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Endogenous and Borrowed Proteolytic Activity in the Borrelia
- Source :
- Microbiology and Molecular Biology Reviews. 85
- Publication Year :
- 2021
- Publisher :
- American Society for Microbiology, 2021.
-
Abstract
- SUMMARY The Borrelia spp. are tick-borne pathogenic spirochetes that include the agents of Lyme disease and relapsing fever. As part of their life cycle, the spirochetes traffic between the tick vector and the vertebrate host, which requires significant physiological changes and remodeling of their outer membranes and proteome. This crucial proteome resculpting is carried out by a diverse set of proteases, adaptor proteins, and related chaperones. Despite its small genome, Borrelia burgdorferi has dedicated a large percentage of its genome to proteolysis, including a full complement of ATP-dependent proteases. Energy-driven proteolysis appears to be an important physiological feature of this dual-life-cycle bacterium. The proteolytic arsenal of Borrelia is strategically deployed for disposal of proteins no longer required as they move from one stage to another or are transferred from one host to another. Likewise, the Borrelia spp. are systemic organisms that need to break down and move through host tissues and barriers, and so their unique proteolytic resources, both endogenous and borrowed, make movement more feasible. Both the Lyme disease and relapsing fever Borrelia spp. bind plasminogen as well as numerous components of the mammalian plasminogen-activating system. This recruitment capacity endows the spirochetes with a borrowed proteolytic competency that can lead to increased invasiveness.
- Subjects :
- 0303 health sciences
Proteases
relapsing fever
medicine.diagnostic_test
030306 microbiology
Proteolysis
Proteolytic enzymes
Biology
bacterial infections and mycoses
biology.organism_classification
medicine.disease
Microbiology
03 medical and health sciences
Infectious Diseases
Lyme disease
Borrelia
Proteome
medicine
Borrelia burgdorferi
Molecular Biology
030304 developmental biology
Subjects
Details
- ISSN :
- 10985557 and 10922172
- Volume :
- 85
- Database :
- OpenAIRE
- Journal :
- Microbiology and Molecular Biology Reviews
- Accession number :
- edsair.doi...........77b91fd061d37ba53f2c5e0dbf3c91de