IAI FigSearch
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Wyss, C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Wyss, C.

Infection and Immunity, December 1998, p. 5751-5754, Vol. 66, No. 12
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Flagellins, but Not Endoflagellar Sheath Proteins, of Treponema pallidum and of Pathogen-Related Oral Spirochetes Are Glycosylated

C. Wyss*

Institut für Orale Mikrobiologie und Allgemeine Immunologie, Zentrum für Zahn-, Mund- und Kieferheilkunde der Universität Zürich, CH-8028 Zürich, Switzerland

Received 26 January 1998/Returned for modification 13 April 1998/Accepted 28 September 1998

Glycosylation of the flagellar core proteins (FlaBs) was detected in Treponema pallidum Nichols and in the type or reference strains of seven oral Treponema species. In several nonmotile strains of oral treponemes, the FlaBs were undetectable by both antibody and glycan staining. In contrast, a spontaneous low-motility variant of T. vincenti£i-related strain RitzA, OMZ 305A, lacked the flagellar sheath protein (FlaA) and the two glycan-staining FlaB bands of the wild type, but antibody labeling revealed a novel FlaB band with a lower relative molecular weight. A ca. 38-kDa component of isolated endoflagella of T. vincentii OMZ 800 was identified on Western blots as FlaA by monoclonal antibody (MAb) H9-2, which specifically labels the 37-kDa FlaA protein of T. pallidum. Glycan and H9-2 labeling patterns similar to those of T. pallidum were observed in whole-cell extracts of T. medium G7201 and of 10 strains classified as T. vincentii and as two T. vincentii-related taxons. These four groups were thus identified as cultivable pathogen (T. pallidum)-related oral spirochetes as defined by labeling with MAb H9-2. No H9-2 MAb-reactive component could be detected in T. amylovorum, T. denticola, T. maltophilum, T. pectinovorum, and the three subspecies of T. socranskii.

* Mailing address: Institut für Orale Mikrobiologie und Allgemeine Immunologie, Plattenstr. 11, Postfach, CH-8028 Zürich, Switzerland. Phone: 411 634 3322. Fax: 411 634 4310. E-mail: wyss.c{at}zzmk.unizh.ch.

Infection and Immunity, December 1998, p. 5751-5754, Vol. 66, No. 12
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:



Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
J. Bacteriol. J. Virol. Eukaryot. Cell
Microbiol. Mol. Biol. Rev. Clin. Vaccine Immunol. All ASM Journals

Copyright © 1998 by the American Society for Microbiology. All rights reserved.