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Infection and Immunity, November 2008, p. 5330-5340, Vol. 76, No. 11
0019-9567/08/$08.00+0     doi:10.1128/IAI.00573-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Modular Arrangement of Allelic Variants Explains the Divergence in Moraxella catarrhalis UspA Protein Function{triangledown}

Michael J. Brooks,1 Jennifer L. Sedillo,2 Nikki Wagner,2 Cassie A. Laurence,2 Wei Wang,2 Ahmed S. Attia,2,3 Eric J. Hansen,2 and Scott D. Gray-Owen1*

Department of Molecular Genetics, University of Toronto, Toronto, Ontario M5S1A8, Canada,1 Department of Microbiology, University of Texas Southwestern Medical Center, Dallas, Texas 75390,2 Department of Microbiology and Immunology, Faculty of Pharmacy, Cairo University, Cairo 11562, Egypt3

Received 9 May 2008/ Returned for modification 26 June 2008/ Accepted 30 July 2008

Ubiquitous surface protein A molecules (UspAs) of Moraxella catarrhalis are large, nonfimbrial, autotransporter proteins that can be visualized as a "fuzzy" layer on the bacterial surface by transmission electron microscopy. Previous studies attributed a wide array of functions and binding activities to the closely related UspA1, UspA2, and/or UspA2H protein, yet the molecular and phylogenetic relationships among these activities remain largely unexplored. To address this issue, we determined the nucleotide sequence of the uspA1 genes from a variety of independent M. catarrhalis isolates and compared the deduced amino acid sequences to those of the previously characterized UspA1, UspA2, and UspA2H proteins. Rather than being conserved proteins, we observed a striking divergence of individual UspA1, UspA2, and UspA2H proteins resulting from the modular assortment of unrelated "cassettes" of peptide sequence. The exchange of certain variant cassettes correlates with strain-specific differences in UspA protein function and confers differing phenotypes upon these mucosal surface pathogens.

* Corresponding author. Mailing address: Department of Molecular Genetics, University of Toronto, Medical Sciences Building, Room 4381, 1 King's College Circle, Toronto, Ontario M5S 1A8, Canada. Phone: (416) 946-5307. Fax: (416) 978-6885. E-mail: scott.gray.owen{at}utoronto.ca

{triangledown} Published ahead of print on 4 August 2008.

Editor: J. N. Weiser

Infection and Immunity, November 2008, p. 5330-5340, Vol. 76, No. 11
0019-9567/08/$08.00+0     doi:10.1128/IAI.00573-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Balder, R., Krunkosky, T. M., Nguyen, C. Q., Feezel, L., Lafontaine, E. R. (2009). Hag Mediates Adherence of Moraxella catarrhalis to Ciliated Human Airway Cells. Infect. Immun. 77: 4597-4608 [Abstract] [Full Text]  
  • de Vries, S. P. W., Bootsma, H. J., Hays, J. P., Hermans, P. W. M. (2009). Molecular Aspects of Moraxella catarrhalis Pathogenesis. Microbiol. Mol. Biol. Rev. 73: 389-406 [Abstract] [Full Text]  
  • Brooks, M. J., Sedillo, J. L., Wagner, N., Wang, W., Attia, A. S., Wong, H., Laurence, C. A., Hansen, E. J., Gray-Owen, S. D. (2008). Moraxella catarrhalis Binding to Host Cellular Receptors Is Mediated by Sequence-Specific Determinants Not Conserved among All UspA1 Protein Variants. Infect. Immun. 76: 5322-5329 [Abstract] [Full Text]  


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