About: Host phosphatidic acid phosphatase lipin1 is rate limiting for functional hepatitis C virus replicase complex formation

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About: Host phosphatidic acid phosphatase lipin1 is rate limiting for functional hepatitis C virus replicase complex formation Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	Host phosphatidic acid phosphatase lipin1 is rate limiting for functional hepatitis C virus replicase complex formation
Creator	Forns, Xavier Calvo, Gema Castro, Victoria Carrascosa, José Gastaminzaid, Pablo Id, Lidia Pé Rez-Del-Pulgarid, Sofía Rodriguez, María Vila-Pérez, Á
source	Medline; PMC
abstract	Hepatitis C virus (HCV) infection constitutes a significant health burden worldwide, because it is a major etiologic agent of chronic liver disease, cirrhosis and hepatocellular carcinoma. HCV replication cycle is closely tied to lipid metabolism and infection by this virus causes profound changes in host lipid homeostasis. We focused our attention on a phosphatidate phosphate (PAP) enzyme family (the lipin family), which mediate the conversion of phosphatidate to diacylglycerol in the cytoplasm, playing a key role in triglyceride biosynthesis and in phospholipid homeostasis. Lipins may also translocate to the nucleus to act as transcriptional regulators of genes involved in lipid metabolism. The best-characterized member of this family is lipin1, which cooperates with lipin2 to maintain glycerophospholipid homeostasis in the liver. Lipin1-deficient cell lines were generated by RNAi to study the role of this protein in different steps of HCV replication cycle. Using surrogate models that recapitulate different aspects of HCV infection, we concluded that lipin1 is rate limiting for the generation of functional replicase complexes, in a step downstream primary translation that leads to early HCV RNA replication. Infection studies in lipin1-deficient cells overexpressing wild type or phosphatase-defective lipin1 proteins suggest that lipin1 phosphatase activity is required to support HCV infection. Finally, ultrastructural and biochemical analyses in replication-independent models suggest that lipin1 may facilitate the generation of the membranous compartment that contains functional HCV replicase complexes.
has issue date	2018-09-18(xsd:dateTime)
bibo:doi	10.1371/journal.ppat.1007284
bibo:pmid	30226904
has license	cc-by
sha1sum (hex)	a62150169f3f45fa30e13124ba0ff6c1945f5c0e
schema:url	https://doi.org/10.1371/journal.ppat.1007284
resource representing a document's title	Host phosphatidic acid phosphatase lipin1 is rate limiting for functional hepatitis C virus replicase complex formation
has PubMed Central identifier	PMC6161900
has PubMed identifier	30226904
schema:publication	PLoS Pathog
resource representing a document's body	covid:a62150169f3f45fa30e13124ba0ff6c1945f5c0e#body_text
is schema:about of	named entity 'HOST' named entity 'PAP' named entity 'member' named entity 'HCV' named entity 'worldwide' named entity 'mediate' named entity 'biochemical' named entity 'HCV' named entity 'HCV' named entity 'studies' named entity 'host' named entity 'PHOSPHATIDIC ACID' named entity 'PHOSPHOLIPID HOMEOSTASIS' named entity 'MEDIATE' named entity 'BEST' named entity 'RNAI' named entity 'LIPIN1' named entity 'TRANSLOCATE' named entity 'STEP' named entity 'HOST' named entity 'DOWNSTREAM' named entity 'CONVERSION' named entity 'HEALTH' named entity 'OUR' named entity 'CHANGES' named entity 'REPLICATION' named entity 'FOCUSED' named entity 'REPLICASE' named entity 'DEFICIENT' named entity 'REQUIRED' named entity 'COMPLEXES' named entity 'MEMBRANOUS' named entity 'COMPARTMENT' named entity 'INVOLVED' named entity 'PROFOUND' named entity 'CAUSES' named entity 'SIGNIFICANT' named entity 'GLYCEROPHOSPHOLIPID' named entity 'HCV INFECTION' named entity 'RATE' named entity 'PLAYING' named entity 'TRIGLYCERIDE BIOSYNTHESIS' named entity 'ENZYME' named entity 'TO SUPPORT' named entity 'PROTEINS' named entity 'LEADS' named entity 'NUCLEUS' named entity 'ACT' named entity 'REPLICATION CYCLE' named entity 'STUDY' named entity 'ATTENTION' named entity 'LIPID HOMEOSTASIS' named entity 'CHARACTERIZED' named entity 'DEFECTIVE' named entity 'CELL LINES' named entity 'CYTOPLASM' named entity 'LIPIN' named entity 'CIRRHOSIS' named entity 'DIACYLGLYCEROL' named entity 'MEMBER OF' named entity 'TIED' named entity 'RNA REPLICATION' named entity 'EARLY' named entity 'AUTHOR' named entity 'INFECTION' named entity 'PROTEIN ' named entity 'GENES' named entity 'HEPATOCELLULAR CARCINOMA' named entity 'ETIOLOGIC AGENT' covid:arg/a62150169f3f45fa30e13124ba0ff6c1945f5c0e named entity 'BIOCHEMICAL' named entity 'STEPS' named entity 'SURROGATE'

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