JB
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 Dugourd, D.
Right arrow Articles by Harel, J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Dugourd, D.
Right arrow Articles by Harel, J.

Journal of Bacteriology, November 1999, p. 6948-6957, Vol. 181, No. 22
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Characterization of a Periplasmic ATP-Binding Cassette Iron Import System of Brachyspira (Serpulina) hyodysenteriae

Dominique Dugourd,1 Christine Martin,2 Clément R. Rioux,3,dagger Mario Jacques,1 and Josée Harel1,*

Groupe de Recherche sur les Maladies Infectieuses du Porc, Département de pathologie et microbiologie, Faculté de médecine vétérinaire, Université de Montréal, Saint-Hyacinthe, Québec, Canada J2S 7C61; Laboratoire de Microbiologie, INRA Clermont-Ferrand-Theix, 63122 St-Genès-Champanelle, France2; and Centre de Recherche en Infectiologie, Centre Hospitalier Universitaire de Québec, Sainte-Foy, Québec, Canada G1V 4G23

Received 30 December 1998/Accepted 17 March 1999

The nucleotide sequence of the pathogenic spirochete Brachyspira hyodysenteriae bit (for "Brachyspira iron transport") genomic region has been determined. The bit region is likely to encode an iron ATP-binding cassette transport system with some homology to those encountered in gram-negative bacteria. Six open reading frames oriented in the same direction and physically linked have been identified. This system possesses a protein containing ATP-binding motifs (BitD), two hydrophobic cytoplasmic membrane permeases (BitE and BitF), and at least three lipoproteins (BitA, BitB, and BitC) with homology to iron periplasmic binding proteins. These periplasmic binding proteins exhibit lipoprotein features. They are labeled by [3H]palmitate when tested in recombinant Escherichia coli, and their signal peptides are typical for substrates of the type II secretory peptidase. The FURTA system and Congo red assay indicate that BitB and BitC are involved in iron binding. The Bit system is detected only in B. hyodysenteriae and is absent from B. innocens and B. pilosicoli.


* Corresponding author. Mailing address: Groupe de Recherche sur les Maladies Infectieuses du Porc, Département de pathologie et microbiologie, Faculté de médecine vétérinaire, Université de Montréal, Saint-Hyacinthe, Québec, Canada J2S 7C6. Phone: (514) 773-8521 ext. 8233. Fax: (514) 778-8108. E-mail: harelj{at}ERE.umontreal.ca.

dagger Present address: Intellivax International Inc., Montréal, Québec, Canada H4P 2R2.


Journal of Bacteriology, November 1999, p. 6948-6957, Vol. 181, No. 22
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.



This article has been cited by other articles:




Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
Appl. Environ. Microbiol. Infect. Immun. Eukaryot. Cell
Mol. Cell. Biol. J. Virol. Microbiol. Mol. Biol. Rev.
ALL ASM JOURNALS

Copyright © 1999 by the American Society for Microbiology. All rights reserved.