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Growth of Serpulina (Treponema) hyodysenteriae under iron-restricted conditions
1Département de Pathologie et Microbiologie, Faculté de Médecine Vétérinaire, Université de Montréal, Saint-Hyacinthe, Québec.
Abstract:
Reference strains of Serpulina hyodysenteriae expressed at least three iron-regulated proteins with apparent molecular masses of > 200, 134, and 109 kDa when grown under iron-restricted conditions. Cells of S. hyodysenteriae grown under these conditions also showed increased outer membrane bleb formation when examined by electron microscopy after negative staining. S. hyodysenteriae did not use the 2 most common types of siderophore, namely catechol and hydroxamate. Western blotting with serum from a pig experimentally infected with S. hyodysenteriae B204 indicated that the 109-kDa major iron-regulated protein was expressed in vivo and was conserved among all strains tested.
Insights
Serpulina hyodysenteriae produces iron-regulated proteins and outer membrane blebs under iron deficiency. A key 109-kDa protein is expressed in vivo and conserved across strains, aiding in understanding swine dysentery pathogenesis.
Area of Science:
- Microbiology
- Veterinary Science
- Molecular Biology
Background:
- Serpulina hyodysenteriae is a swine pathogen causing swine dysentery.
- Iron acquisition is crucial for bacterial survival and virulence.
- Understanding iron-regulated mechanisms in S. hyodysenteriae is important for disease control.
Purpose of the Study:
- To investigate the iron-regulated proteins and outer membrane characteristics of Serpulina hyodysenteriae.
- To determine the in vivo expression and conservation of identified iron-regulated proteins.
Main Methods:
- Bacterial cultures grown under iron-restricted conditions.
- Analysis of iron-regulated proteins using SDS-PAGE and Western blotting.
- Electron microscopy for outer membrane structure examination.
- Siderophore analysis to identify iron uptake mechanisms.
Main Results:
- Three major iron-regulated proteins (>200, 134, and 109 kDa) were identified in S. hyodysenteriae.
- Increased outer membrane blebbing observed under iron restriction.
- S. hyodysenteriae does not utilize common catechol or hydroxamate siderophores.
- A 109-kDa iron-regulated protein was expressed in vivo and conserved across strains.
Conclusions:
- S. hyodysenteriae employs specific iron-regulated proteins, including a conserved 109-kDa protein, for iron acquisition.
- Outer membrane blebbing may play a role in the pathogen's response to iron limitation.
- These findings contribute to understanding the virulence factors of S. hyodysenteriae.