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Título

One cannot rule them all: Are bacterial toxins antitoxins druggable?

Otros títulosDruggability of bacterial toxins-antitoxins
AutorChan, Wai Ting CSIC; Balsa, Dolors; Espinosa, Manuel CSIC ORCID
Palabras claveToxin-antitoxin operons
Drug discovery
Drug delivery
Antibacterials
Antivirals
Inhibitors of protein-protein interactions
Fecha de publicación16-ene-2015
CitaciónFEMS Microbiology Reviews
ResumenType II (proteic) toxin-antitoxin (TA) operons are widely spread in bacteria and archaea. They are organized as operons in which, usually, the antitoxin gene precedes the cognate toxin gene. The antitoxin is generally acting as a transcriptional self-repressor, whereas the toxin acts as a co-repressor, both proteins constituting a harmless complex. When bacteria encounter a stressful environment, TAs are triggered. The antitoxin protein is unstable and will be degraded by host proteases, releasing the free toxin to halt essential processes. The result is a detention of cell growth or even death. Because of their ubiquity and the essential processes targeted, TAs have been proposed as good candidates for development of novel antimicrobials. We discuss here the possible druggability of TAs as antivirals and antibacterials, with focus on the advantages and the challenges that their use may found in the ‘real’ world. We present strategies to develop TAs as antibacterials under the light of novel technologies, such as the use of very small molecules (fragments) as inhibitors of protein-protein interactions. Appropriate fragments could disrupt the T:A interfaces leading to the release of the targeted TA pair. Possible ways of delivery and formulation of TAs are also discussed.
Descripción53 p.-8 fig.-3 tab.
URIhttp://hdl.handle.net/10261/109433
ISSN0168-6445
E-ISSN1574-6976
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