Molecular Targets and Strategies for Inhibition of the Bacterial Type III Secretion System (T3SS); Inhibitors Directly Binding to T3SS Components
| Autor: | Aaron E May, Julia A. Hotinger, Heather A Pendergrass |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
Cytoplasm
Genomic Islands medicine.drug_class Antibiotics lcsh:QR1-502 Virulence Review Biology medicine.disease_cause Biochemistry anti-virulence lcsh:Microbiology Type three secretion system 03 medical and health sciences Bacterial Proteins Protein Domains Salmonella Gram-Negative Bacteria medicine Type III Secretion Systems Basal body Animals Humans Molecular Biology Pathogen 030304 developmental biology antibacterials Adenosine Triphosphatases 0303 health sciences 030306 microbiology Effector Pathogenic bacteria biochemical phenomena metabolism and nutrition Translocon bacterial infections and mycoses inhibition Cell biology Anti-Bacterial Agents type III secretion system Protein Transport Periplasm bacteria Peptides Bacterial Outer Membrane Proteins Molecular Chaperones Protein Binding |
| Zdroj: | Biomolecules, Vol 11, Iss 316, p 316 (2021) Biomolecules |
| Popis: | The type III secretion system (T3SS) is a virulence apparatus used by many Gram-negative pathogenic bacteria to cause infections. Pathogens utilizing a T3SS are responsible for millions of infections yearly. Since many T3SS knockout strains are incapable of causing systemic infection, the T3SS has emerged as an attractive anti-virulence target for therapeutic design. The T3SS is a multiprotein molecular syringe that enables pathogens to inject effector proteins into host cells. These effectors modify host cell mechanisms in a variety of ways beneficial to the pathogen. Due to the T3SS’s complex nature, there are numerous ways in which it can be targeted. This review will be focused on the direct targeting of components of the T3SS, including the needle, translocon, basal body, sorting platform, and effector proteins. Inhibitors will be considered a direct inhibitor if they have a binding partner that is a T3SS component, regardless of the inhibitory effect being structural or functional. |
| Databáze: | OpenAIRE |
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