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Journal of Bacteriology, March 2000, p. 1364-1373, Vol. 182, No. 5
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

The UspA1 Protein and a Second Type of UspA2 Protein Mediate Adherence of Moraxella catarrhalis to Human Epithelial Cells In Vitro

Eric R. Lafontaine,1 Leslie D. Cope,1 Christoph Aebi,1,2,dagger Jo L. Latimer,1 George H. McCracken Jr.,2 and Eric J. Hansen1,*

Departments of Microbiology1 and Pediatrics,2 University of Texas Southwestern Medical Center, Dallas, Texas 75235-9048

Received 3 September 1999/Accepted 30 November 1999

The UspA1 and UspA2 proteins of Moraxella catarrhalis are structurally related, are exposed on the bacterial cell surface, and migrate as very high-molecular-weight complexes in sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Previous analysis of uspA1 and uspA2 mutants of M. catarrhalis strain 035E indicated that UspA1 was involved in adherence of this organism to Chang conjunctival epithelial cells in vitro and that expression of UspA2 was essential for resistance of this strain to killing by normal human serum (C. Aebi, E. R. Lafontaine, L. D. Cope, J. L. Latimer, S. R. Lumbley, G. H. McCracken, Jr., and E. J. Hansen, Infect. Immun. 66:3113-3119, 1998). In the present study, isogenic uspA1, uspA2, and uspA1 uspA2 mutations were constructed in three additional M. catarrhalis strains: 012E, TTA37, and 046E. The uspA1 mutant of strain 012E had a decreased ability to attach to Chang cells. However, inactivation of the uspA1 gene in both strain TTA37 and strain 046E did not cause a significant decrease in attachment ability. Inactivation of the uspA2 gene of strain TTA37 did result in a loss of attachment ability. Nucleotide sequence analysis revealed that the predicted protein encoded by the uspA2 genes of both strains TTA37 and 046E had a N-terminal half that resembled the N-terminal half of UspA1 proteins, whereas the C-terminal half of this protein was nearly identical to those of previously characterized UspA2 proteins. The gene encoding this "hybrid" protein was designated uspA2H. PCR-based analysis revealed that approximately 20% of M. catarrhalis strains apparently possess a uspA2H gene instead of a uspA2 gene. The M. catarrhalis uspA1, uspA2, and uspA2H genes were cloned and expressed in Haemophilus influenzae cells, which were used to prove that both the UspA1 and UspA2H proteins can function as adhesins in vitro.

* Corresponding author. Mailing address: Department of Microbiology, Hamon Building, NA6.200, University of Texas Southwestern Medical Center, 6000 Harry Hines Boulevard, Dallas, TX 75235-9048. Phone: (214) 648-5974. Fax: (214) 648-5905. E-mail: hansen01{at}utsw.swmed.edu.

dagger Present address: Department of Pediatrics, University of Bern, Inselspital, CH-3010 Bern, Switzerland.

Journal of Bacteriology, March 2000, p. 1364-1373, Vol. 182, No. 5
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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