The Endonucleolytic RNA Cleavage Function of nsp1 of Middle East Respiratory Syndrome Coronavirus Promotes the Production of Infectious Virus Particles in Specific Human Cell Lines.
Identifieur interne : 000790 ( Main/Merge ); précédent : 000789; suivant : 000791The Endonucleolytic RNA Cleavage Function of nsp1 of Middle East Respiratory Syndrome Coronavirus Promotes the Production of Infectious Virus Particles in Specific Human Cell Lines.
Auteurs : Keisuke Nakagawa [États-Unis] ; Krishna Narayanan [États-Unis] ; Masami Wada [États-Unis] ; Vsevolod L. Popov [États-Unis] ; Maria Cajimat [États-Unis] ; Ralph S. Baric [États-Unis] ; Shinji Makino [États-Unis]Source :
- Journal of virology [ 1098-5514 ] ; 2018.
Descripteurs français
- KwdFr :
- ARN messager (métabolisme), Animaux, Assemblage viral (génétique), Cellules HEK293, Cellules HeLa, Cellules Vero, Clivage de l'ARN (physiologie), Coronavirus du syndrome respiratoire du Moyen-Orient (génétique), Expression des gènes (génétique), Humains, Infections à coronavirus (anatomopathologie), Interféron bêta (biosynthèse), Interféron bêta (génétique), Interféron gamma (biosynthèse), Interféron gamma (génétique), Lignée cellulaire, Protéines virales non structurales (génétique), Protéines virales non structurales (métabolisme), Stabilité de l'ARN (physiologie).
- MESH :
- anatomopathologie : Infections à coronavirus.
- biosynthèse : Interféron bêta, Interféron gamma.
- génétique : Assemblage viral, Coronavirus du syndrome respiratoire du Moyen-Orient, Expression des gènes, Interféron bêta, Interféron gamma, Protéines virales non structurales.
- métabolisme : ARN messager, Protéines virales non structurales.
- physiologie : Clivage de l'ARN, Stabilité de l'ARN.
- Animaux, Cellules HEK293, Cellules HeLa, Cellules Vero, Humains, Lignée cellulaire.
English descriptors
- KwdEn :
- Animals, Cell Line, Chlorocebus aethiops, Coronavirus Infections (pathology), Gene Expression (genetics), HEK293 Cells, HeLa Cells, Humans, Interferon-beta (biosynthesis), Interferon-beta (genetics), Interferon-gamma (biosynthesis), Interferon-gamma (genetics), Middle East Respiratory Syndrome Coronavirus (genetics), RNA Cleavage (physiology), RNA Stability (physiology), RNA, Messenger (metabolism), Vero Cells, Viral Nonstructural Proteins (genetics), Viral Nonstructural Proteins (metabolism), Virus Assembly (genetics).
- MESH :
- chemical , biosynthesis : Interferon-beta, Interferon-gamma.
- genetics : Gene Expression, Interferon-beta, Interferon-gamma, Middle East Respiratory Syndrome Coronavirus, Viral Nonstructural Proteins, Virus Assembly.
- chemical , metabolism : RNA, Messenger, Viral Nonstructural Proteins.
- pathology : Coronavirus Infections.
- physiology : RNA Cleavage, RNA Stability.
- Animals, Cell Line, Chlorocebus aethiops, HEK293 Cells, HeLa Cells, Humans, Vero Cells.
Abstract
Middle East respiratory syndrome coronavirus (MERS-CoV) nsp1 suppresses host gene expression in expressed cells by inhibiting translation and inducing endonucleolytic cleavage of host mRNAs, the latter of which leads to mRNA decay. We examined the biological functions of nsp1 in infected cells and its role in virus replication by using wild-type MERS-CoV and two mutant viruses with specific mutations in the nsp1; one mutant lacked both biological functions, while the other lacked the RNA cleavage function but retained the translation inhibition function. In Vero cells, all three viruses replicated efficiently with similar replication kinetics, while wild-type virus induced stronger host translational suppression and host mRNA degradation than the mutants, demonstrating that nsp1 suppressed host gene expression in infected cells. The mutant viruses replicated less efficiently than wild-type virus in Huh-7 cells, HeLa-derived cells, and 293-derived cells, the latter two of which stably expressed a viral receptor protein. In 293-derived cells, the three viruses accumulated similar levels of nsp1 and major viral structural proteins and did not induce IFN-β and IFN-λ mRNAs; however, both mutants were unable to generate intracellular virus particles as efficiently as wild-type virus, leading to inefficient production of infectious viruses. These data strongly suggest that the endonucleolytic RNA cleavage function of the nsp1 promoted MERS-CoV assembly and/or budding in a 293-derived cell line. MERS-CoV nsp1 represents the first CoV gene 1 protein that plays an important role in virus assembly/budding and is the first identified viral protein whose RNA cleavage-inducing function promotes virus assembly/budding.IMPORTANCE MERS-CoV represents a high public health threat. Because CoV nsp1 is a major viral virulence factor, uncovering the biological functions of MERS-CoV nsp1 could contribute to our understanding of MERS-CoV pathogenicity and spur development of medical countermeasures. Expressed MERS-CoV nsp1 suppresses host gene expression, but its biological functions for virus replication and effects on host gene expression in infected cells are largely unexplored. We found that nsp1 suppressed host gene expression in infected cells. Our data further demonstrated that nsp1, which was not detected in virus particles, promoted virus assembly or budding in a 293-derived cell line, leading to efficient virus replication. These data suggest that nsp1 plays an important role in MERS-CoV replication and possibly affects virus-induced diseases by promoting virus particle production in infected hosts. Our data, which uncovered an unexpected novel biological function of nsp1 in virus replication, contribute to further understanding of the MERS-CoV replication strategies.
DOI: 10.1128/JVI.01157-18
PubMed: 30111568
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<front><div type="abstract" xml:lang="en">Middle East respiratory syndrome coronavirus (MERS-CoV) nsp1 suppresses host gene expression in expressed cells by inhibiting translation and inducing endonucleolytic cleavage of host mRNAs, the latter of which leads to mRNA decay. We examined the biological functions of nsp1 in infected cells and its role in virus replication by using wild-type MERS-CoV and two mutant viruses with specific mutations in the nsp1; one mutant lacked both biological functions, while the other lacked the RNA cleavage function but retained the translation inhibition function. In Vero cells, all three viruses replicated efficiently with similar replication kinetics, while wild-type virus induced stronger host translational suppression and host mRNA degradation than the mutants, demonstrating that nsp1 suppressed host gene expression in infected cells. The mutant viruses replicated less efficiently than wild-type virus in Huh-7 cells, HeLa-derived cells, and 293-derived cells, the latter two of which stably expressed a viral receptor protein. In 293-derived cells, the three viruses accumulated similar levels of nsp1 and major viral structural proteins and did not induce <i>IFN</i>
-β and <i>IFN</i>
-λ mRNAs; however, both mutants were unable to generate intracellular virus particles as efficiently as wild-type virus, leading to inefficient production of infectious viruses. These data strongly suggest that the endonucleolytic RNA cleavage function of the nsp1 promoted MERS-CoV assembly and/or budding in a 293-derived cell line. MERS-CoV nsp1 represents the first CoV gene 1 protein that plays an important role in virus assembly/budding and is the first identified viral protein whose RNA cleavage-inducing function promotes virus assembly/budding.<b>IMPORTANCE</b>
MERS-CoV represents a high public health threat. Because CoV nsp1 is a major viral virulence factor, uncovering the biological functions of MERS-CoV nsp1 could contribute to our understanding of MERS-CoV pathogenicity and spur development of medical countermeasures. Expressed MERS-CoV nsp1 suppresses host gene expression, but its biological functions for virus replication and effects on host gene expression in infected cells are largely unexplored. We found that nsp1 suppressed host gene expression in infected cells. Our data further demonstrated that nsp1, which was not detected in virus particles, promoted virus assembly or budding in a 293-derived cell line, leading to efficient virus replication. These data suggest that nsp1 plays an important role in MERS-CoV replication and possibly affects virus-induced diseases by promoting virus particle production in infected hosts. Our data, which uncovered an unexpected novel biological function of nsp1 in virus replication, contribute to further understanding of the MERS-CoV replication strategies.</div>
</front>
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