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Infection and Immunity, November 2008, p. 5322-5329, Vol. 76, No. 11
0019-9567/08/$08.00+0     doi:10.1128/IAI.00572-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Moraxella catarrhalis Binding to Host Cellular Receptors Is Mediated by Sequence-Specific Determinants Not Conserved among All UspA1 Protein Variants{triangledown}

Michael J. Brooks,1 Jennifer L. Sedillo,2 Nikki Wagner,2 Wei Wang,2 Ahmed S. Attia,2,3 Henry Wong,1 Cassie A. Laurence,2 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

The Moraxella catarrhalis ubiquitous surface proteins (UspAs) are autotransporter molecules reported to interact with a variety of different host proteins and to affect processes ranging from serum resistance to cellular adhesion. The role of UspA1 as an adhesin has been confirmed with a number of different human cell types and is mediated by binding to eukaryotic proteins including carcinoembryonic antigen-related cellular adhesion molecules (CEACAMs), fibronectin, and laminin. A distinct difference in the ability of prototypical M. catarrhalis strains to adhere to CEACAM-expressing cell lines prompted us to perform strain-specific structure-function analyses of UspA1 proteins. In this study, we characterized CEACAM binding by a diverse set of UspA1 proteins and showed that 3 out of 10 UspA1 proteins were incapable of binding CEACAM. This difference resulted from the absence of a distinct CEACAM binding motif in nonadhering strains. Our sequence analysis also revealed a single M. catarrhalis isolate that lacked the fibronectin-binding motif and was defective in adherence to Chang conjunctival epithelial cells. These results clearly demonstrate that UspA1-associated adhesive functions are not universally conserved. Instead, UspA1 proteins must be considered as variants with the potential to confer both different cell tropisms and host cell responses.

* 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. 5322-5329, Vol. 76, No. 11
0019-9567/08/$08.00+0     doi:10.1128/IAI.00572-08
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., Laurence, C. A., Wang, W., Attia, A. S., Hansen, E. J., Gray-Owen, S. D. (2008). Modular Arrangement of Allelic Variants Explains the Divergence in Moraxella catarrhalis UspA Protein Function. Infect. Immun. 76: 5330-5340 [Abstract] [Full Text]  


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