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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: |
author_facet |
Ge, Y Charon, N W Ge, Y Charon, N W |
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author |
Ge, Y Charon, N W |
spellingShingle |
Ge, Y Charon, N W Journal of Bacteriology An unexpected flaA homolog is present and expressed in Borrelia burgdorferi Molecular Biology Microbiology |
author_sort |
ge, y |
spelling |
Ge, Y Charon, N W 0021-9193 1098-5530 American Society for Microbiology Molecular Biology Microbiology http://dx.doi.org/10.1128/jb.179.2.552-556.1997 <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> An unexpected flaA homolog is present and expressed in Borrelia burgdorferi Journal of Bacteriology |
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American Society for Microbiology, 1997 |
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American Society for Microbiology, 1997 |
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American Society for Microbiology |
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Journal of Bacteriology |
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title |
An unexpected flaA homolog is present and expressed in Borrelia burgdorferi |
title_unstemmed |
An unexpected flaA homolog is present and expressed in Borrelia burgdorferi |
title_full |
An unexpected flaA homolog is present and expressed in Borrelia burgdorferi |
title_fullStr |
An unexpected flaA homolog is present and expressed in Borrelia burgdorferi |
title_full_unstemmed |
An unexpected flaA homolog is present and expressed in Borrelia burgdorferi |
title_short |
An unexpected flaA homolog is present and expressed in Borrelia burgdorferi |
title_sort |
an unexpected flaa homolog is present and expressed in borrelia burgdorferi |
topic |
Molecular Biology Microbiology |
url |
http://dx.doi.org/10.1128/jb.179.2.552-556.1997 |
publishDate |
1997 |
physical |
552-556 |
description |
<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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author | Ge, Y, Charon, N W |
author_facet | Ge, Y, Charon, N W, Ge, Y, Charon, N W |
author_sort | ge, y |
container_issue | 2 |
container_start_page | 552 |
container_title | Journal of Bacteriology |
container_volume | 179 |
description | <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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spelling | Ge, Y Charon, N W 0021-9193 1098-5530 American Society for Microbiology Molecular Biology Microbiology http://dx.doi.org/10.1128/jb.179.2.552-556.1997 <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> An unexpected flaA homolog is present and expressed in Borrelia burgdorferi Journal of Bacteriology |
spellingShingle | Ge, Y, Charon, N W, Journal of Bacteriology, An unexpected flaA homolog is present and expressed in Borrelia burgdorferi, Molecular Biology, Microbiology |
title | An unexpected flaA homolog is present and expressed in Borrelia burgdorferi |
title_full | An unexpected flaA homolog is present and expressed in Borrelia burgdorferi |
title_fullStr | An unexpected flaA homolog is present and expressed in Borrelia burgdorferi |
title_full_unstemmed | An unexpected flaA homolog is present and expressed in Borrelia burgdorferi |
title_short | An unexpected flaA homolog is present and expressed in Borrelia burgdorferi |
title_sort | an unexpected flaa homolog is present and expressed in borrelia burgdorferi |
title_unstemmed | An unexpected flaA homolog is present and expressed in Borrelia burgdorferi |
topic | Molecular Biology, Microbiology |
url | http://dx.doi.org/10.1128/jb.179.2.552-556.1997 |