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An unexpected flaA homolog is present and expressed in Borrelia burgdorferi
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| Zeitschriftentitel: | Journal of Bacteriology |
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| Personen und Körperschaften: | , |
| In: | Journal of Bacteriology, 179, 1997, 2, S. 552-556 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
American Society for Microbiology
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| Schlagwörter: |
| Zusammenfassung: | <jats:p>Most investigators have assumed that the periplasmic flagella (PFs) of Borrelia burgdorferi are composed of only one flagellin protein. The PFs of most other spirochete species are complex: these PFs contain an outer sheath of FlaA proteins and a core filament of FlaB proteins. During an analysis of a chemotaxis gene cluster of B. burgdorferi 212, we were surprised to find a flaA gene homolog with a deduced polypeptide having 54 to 58% similarity to FlaA from other spirochetes. Like other FlaA proteins, B. burgdorferi FlaA has a conserved signal sequence at its N terminus. Based on reverse transcription-PCR and primer extension analysis, this flaA homolog and five chemotaxis genes constitute a motility-chemotaxis operon. Immunoblots using anti-FlaA serum from Treponema pallidum and a lysate of B. burgdorferi showed strong reactivity to a protein of 38.0 kDa, which is consistent with the expression of flaA in growing cells.</jats:p> |
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| Umfang: | 552-556 |
| ISSN: |
0021-9193
1098-5530 |
| DOI: | 10.1128/jb.179.2.552-556.1997 |