RESUMEN
The increase in Antimicrobial resistance (AMR) microorganisms has been exacerbated by exposure to antimicrobial drugs (e.g. antibiotics). A solution to AMR may require academic researchers to not only contribute to the drug discovery pipeline through laboratory research, but also to engage and inform non-specialist audiences using a variety of interventions in order to change behaviour towards our use of antibiotics. In this paper, the authors describe a hands-on public engagement event focusing on AMR. 'A Spoonful of Soil', was created by drawing on the past experiences of the delivering team (also described), with planning focusing on clear concise messages, selection of an appropriate audience and ensuring the event would be of significant interest to the audience. The event had a significant footfall of over 300 visitors. Key messages which aimed to raise awareness of AMR and educate visitors on the actions and behaviours that can help address the global issue of AMR were delivered by appropriate experts successfully, however success in reaching audience cannot be concluded from the feedback and evaluation gathered.
Asunto(s)
Antibacterianos/metabolismo , Farmacorresistencia Bacteriana , Promoción de la Salud , Bacterias/efectos de los fármacos , Humanos , Salud Pública/educación , Microbiología del SueloRESUMEN
The Bacillus subtilis oxalate decarboxylase (EC ), YvrK, converts oxalate to formate and CO(2). YvrK and the related hypothetical proteins YoaN and YxaG from B. subtilis have been successfully overexpressed in Escherichia coli. Recombinant YvrK and YoaN were found to be soluble enzymes with oxalate decarboxylase activity only when expressed in the presence of manganese salts. No enzyme activity has yet been detected for YxaG, which was expressed as a soluble protein without the requirement for manganese salts. YvrK and YoaN were found to catalyze minor side reactions: oxalate oxidation to produce H(2)O(2); and oxalate-dependent, H(2)O(2)-independent dye oxidations. The oxalate decarboxylase activity of purified YvrK was O(2)-dependent. YvrK was found to contain between 0.86 and 1.14 atoms of manganese/subunit. EPR spectroscopy showed that the metal ion was predominantly but not exclusively in the Mn(II) oxidation state. The hyperfine coupling constant (A = 9.5 millitesla) of the main g = 2 signal was consistent with oxygen and nitrogen ligands with hexacoordinate geometry. The structure of YvrK was modeled on the basis of homology with oxalate oxidase, canavalin, and phaseolin, and its hexameric oligomerization was predicted by analogy with proglycinin and homogentisate 1,2-dioxygenase. Although YvrK possesses two potential active sites, only one could be fully occupied by manganese. The possibility that the C-terminal domain active site has no manganese bound and is buried in an intersubunit interface within the hexameric enzyme is discussed. A mechanism for oxalate decarboxylation is proposed, in which both Mn(II) and O(2) are cofactors that act together as a two-electron sink during catalysis.