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 Mu, X.-Q.
Right arrow Articles by Bullitt, E.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Mu, X.-Q.
Right arrow Articles by Bullitt, E.

 Previous Article  |  Next Article 

Journal of Bacteriology, September 2002, p. 4868-4874, Vol. 184, No. 17
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.17.4868-4874.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Structure and Function of Hib Pili from Haemophilus influenzae Type b

Xiang-Qi Mu,1 Edward H. Egelman,2 and Esther Bullitt1*

Department of Physiology & Biophysics, Boston University School of Medicine, Boston, Massachusetts 02118-2526,1 Department of Biochemistry & Molecular Genetics, University of Virginia, Charlottesville, Virginia 22908-07332

Received 15 March 2002/ Accepted 21 May 2002

Pathogenic bacteria are specifically adapted to bind to their customary host. Disease is then caused by subsequent colonization and/or invasion of the local environmental niche. Initial binding of Haemophilus influenzae type b to the human nasopharynx is facilitated by Hib pili, filaments expressed on the bacterial surface. With three-dimensional reconstruction of electron micrograph images, we show that Hib pili comprise a helix 70 Å in diameter with threefold symmetry. The Hib pilus filament has 3.0 subunits per turn, with each set of three subunits translated 26.9 Å along and rotated 53 degrees about the helical axis. Amino acid sequence analysis of pilins from Hib pili and from P-pili expressed on uropathogenic Escherichia coli were used to predict the physical location of the highly variable and immunogenic region of the HifA pilin in the Hib pilus structure. Structural differences between Hib pili and P-pili suggest a difference in the strategies by which bacteria remain bound to their host cells: P-pili were shown to be capable of unwinding to five times their original length (E. Bullitt and L. Makowski, Nature 373:164-167, 1995), while damage to Hib pili occurs by slight shearing of subunits with respect to those further along the helical axis. This capacity to resist unwinding may be important for continued adherence of H. influenzae type b to the nasopharynx, where the three-stranded Hib pilus filaments provide a robust tether to withstand coughs and sneezes.

* Corresponding author. Mailing address: Department of Physiology & Biophysics, Boston University School of Medicine, Boston, MA 02118-2526. Phone: (617) 638-5037. Fax: (617) 638-4041. E-mail: bullitt{at}bu.edu.

Journal of Bacteriology, September 2002, p. 4868-4874, Vol. 184, No. 17
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.17.4868-4874.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Li, Y.-F., Poole, S., Nishio, K., Jang, K., Rasulova, F., McVeigh, A., Savarino, S. J., Xia, D., Bullitt, E. (2009). Structure of CFA/I fimbriae from enterotoxigenic Escherichia coli. Proc. Natl. Acad. Sci. USA 106: 10793-10798 [Abstract] [Full Text]  
  • Arce, F. T., Carlson, R., Monds, J., Veeh, R., Hu, F. Z., Stewart, P. S., Lal, R., Ehrlich, G. D., Avci, R. (2009). Nanoscale Structural and Mechanical Properties of Nontypeable Haemophilus influenzae Biofilms. J. Bacteriol. 191: 2512-2520 [Abstract] [Full Text]  
  • Nuccio, S.-P., Baumler, A. J. (2007). Evolution of the Chaperone/Usher Assembly Pathway: Fimbrial Classification Goes Greek. Microbiol. Mol. Biol. Rev. 71: 551-575 [Abstract] [Full Text]  
  • Touhami, A., Jericho, M. H., Boyd, J. M., Beveridge, T. J. (2006). Nanoscale Characterization and Determination of Adhesion Forces of Pseudomonas aeruginosa Pili by Using Atomic Force Microscopy. J. Bacteriol. 188: 370-377 [Abstract] [Full Text]  
  • Collins, R. F., Frye, S. A., Balasingham, S., Ford, R. C., Tonjum, T., Derrick, J. P. (2005). Interaction with Type IV Pili Induces Structural Changes in the Bacterial Outer Membrane Secretin PilQ. J. Biol. Chem. 280: 18923-18930 [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»