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

Author:

Dugourd Dominique1,Martin Christine2,Rioux Clément R.3,Jacques Mario1,Harel Josée1

Affiliation:

1. 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;

2. Laboratoire de Microbiologie, INRA Clermont-Ferrand-Theix, 63122 St-Genès-Champanelle, France2; and

3. Centre de Recherche en Infectiologie, Centre Hospitalier Universitaire de Québec, Sainte-Foy, Québec, Canada G1V 4G23

Abstract

ABSTRACT 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 [ 3 H]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 .

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

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