{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["13"],"submitter":["Cabezas A"],"pubmed_abstract":["<i>Streptococcus suis</i> and <i>Streptococcus agalactiae</i> evade the innate immune system of the infected host by mechanisms mediated by cell wall-anchored proteins: SntA and CdnP, respectively. The former has been reported to interfere with complement responses, and the latter dampens STING-dependent type-I interferon (IFN) response by hydrolysis of bacterial cyclic-di-AMP (c-di-AMP). Both proteins are homologous but, while CdnP has been studied as a phosphohydrolase, the enzyme activities of SntA have not been investigated. The core structure of SntA was expressed in <i>Escherichia coli</i> as a GST-tagged protein that, after affinity purification, was characterized as phosphohydrolase with a large series of substrates. This included 3'-nucleotides, 2',3'-cyclic nucleotides, cyclic an"],"journal":["Frontiers in microbiology"],"pagination":["843068"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8981391"],"repository":["biostudies-literature"],"pubmed_title":["Enzyme Characterization of Pro-virulent SntA, a Cell Wall-Anchored Protein of <i>Streptococcus suis</i>, With Phosphodiesterase Activity on cyclic-di-AMP at a Level Suited to Limit the Innate Immune System."],"pmcid":["PMC8981391"],"pubmed_authors":["Cabezas A","Ribeiro JM","Canales J","Costas MJ","Pinto RM","Rodrigues JR","Cameselle JC"],"additional_accession":[]},"is_claimable":false,"name":"Enzyme Characterization of Pro-virulent SntA, a Cell Wall-Anchored Protein of <i>Streptococcus suis</i>, With Phosphodiesterase Activity on cyclic-di-AMP at a Level Suited to Limit the Innate Immune System.","description":"<i>Streptococcus suis</i> and <i>Streptococcus agalactiae</i> evade the innate immune system of the infected host by mechanisms mediated by cell wall-anchored proteins: SntA and CdnP, respectively. The former has been reported to interfere with complement responses, and the latter dampens STING-dependent type-I interferon (IFN) response by hydrolysis of bacterial cyclic-di-AMP (c-di-AMP). Both proteins are homologous but, while CdnP has been studied as a phosphohydrolase, the enzyme activities of SntA have not been investigated. The core structure of SntA was expressed in <i>Escherichia coli</i> as a GST-tagged protein that, after affinity purification, was characterized as phosphohydrolase with a large series of substrates. This included 3'-nucleotides, 2',3'-cyclic nucleotides, cyclic an","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022","modification":"2025-04-04T13:26:06.931Z","creation":"2024-11-19T16:36:21.322Z"},"accession":"S-EPMC8981391","cross_references":{"pubmed":["35391727"],"doi":["10.3389/fmicb.2022.843068"]}}