{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Fisch D"],"funding":["Cancer Research UK","Francis Crick Institute","Medical Research Council","The Francis Crick Institute","Japan Agency for Medical Research and Development","Ministry of Education, Culture, Sports, Science and Technology","Wellcome Trust","Boehringer Ingelheim Fonds"],"pagination":["108008"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7435695"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["32(6)"],"pubmed_abstract":["Interferon-inducible guanylate-binding proteins (GBPs) promote cell-intrinsic defense through host cell death. GBPs target pathogens and pathogen-containing vacuoles and promote membrane disruption for release of microbial molecules that activate inflammasomes. GBP1 mediates pyroptosis or atypical apoptosis of Salmonella Typhimurium (STm)- or Toxoplasma gondii (Tg)- infected human macrophages, respectively. The pathogen-proximal detection-mechanisms of GBP1 remain poorly understood, as humans lack functional immunity-related GTPases (IRGs) that assist murine Gbps. Here, we establish that GBP1 promotes the lysis of Tg-containing vacuoles and parasite plasma membranes, releasing Tg-DNA. In contrast, we show GBP1 targets cytosolic STm and recruits caspase-4 to the bacterial surface for its ac"],"journal":["Cell reports"],"pubmed_title":["Human GBP1 Differentially Targets Salmonella and Toxoplasma to License Recognition of Microbial Ligands and Caspase-Mediated Death."],"pmcid":["PMC7435695"],"funding_grant_id":["MR/P028225/1","MC_UP_1202/12","FC001076","FC001999","217202/Z/19/Z","JP18fk0108046","MR/P022138/1","108246/Z/15/Z","10011","10076","17K15677","091664/B/10/Z","JP18fk0108047","10004"],"pubmed_authors":["Shenoy AR","Encheva V","Yamamoto M","Frickel EM","Snijders AP","Collinson LM","Clough B","Bando H","Fisch D","Domart MC"],"additional_accession":[]},"is_claimable":false,"name":"Human GBP1 Differentially Targets Salmonella and Toxoplasma to License Recognition of Microbial Ligands and Caspase-Mediated Death.","description":"Interferon-inducible guanylate-binding proteins (GBPs) promote cell-intrinsic defense through host cell death. GBPs target pathogens and pathogen-containing vacuoles and promote membrane disruption for release of microbial molecules that activate inflammasomes. GBP1 mediates pyroptosis or atypical apoptosis of Salmonella Typhimurium (STm)- or Toxoplasma gondii (Tg)- infected human macrophages, respectively. The pathogen-proximal detection-mechanisms of GBP1 remain poorly understood, as humans lack functional immunity-related GTPases (IRGs) that assist murine Gbps. Here, we establish that GBP1 promotes the lysis of Tg-containing vacuoles and parasite plasma membranes, releasing Tg-DNA. In contrast, we show GBP1 targets cytosolic STm and recruits caspase-4 to the bacterial surface for its ac","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 Aug","modification":"2026-05-02T21:02:48.8Z","creation":"2020-08-24T07:07:27Z"},"accession":"S-EPMC7435695","cross_references":{"pubmed":["32783936"],"doi":["10.1016/j.celrep.2020.108008"]}}