{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Ferrer-Orta C"],"funding":["PLATESA2 from Comunidad de Madrid/FEDER","Ministerio de Ciencia e Innovación (MCIN)","MEC | Instituto de Salud Carlos III","MEC | Consejo Superior de Investigaciones Científicas (CSIC)","Fundaci&amp;#x00F3; La Marato TV3","MEC | Instituto de Salud Carlos III (ISCIII)","Fundaci&amp;amp;#x00F3; La Marato TV3","Ministerio de Ciencia e Innovación","MEC | Consejo Superior de Investigaciones Científicas"],"pagination":["e2317977121"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11260105"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["121(29)"],"pubmed_abstract":["In a recent characterization of the Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) variability present in 30 diagnostic samples from patients of the first COVID-19 pandemic wave, 41 amino acid substitutions were documented in the RNA-dependent RNA polymerase (RdRp) nsp12. Eight substitutions were selected in this work to determine whether they had an impact on the RdRp activity of the SARS-CoV-2 nsp12-nsp8-nsp7 replication complex. Three of these substitutions were found around the polymerase central cavity, in the template entry channel (D499G and M668V), and within the motif B (V560A), and they showed polymerization rates similar to the wild type RdRp. The remaining five mutations (P323L, L372F, L372P, V373A, and L527H) were placed near the nsp12-nsp8<sub>F</sub> contact su"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["Point mutations at specific sites of the nsp12-nsp8 interface dramatically affect the RNA polymerization activity of SARS-CoV-2."],"pmcid":["PMC11260105"],"funding_grant_id":["PI21/00139","FI19/00119","CSIC-COV19-014","PID2020-117976 GB-I00","202136-31","202136-30","PID2020-113888RB-I00","S2018/BAA-4370","202220I116"],"pubmed_authors":["Verdaguer N","Domingo E","Vazquez-Monteagudo S","Ferrer-Orta C","Martinez-Gonzalez B","Perales C","Ferrero DS"],"additional_accession":[]},"is_claimable":false,"name":"Point mutations at specific sites of the nsp12-nsp8 interface dramatically affect the RNA polymerization activity of SARS-CoV-2.","description":"In a recent characterization of the Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) variability present in 30 diagnostic samples from patients of the first COVID-19 pandemic wave, 41 amino acid substitutions were documented in the RNA-dependent RNA polymerase (RdRp) nsp12. Eight substitutions were selected in this work to determine whether they had an impact on the RdRp activity of the SARS-CoV-2 nsp12-nsp8-nsp7 replication complex. Three of these substitutions were found around the polymerase central cavity, in the template entry channel (D499G and M668V), and within the motif B (V560A), and they showed polymerization rates similar to the wild type RdRp. The remaining five mutations (P323L, L372F, L372P, V373A, and L527H) were placed near the nsp12-nsp8<sub>F</sub> contact su","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Jul","modification":"2026-06-01T19:36:44.433Z","creation":"2025-02-19T02:01:53.861Z"},"accession":"S-EPMC11260105","cross_references":{"pubmed":["38990941"],"doi":["10.1073/pnas.2317977121"]}}