Characterisation of the organophosphate hydrolase catalytic activity of SsoPox
Authors: Mikael Elias
Eric Chabriere
Julien Hiblot
Guillaume Gotthard
Journal: Scientific Reports (2012)
Discipline: Multidisciplinary
Keywords: SsoPox; lactonase; phosphotriesterase; Sulfolobus solfataricus; bioscavenger
Affiliations: URMITE UMR CNRS-IRD 6236, IFR48, Faculté de Médecine et de Pharmacie, Université de la Méditerranée, Marseille, France.

Abstract:  SsoPox is a lactonase endowed with promiscuous phosphotriesterase activity isolated from Sulfolobus solfataricus that belongs to the Phosphotriesterase-Like Lactonase family. Because of its intrinsic thermal stability, SsoPox is seen as an appealing candidate as a bioscavenger for organophosphorus compounds. A comprehensive kinetic characterisation of SsoPox has been performed with various phosphotriesters (insecticides) and phosphodiesters (nerve agent analogues) as substrates. We show that SsoPox is active for a broad range of OPs and remains active under denaturing conditions. In addition, its OP hydrolase activity is highly stimulated by anionic detergent at ambient temperature and exhibits catalytic efficiencies as high as k(cat)/K(M) of 10(5) M(-1)s(-1) against a nerve agent analogue. The structure of SsoPox bound to the phosphotriester fensulfothion reveals an unexpected and non-productive binding mode. This feature suggests that SsoPox's active site is sub-optimal for phosphotriester binding, which depends not only upon shape but also on localised charge of the ligand. 

Retracted: No

PubPeer comments:
 This paper describes SsoPox, a protein with phosphotriesterase activity isolated from Sulfolobus solfataricus, a hyperthermophilic archaeon. They describe the enzyme as an appealing candidate for biodecontamination of organophosphorus compounds. The authors declare no competing interests. ![file] However, authors of this paper appear on a patent, US8,372,618B2, with a PCT file date (April 2008), and a prior publication date of Dec 2010, both pre-dating the submission of this paper (8 June 2012). See: https: patentimages.storage.googleapis.com 3d 31 8e 4b2e8143b7fe9d US8372618.pdf This patent describes the use of hyperthermophilic phosphotriesterases for the decontamination of organophosphorus compounds . Could the authors please clarify why these (provisional) patent applications were not disclosed? ![file] , 
 Dr Bik, As you well know, scientific publications did not typically disclose patents related to the subject of the publication at that time, unless it constituted a competing financial interest (i.e. a license, royalties, etc; see The Duty to Disclose Patent Rights, by R. M Lebovitz, 2007). Accordingly, perhaps regrettably, several journal policies, at that time (and possibly still today), did not require the disclosure of patents related to the subject of the publication in that case. In light of the above, this patent was not licensed at the time of the publication, it was not still may not be viewed as a competing financial interest (See The Duty to Disclose Patent Rights, by R. M Lebovitz, 2007). Quote: Scientific research publications do not, as a rule, disclose the existence of patent rights associated with the subject matter of the publication.  With that said, and the greater efforts in the last decade to increase transparency and education of researchers around potential COI (mentioned by Lebovitz), this work published today would certainly include the patent information. And that would indeed be better. Thanks much, Mikael Elias , 
 Additional point: The patent that you are referring to, focuses on and protects specific mutants of the enzyme SsoPox, not the wild-type enzyme described in the paper. The simple reason as to why mutants can be patented is because they are artificial different molecules, with possibly different properties. The wild type enzyme cannot be patented. None of the proteins protected by the patent is in this research paper. These two pieces are therefore discussing different subject of study. ,