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Paradoxical β-lactamase activity of archaeal encoding enzymes

biorxiv. 2019; 
Seydina M.?Diene, Lucile?Pinault, Nicholas?Armstrong, Vivek?Keshri, Saber?Khelaifia, Eric?Chabrière, Gustavo?Caetano-Anolles, Jean-Marc?Rolain, Pierre?Pontarotti, Didier?Raoult
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Recombinant Proteins The selected beta-lactamases were optimized for protein expression in?Escherichia coliand synthesized by GenScript (Piscataway, NJ, USA) and then cloned into the pET24a(+) expression vector. Recombinant β-lactamases were expressed in?E. coli?BL21(DE3)-pGro7/GroEL (TaKaRa) using ZYP-5052 media. Each culture was grown at 37°C until reaching an OD600 nm = 0.8, followed by addition of L-arabinose (0.2% m/v) and induction with a temperature transition to 16°C over 20 hours.? Get A Quote

摘要

β-lactams targeting the bacterial cell wall are not efficient on archaea. Using phylogenetic analysis and common ancestor sequences for bacterial β-lactamases, we found serendipitously class B and class C-like β-lactamase genes in most archaea genomes. The class B β-lactamase appears to be highly conserved in archaea and to has been transferred in the bacterial genus?Elizabethkingia. The experimentaly expressed class B enzyme from?Methanosarcina barkeri?was able to digest penicillin G and was inhibited by a β-lactamase inhibitor (i.e. sulbactam). The class C-like β-lactamase was more closely related to DD-peptidase enzymes than know bacterial class C β-lactamases. The use of these very conserved genes... More

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