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Journal of Bacteriology, July 1999, p. 4026-4034, Vol. 181, No. 13
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Characterization of the Moraxella catarrhalis uspA1 and uspA2 Genes and Their Encoded Products

Leslie D. Cope,1 Eric R. Lafontaine,1 Clive A. Slaughter,2 Charles A. Hasemann Jr.,3 Christoph Aebi,1,4 Frederick W. Henderson,5 George H. McCracken Jr.,4 and Eric J. Hansen1,*

Departments of Microbiology,1 Biochemistry,2 Internal Medicine,3 and Pediatrics,4 University of Texas Southwestern Medical Center, Dallas, Texas 75235-9048, and Department of Pediatrics, University of North Carolina, Chapel Hill, North Carolina 275995

Received 11 February 1999/Accepted 13 April 1999

The uspA1 and uspA2 genes of M. catarrhalis O35E encode two different surface-exposed proteins which were previously shown to share a 140-amino-acid region with 93% identity (C. Aebi, I. Maciver, J. L. Latimer, L. D. Cope, M. K. Stevens, S. E. Thomas, G. H. McCracken, Jr., and E. J. Hansen, Infect. Immun. 65:4367-4377, 1997). The N-terminal amino acid sequences of the mature forms of both UspA1 and UspA2 from strain O35E were determined after enzymatic treatment to remove the N-terminal pyroglutamyl residue that had blocked Edman degradation. Mass spectrometric analysis indicated that the molecular mass of UspA1 from M. catarrhalis O35E was 83,500 ± 116 Da. Nucleotide sequence analysis of the uspA1 and uspA2 genes from three other M. catarrhalis strains (TTA24, ATCC 25238, and V1171) revealed that the encoded protein products were very similar to those from strain O35E. Western blot analysis was used to confirm that each of these three strains of M. catarrhalis expressed both UspA1 and UspA2 proteins. Several different and repetitive amino acid motifs were present in both UspA1 and UspA2 from these four strains, and some of these were predicted to form coiled coils. Linear DNA templates were used in an in vitro transcription-translation system to determine the sizes of the monomeric forms of the UspA1 and UspA2 proteins from strains O35E and TTA24.

* Corresponding author. Mailing address: Department of Microbiology, University of Texas Southwestern Medical Center, 5323 Harry Hines Blvd., Dallas, TX 75235-9048. Phone: (214) 648-5974. Fax: (214) 648-5905. E-mail: hansen01{at}utsw.swmed.edu.

Journal of Bacteriology, July 1999, p. 4026-4034, Vol. 181, No. 13
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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