{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Khalfi P"],"funding":["Ligue Contre le Cancer","Ministère de la Recherche","Institut Pasteur","Centre National de la Recherche Scientifique"],"pagination":["e1011170"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9983871"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["19(2)"],"pubmed_abstract":["Viruses have evolved countless mechanisms to subvert and impair the host innate immune response. Measles virus (MeV), an enveloped, non-segmented, negative-strand RNA virus, alters the interferon response through different mechanisms, yet no viral protein has been described as directly targeting mitochondria. Among the crucial mitochondrial enzymes, 5'-aminolevulinate synthase (ALAS) is an enzyme that catalyzes the first step in heme biosynthesis, generating 5'-aminolevulinate from glycine and succinyl-CoA. In this work, we demonstrate that MeV impairs the mitochondrial network through the V protein, which antagonizes the mitochondrial enzyme ALAS1 and sequesters it to the cytosol. This re-localization of ALAS1 leads to a decrease in mitochondrial volume and impairment of its metabolic pot"],"journal":["PLoS pathogens"],"pubmed_title":["Antagonism of ALAS1 by the Measles Virus V protein contributes to degradation of the mitochondrial network and promotes interferon response."],"pmcid":["PMC9983871"],"funding_grant_id":["IP/SC-15364"],"pubmed_authors":["Ghozlane A","Suspene R","Volant S","Tangy F","Vartanian JP","Rigaud S","Caval V","Caignard G","Khalfi P","Berry N","Rufie C","Raymond KA","Thiers V","Combredet C","Komarova AV"],"additional_accession":[]},"is_claimable":false,"name":"Antagonism of ALAS1 by the Measles Virus V protein contributes to degradation of the mitochondrial network and promotes interferon response.","description":"Viruses have evolved countless mechanisms to subvert and impair the host innate immune response. Measles virus (MeV), an enveloped, non-segmented, negative-strand RNA virus, alters the interferon response through different mechanisms, yet no viral protein has been described as directly targeting mitochondria. Among the crucial mitochondrial enzymes, 5'-aminolevulinate synthase (ALAS) is an enzyme that catalyzes the first step in heme biosynthesis, generating 5'-aminolevulinate from glycine and succinyl-CoA. In this work, we demonstrate that MeV impairs the mitochondrial network through the V protein, which antagonizes the mitochondrial enzyme ALAS1 and sequesters it to the cytosol. This re-localization of ALAS1 leads to a decrease in mitochondrial volume and impairment of its metabolic pot","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Feb","modification":"2026-07-15T01:38:12.417Z","creation":"2025-04-05T19:16:45.017Z"},"accession":"S-EPMC9983871","cross_references":{"pubmed":["36802406"],"doi":["10.1371/journal.ppat.1011170"]}}