{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Colson P"],"funding":["Agence Nationale de la Recherche","Région Provence-Alpes-Côte d’Azur and Europe"],"pagination":["21685"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7729979"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["10(1)"],"pubmed_abstract":["Proteins with a metallo-beta-lactamase (MBL) fold have been largely studied in bacteria in the framework of resistance to beta-lactams, but their spectrum of activities is broader. We show here that the giant Tupanvirus also encodes a MBL fold-protein that has orthologs in other giant viruses, a deep phylogenetic root and is clustered with tRNases. This protein is significantly associated with translation components in giant viruses. After expression in Escherichia coli, it was found to hydrolyse nitrocefin, a beta-lactam, and penicillin G. This was inhibited by sulbactam, a beta-lactamase inhibitor. In addition, the tupanvirus MBL fold-protein was not active on single- or double-stranded DNA, but degraded RNAs from bacteria and Acanthamoeba castellanii, the tupanvirus amoebal host. This a"],"journal":["Scientific reports"],"pubmed_title":["A protein of the metallo-hydrolase/oxidoreductase superfamily with both beta-lactamase and ribonuclease activity is linked with translation in giant viruses."],"pmcid":["PMC7729979"],"funding_grant_id":["Méditerranée-Infection 10-IAHU-03","FEDER PA 0000320 PRIMMI"],"pubmed_authors":["Colson P","Pinault L","Azza S","Chabriere E","Pontarotti P","Armstrong N","Raoult D","La Scola B"],"additional_accession":[]},"is_claimable":false,"name":"A protein of the metallo-hydrolase/oxidoreductase superfamily with both beta-lactamase and ribonuclease activity is linked with translation in giant viruses.","description":"Proteins with a metallo-beta-lactamase (MBL) fold have been largely studied in bacteria in the framework of resistance to beta-lactams, but their spectrum of activities is broader. We show here that the giant Tupanvirus also encodes a MBL fold-protein that has orthologs in other giant viruses, a deep phylogenetic root and is clustered with tRNases. This protein is significantly associated with translation components in giant viruses. After expression in Escherichia coli, it was found to hydrolyse nitrocefin, a beta-lactam, and penicillin G. This was inhibited by sulbactam, a beta-lactamase inhibitor. In addition, the tupanvirus MBL fold-protein was not active on single- or double-stranded DNA, but degraded RNAs from bacteria and Acanthamoeba castellanii, the tupanvirus amoebal host. This a","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 Dec","modification":"2025-04-19T14:02:05.51Z","creation":"2021-02-20T11:33:19Z"},"accession":"S-EPMC7729979","cross_references":{"pubmed":["33303919"],"doi":["10.1038/s41598-020-78658-8"]}}