Characterization of the Moraxella catarrhalis uspA1 and uspA2 Genes and Their Encoded Products
Autor: | Clive A. Slaughter, Leslie D. Cope, Eric J. Hansen, Frederick W. Henderson, George H. McCracken, Eric R. Lafontaine, Christoph Aebi, Charles A. Hasemann |
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Rok vydání: | 1999 |
Předmět: |
Repetitive Sequences
Amino Acid Transcription Genetic Sequence analysis Molecular Sequence Data Gene Expression Cell Surfaces Biology Microbiology Mass Spectrometry Moraxella catarrhalis Species Specificity Amino Acid Sequence Molecular Biology Peptide sequence Gene chemistry.chemical_classification Antigens Bacterial Base Sequence Sequence Homology Amino Acid Edman degradation Molecular mass Nucleic acid sequence biology.organism_classification Amino acid Molecular Weight chemistry Biochemistry Genes Bacterial Protein Biosynthesis Antigens Surface Sequence Analysis Bacterial Outer Membrane Proteins |
Zdroj: | Journal of Bacteriology. 181:4026-4034 |
ISSN: | 1098-5530 0021-9193 |
Popis: | 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. |
Databáze: | OpenAIRE |
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