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Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092
Published on: October 2, 2017
Penicillin-binding proteins in the pathogenic intestinal spirochete Brachyspira pilosicoli
Rohana P Dassanayake1, Gautam Sarath, Gerald E Duhamel
1Department of Veterinary and Biomedical Sciences, University of Nebraska--Lincoln, Rm. 147, VBS Bldg., Lincoln, Nebraska 68583-0905, USA.
Abstract:
Penicillin-binding proteins (PBPs) of slightly different molecular masses (94, 62 or 68, 42 or 50, 25, and 22 kDa) were identified in one human and two porcine Brachyspira pilosicoli strains. Identification of PBPs of B. pilosicoli provides a basis for characterization of the genes encoding these proteins among pathogenic intestinal spirochetes of humans and animals.
Insights
Researchers identified penicillin-binding proteins (PBPs) in Brachyspira pilosicoli strains from humans and pigs. This finding aids in understanding the genes of these proteins in intestinal spirochetes.
Area of Science:
- Microbiology
- Molecular Biology
- Veterinary Medicine
Background:
- Brachyspira pilosicoli is a pathogenic intestinal spirochete affecting both humans and animals.
- Penicillin-binding proteins (PBPs) are essential targets for beta-lactam antibiotics.
- Understanding PBPs in B. pilosicoli is crucial for developing effective treatments.
Purpose of the Study:
- To identify and characterize penicillin-binding proteins (PBPs) in Brachyspira pilosicoli.
- To lay the groundwork for gene characterization of PBPs in pathogenic intestinal spirochetes.
Main Methods:
- Proteomic analysis was used to identify PBPs.
- Bacterial strains included one human and two porcine isolates of B. pilosicoli.
Main Results:
- Penicillin-binding proteins (PBPs) with varying molecular masses (94, 62/68, 42/50, 25, and 22 kDa) were identified.
- PBPs were detected in both human and porcine B. pilosicoli strains.
Conclusions:
- The identification of PBPs in B. pilosicoli is a significant step.
- This research provides a foundation for studying the genes encoding PBPs in pathogenic intestinal spirochetes of clinical and veterinary importance.
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