella, M. A.

Next Article 

Infection and Immunity, September 2005, p. 5291-5300, Vol. 73, No. 9
0019-9567/05/$08.00+0     doi:10.1128/IAI.73.9.5291-5300.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Novel Sialic Acid Transporter of Haemophilus influenzae{dagger}

Simon Allen,1 Anthony Zaleski,2 Jason W. Johnston,2 Bradford W. Gibson,1,3 and Michael A. Apicella2*

Buck Institute for Age Research, 8001 Redwood Blvd., Novato, California 94945,1 Department of Microbiology, University of Iowa, Iowa City, Iowa 52242,2 Department of Pharmaceutical Chemistry, University of California, San Francisco, California 94143-04463

Received 7 February 2005/ Returned for modification 30 March 2005/ Accepted 24 May 2005

Nontypeable Haemophilus influenzae is an opportunistic pathogen and a common cause of otitis media in children and of chronic bronchitis and pneumonia in patients with chronic obstructive pulmonary disease. The lipooligosaccharides, a major component of the outer membrane of H. influenzae, play an important role in microbial virulence and pathogenicity. N-Acetylneuraminic acid (sialic acid) can be incorporated into the lipooligosaccharides as a terminal nonreducing sugar. Although much of the pathway of sialic acid incorporation into lipooligosaccharides is understood, the transporter responsible for N-acetylneuraminic acid uptake in H. influenzae has yet to be characterized. In this paper we demonstrate that this transporter is a novel sugar transporter of the tripartite ATP-independent periplasmic transporter family. In the absence of this transporter, H. influenzae cannot incorporate sialic acid into its lipooligosaccharides, making the organism unable to survive when exposed to human serum and causing reduced viability in biofilm growth.

* Corresponding author. Mailing address: Department of Microbiology, University of Iowa, Iowa City, IA 52242. Phone: (319) 335-7807. Fax: (319) 335-9006. E-mail: michael-apicella{at}uiowa.edu.

{dagger} Supplemental material for this article may be found at http://iai.asm.org/.

Editor: J. N. Weiser

Infection and Immunity, September 2005, p. 5291-5300, Vol. 73, No. 9
0019-9567/05/$08.00+0     doi:10.1128/IAI.73.9.5291-5300.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Brigham, C., Caughlan, R., Gallegos, R., Dallas, M. B., Godoy, V. G., Malamy, M. H. (2009). Sialic Acid (N-Acetyl Neuraminic Acid) Utilization by Bacteroides fragilis Requires a Novel N-Acetyl Mannosamine Epimerase. J. Bacteriol. 191: 3629-3638 [Abstract] [Full Text]  
  • Mulligan, C., Geertsma, E. R., Severi, E., Kelly, D. J., Poolman, B., Thomas, G. H. (2009). The substrate-binding protein imposes directionality on an electrochemical sodium gradient-driven TRAP transporter. Proc. Natl. Acad. Sci. USA 106: 1778-1783 [Abstract] [Full Text]  
  • Severi, E., Muller, A., Potts, J. R., Leech, A., Williamson, D., Wilson, K. S., Thomas, G. H. (2008). Sialic Acid Mutarotation Is Catalyzed by the Escherichia coli {beta}-Propeller Protein YjhT. J. Biol. Chem. 283: 4841-4849 [Abstract] [Full Text]  
  • Johnston, J. W., Coussens, N. P., Allen, S., Houtman, J. C. D., Turner, K. H., Zaleski, A., Ramaswamy, S., Gibson, B. W., Apicella, M. A. (2008). Characterization of the N-Acetyl-5-neuraminic Acid-binding Site of the Extracytoplasmic Solute Receptor (SiaP) of Nontypeable Haemophilus influenzae Strain 2019. J. Biol. Chem. 283: 855-865 [Abstract] [Full Text]  
  • Severi, E., Hood, D. W., Thomas, G. H. (2007). Sialic acid utilization by bacterial pathogens. Microbiology 153: 2817-2822 [Abstract] [Full Text]  
  • Erwin, A. L., Allen, S., Ho, D. K., Bonthius, P. J., Jarisch, J., Nelson, K. L., Tsao, D. L., Unrath, W. C. T., Watson, M. E. Jr., Gibson, B. W., Apicella, M. A., Smith, A. L. (2006). Role of lgtC in Resistance of Nontypeable Haemophilus influenzae Strain R2866 to Human Serum. Infect. Immun. 74: 6226-6235 [Abstract] [Full Text]  
  • Muller, A., Severi, E., Mulligan, C., Watts, A. G., Kelly, D. J., Wilson, K. S., Wilkinson, A. J., Thomas, G. H. (2006). Conservation of Structure and Mechanism in Primary and Secondary Transporters Exemplified by SiaP, a Sialic Acid Binding Virulence Factor from Haemophilus influenzae. J. Biol. Chem. 281: 22212-22222 [Abstract] [Full Text]  
  • Thomas, G. H., Southworth, T., Leon-Kempis, M. R., Leech, A., Kelly, D. J. (2006). Novel ligands for the extracellular solute receptors of two bacterial TRAP transporters. Microbiology 152: 187-198 [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»