biostudies-literatureUnknown13Cabezas A<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 anFrontiers in microbiology843068https://www.ebi.ac.uk/biostudies/studies/S-EPMC8981391biostudies-literatureEnzyme 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.PMC8981391Cabezas ARibeiro JMCanales JCostas MJPinto RMRodrigues JRCameselle JCfalseEnzyme 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.<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 an2022-01-01T00:00:00Z20222025-04-04T13:26:06.931Z2024-11-19T16:36:21.322ZS-EPMC89813913539172710.3389/fmicb.2022.843068