Centre National De La Recherche Scientifique

Université´ D'aix-marseille

University of Minnesota

Institut National De La Sante Et De La Recherche Medicale

Universitéde Strasbourg

Assistance Publique Hopitaux De Marseille

Aix-marseille Université

Université De La Méditerranée

Université Henri Poincaré-nancy I

Université Henri Poincaré Nancy 1

Gene and Green Tk

La Fondation Mediterranee Infection

Universite Dé Lorraine

Etablissement Francais Du Sang

Fondation Mediterranee Infection

Eric Chabriere

Mikael Elias

Didier Raoult

Saber Khelaifia

Bernard La Scola

Florence Fenollar

Julien Hiblot

Carlos Contreras-Martel

Mickael Elias

Juan Fontecilla-Camps

Olivier Rohr

David Daude

Christian Schwartz

Camille Gouiran

Jean-Christophe Lagier

Sara Bellali

Christophe Flaudrops

Lucile Pinault

Laurence Camoin

Pierre Gallian

Jacques Chiaroni

Marie Vialatte

Fabienne Bregeon

Disclosed are mutated phosphotriesterase enzymes with improved stability and activity, as well as their use in particular for degrading organophosphorus compounds.

Mutated PTE enzymes

Provided is a mutated hyperthermophilic PTE having a lactonase activity derived from a hyperthermophilic phosphotriesterase corresponding to the consensus sequence of SEQ ID NO: 1, the mutated PTE including the at least one mutation chosen amongst 55 putative positions and the mutated PTE having enhanced properties. Also provided are compositions including the mutated hyperthermophilic PTE and the uses thereof, notably as bioscavenger of organophosphate compounds or as quorum quencher of the bacteria using lactones to communicate.

Vulcanisaetal phosphotriesterase-like lactonases (PLL) having enhanced properties and the uses thereof

Mutated hyperthermophilic PTE having a lactonase activity derived from a hyperthermophilic phosphotriesterase corresponding to the consensus sequence of SEQ ID NO: 1, the mutated PTE including the at least one mutation chosen amongst 53 putative positions and the mutated PTE having enhanced properties. Also provided are compositions including the mutated hyperthermophilic PTE and the uses thereof, notably as bioscavenger of organophosphate compounds or as quorum quencher of the bacteria using lactones to communicate.

Sulfolobal phosphotriesterase-like (PLL) lactonases activity having enhanced properties and the uses thereof

The present invention describes the use of a composition including or constituted by at least one element chosen from:

Antiviral agent

A subject of the present invention is mutated hyperthermophilic phosphotriesterases (PTEs) possessing a lactonase activity, and their uses as bioscavengers within the context of the decontamination of the surfaces of materials, of the skin or mucous membranes, contaminated with organophosphorus compounds, or within the context of the preparation of medicaments which can be used within the context of the prevention or treatment of an external contamination or of an internal poisoning by ingestion or inhalation by organophosphorus compounds, or within the context of the pollution control of water polluted with organophosphorus compounds.

Mutated hyperthermophilic phosphotriesterases and their uses

A protein includes or is formed by: (i) SEQ ID NO: 1; (ii) any sequence that is derived from sequence SEQ ID NO: 1, for example, by the substitution, removal or addition of one or more amino acids, on the condition that the derivative sequence binds to the phosphate; (iii) any sequence that is homologous to sequence SEQ ID NO: 1, preferably having a homology of at least approximately 80% with sequence SEQ ID NO: 1, on the condition that the homologous sequence binds to the phosphate; or (iv) any fragment of one of the aforementioned sequences on the condition that the fragment binds to the phosphate, such as any fragment comprising at least approximately 20 contiguous amino acids in sequence SEQ ID NO: 1.

Phosphate-binding protein, pharmaceutical compositions containing same and use thereof

Growing community of inventors

Marseilles, France

Eric Chabriere