BST2 inhibits infection of influenza A virus by promoting apoptosis of infected cells.
Identifieur interne : 000913 ( Main/Exploration ); précédent : 000912; suivant : 000914BST2 inhibits infection of influenza A virus by promoting apoptosis of infected cells.
Auteurs : Eunbi Yi [Corée du Sud] ; Jinsoo Oh [Corée du Sud] ; Hye-Ri Kang [Corée du Sud] ; Moon Jung Song [Corée du Sud] ; Se-Ho Park [Corée du Sud]Source :
- Biochemical and biophysical research communications [ 1090-2104 ] ; 2019.
Descripteurs français
- KwdFr :
- Animaux, Antigènes CD (génétique), Antigènes CD (immunologie), Apoptose (génétique), Apoptose (immunologie), Caspase-3 (génétique), Caspase-3 (immunologie), Caspase-9 (génétique), Caspase-9 (immunologie), Cellules HEK293, Cellules Vero, Cellules rénales canines Madin-Darby, Chiens, Cytochromes c (génétique), Cytochromes c (immunologie), Endoribonucleases (génétique), Endoribonucleases (immunologie), Humains, Immunité innée, Interactions hôte-pathogène (génétique), Interactions hôte-pathogène (immunologie), Poly(ADP-ribose) polymerases (génétique), Poly(ADP-ribose) polymerases (immunologie), Protein-Serine-Threonine Kinases (génétique), Protein-Serine-Threonine Kinases (immunologie), Protéine-1 liant la boite X (génétique), Protéine-1 liant la boite X (immunologie), Protéines liées au GPI (génétique), Protéines liées au GPI (immunologie), Régulation de l'expression des gènes, Réplication virale, Réticulum endoplasmique (génétique), Réticulum endoplasmique (immunologie), Sous-type H1N1 du virus de la grippe A (génétique), Sous-type H1N1 du virus de la grippe A (immunologie), Stress du réticulum endoplasmique (génétique), Stress du réticulum endoplasmique (immunologie), Transduction du signal.
- MESH :
- génétique : Antigènes CD, Apoptose, Caspase-3, Caspase-9, Cytochromes c, Endoribonucleases, Interactions hôte-pathogène, Poly(ADP-ribose) polymerases, Protein-Serine-Threonine Kinases, Protéine-1 liant la boite X, Protéines liées au GPI, Réticulum endoplasmique, Sous-type H1N1 du virus de la grippe A, Stress du réticulum endoplasmique.
- immunologie : Antigènes CD, Apoptose, Caspase-3, Caspase-9, Cytochromes c, Endoribonucleases, Interactions hôte-pathogène, Poly(ADP-ribose) polymerases, Protein-Serine-Threonine Kinases, Protéine-1 liant la boite X, Protéines liées au GPI, Réticulum endoplasmique, Sous-type H1N1 du virus de la grippe A, Stress du réticulum endoplasmique.
- Animaux, Cellules HEK293, Cellules Vero, Cellules rénales canines Madin-Darby, Chiens, Humains, Immunité innée, Régulation de l'expression des gènes, Réplication virale, Transduction du signal.
English descriptors
- KwdEn :
- Animals, Antigens, CD (genetics), Antigens, CD (immunology), Apoptosis (genetics), Apoptosis (immunology), Caspase 3 (genetics), Caspase 3 (immunology), Caspase 9 (genetics), Caspase 9 (immunology), Chlorocebus aethiops, Cytochromes c (genetics), Cytochromes c (immunology), Dogs, Endoplasmic Reticulum (genetics), Endoplasmic Reticulum (immunology), Endoplasmic Reticulum Stress (genetics), Endoplasmic Reticulum Stress (immunology), Endoribonucleases (genetics), Endoribonucleases (immunology), GPI-Linked Proteins (genetics), GPI-Linked Proteins (immunology), Gene Expression Regulation, HEK293 Cells, Host-Pathogen Interactions (genetics), Host-Pathogen Interactions (immunology), Humans, Immunity, Innate, Influenza A Virus, H1N1 Subtype (genetics), Influenza A Virus, H1N1 Subtype (immunology), Madin Darby Canine Kidney Cells, Poly(ADP-ribose) Polymerases (genetics), Poly(ADP-ribose) Polymerases (immunology), Protein-Serine-Threonine Kinases (genetics), Protein-Serine-Threonine Kinases (immunology), Signal Transduction, Vero Cells, Virus Replication, X-Box Binding Protein 1 (genetics), X-Box Binding Protein 1 (immunology).
- MESH :
- chemical , genetics : Antigens, CD, Caspase 3, Caspase 9, Cytochromes c, Endoribonucleases, GPI-Linked Proteins, Poly(ADP-ribose) Polymerases, Protein-Serine-Threonine Kinases, X-Box Binding Protein 1.
- chemical , immunology : Antigens, CD, Caspase 3, Caspase 9, Cytochromes c, Endoribonucleases, GPI-Linked Proteins, Poly(ADP-ribose) Polymerases, Protein-Serine-Threonine Kinases, X-Box Binding Protein 1.
- genetics : Apoptosis, Endoplasmic Reticulum, Endoplasmic Reticulum Stress, Host-Pathogen Interactions, Influenza A Virus, H1N1 Subtype.
- immunology : Apoptosis, Endoplasmic Reticulum, Endoplasmic Reticulum Stress, Host-Pathogen Interactions, Influenza A Virus, H1N1 Subtype.
- Animals, Chlorocebus aethiops, Dogs, Gene Expression Regulation, HEK293 Cells, Humans, Immunity, Innate, Madin Darby Canine Kidney Cells, Signal Transduction, Vero Cells, Virus Replication.
Abstract
BST2 is an antiviral factor that inhibits the release of enveloped virus at the plasma membrane via an unusual topology in which its N-terminal is in the cytosol while its C-terminal is anchored by glycophosphatidylinositol (GPI). BST2-deficient cells showed substantially higher release of virions than wild type cells. Influenza-infected BST2-deficient cells showed greatly reduced cytopathic effect (CPE) than wild type cells despite their generally robust virus production. This finding prompted us to determine whether BST2 was involved in the apoptotic process of virus-infected host cells. Our results revealed that BST2 might be involved in IRE1α-mediated ER stress pathway by increasing spliced form XBP-1. Consequently, levels of cytochrome C, caspase-3, caspase-9, and PARP as representative molecules of apoptosis were significantly increased in wild type cells than those in BST2-deficient cells. These results suggest that BST2 might participate in innate host defense by augmenting ER-stress-induced apoptotic signaling to inhibit the replication and spread of virus.
DOI: 10.1016/j.bbrc.2018.12.110
PubMed: 30594400
Affiliations:
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Electronic address: sehopark@korea.ac.kr.</nlm:affiliation><country xml:lang="fr">Corée du Sud</country><wicri:regionArea>College of Life Science and Biotechnology, Korea University, 145 Anam-ro, Seongbuk-gu, Seoul, 02841</wicri:regionArea><wicri:noRegion>02841</wicri:noRegion></affiliation></author></analytic><series><title level="j">Biochemical and biophysical research communications</title><idno type="eISSN">1090-2104</idno><imprint><date when="2019" type="published">2019</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Antigens, CD (genetics)</term><term>Antigens, CD (immunology)</term><term>Apoptosis (genetics)</term><term>Apoptosis (immunology)</term><term>Caspase 3 (genetics)</term><term>Caspase 3 (immunology)</term><term>Caspase 9 (genetics)</term><term>Caspase 9 (immunology)</term><term>Chlorocebus aethiops</term><term>Cytochromes c (genetics)</term><term>Cytochromes c (immunology)</term><term>Dogs</term><term>Endoplasmic Reticulum (genetics)</term><term>Endoplasmic Reticulum (immunology)</term><term>Endoplasmic Reticulum Stress (genetics)</term><term>Endoplasmic Reticulum Stress (immunology)</term><term>Endoribonucleases (genetics)</term><term>Endoribonucleases (immunology)</term><term>GPI-Linked Proteins (genetics)</term><term>GPI-Linked Proteins (immunology)</term><term>Gene Expression Regulation</term><term>HEK293 Cells</term><term>Host-Pathogen Interactions (genetics)</term><term>Host-Pathogen Interactions (immunology)</term><term>Humans</term><term>Immunity, Innate</term><term>Influenza A Virus, H1N1 Subtype (genetics)</term><term>Influenza A Virus, H1N1 Subtype (immunology)</term><term>Madin Darby Canine Kidney Cells</term><term>Poly(ADP-ribose) Polymerases (genetics)</term><term>Poly(ADP-ribose) Polymerases (immunology)</term><term>Protein-Serine-Threonine Kinases (genetics)</term><term>Protein-Serine-Threonine Kinases (immunology)</term><term>Signal Transduction</term><term>Vero Cells</term><term>Virus Replication</term><term>X-Box Binding Protein 1 (genetics)</term><term>X-Box Binding Protein 1 (immunology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Antigènes CD (génétique)</term><term>Antigènes CD (immunologie)</term><term>Apoptose (génétique)</term><term>Apoptose (immunologie)</term><term>Caspase-3 (génétique)</term><term>Caspase-3 (immunologie)</term><term>Caspase-9 (génétique)</term><term>Caspase-9 (immunologie)</term><term>Cellules HEK293</term><term>Cellules Vero</term><term>Cellules rénales canines Madin-Darby</term><term>Chiens</term><term>Cytochromes c (génétique)</term><term>Cytochromes c (immunologie)</term><term>Endoribonucleases (génétique)</term><term>Endoribonucleases (immunologie)</term><term>Humains</term><term>Immunité innée</term><term>Interactions hôte-pathogène (génétique)</term><term>Interactions hôte-pathogène (immunologie)</term><term>Poly(ADP-ribose) polymerases (génétique)</term><term>Poly(ADP-ribose) polymerases (immunologie)</term><term>Protein-Serine-Threonine Kinases (génétique)</term><term>Protein-Serine-Threonine Kinases (immunologie)</term><term>Protéine-1 liant la boite X (génétique)</term><term>Protéine-1 liant la boite X (immunologie)</term><term>Protéines liées au GPI (génétique)</term><term>Protéines liées au GPI (immunologie)</term><term>Régulation de l'expression des gènes</term><term>Réplication virale</term><term>Réticulum endoplasmique (génétique)</term><term>Réticulum endoplasmique (immunologie)</term><term>Sous-type H1N1 du virus de la grippe A (génétique)</term><term>Sous-type H1N1 du virus de la grippe A (immunologie)</term><term>Stress du réticulum endoplasmique (génétique)</term><term>Stress du réticulum endoplasmique (immunologie)</term><term>Transduction du signal</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Antigens, CD</term><term>Caspase 3</term><term>Caspase 9</term><term>Cytochromes c</term><term>Endoribonucleases</term><term>GPI-Linked Proteins</term><term>Poly(ADP-ribose) Polymerases</term><term>Protein-Serine-Threonine Kinases</term><term>X-Box Binding Protein 1</term></keywords><keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Antigens, CD</term><term>Caspase 3</term><term>Caspase 9</term><term>Cytochromes c</term><term>Endoribonucleases</term><term>GPI-Linked Proteins</term><term>Poly(ADP-ribose) Polymerases</term><term>Protein-Serine-Threonine Kinases</term><term>X-Box Binding Protein 1</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Apoptosis</term><term>Endoplasmic Reticulum</term><term>Endoplasmic Reticulum Stress</term><term>Host-Pathogen Interactions</term><term>Influenza A Virus, H1N1 Subtype</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Antigènes CD</term><term>Apoptose</term><term>Caspase-3</term><term>Caspase-9</term><term>Cytochromes c</term><term>Endoribonucleases</term><term>Interactions hôte-pathogène</term><term>Poly(ADP-ribose) polymerases</term><term>Protein-Serine-Threonine Kinases</term><term>Protéine-1 liant la boite X</term><term>Protéines liées au GPI</term><term>Réticulum endoplasmique</term><term>Sous-type H1N1 du virus de la grippe A</term><term>Stress du réticulum endoplasmique</term></keywords><keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Antigènes CD</term><term>Apoptose</term><term>Caspase-3</term><term>Caspase-9</term><term>Cytochromes c</term><term>Endoribonucleases</term><term>Interactions hôte-pathogène</term><term>Poly(ADP-ribose) polymerases</term><term>Protein-Serine-Threonine Kinases</term><term>Protéine-1 liant la boite X</term><term>Protéines liées au GPI</term><term>Réticulum endoplasmique</term><term>Sous-type H1N1 du virus de la grippe A</term><term>Stress du réticulum endoplasmique</term></keywords><keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>Apoptosis</term><term>Endoplasmic Reticulum</term><term>Endoplasmic Reticulum Stress</term><term>Host-Pathogen Interactions</term><term>Influenza A Virus, H1N1 Subtype</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Chlorocebus aethiops</term><term>Dogs</term><term>Gene Expression Regulation</term><term>HEK293 Cells</term><term>Humans</term><term>Immunity, Innate</term><term>Madin Darby Canine Kidney Cells</term><term>Signal Transduction</term><term>Vero Cells</term><term>Virus Replication</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Cellules HEK293</term><term>Cellules Vero</term><term>Cellules rénales canines Madin-Darby</term><term>Chiens</term><term>Humains</term><term>Immunité innée</term><term>Régulation de l'expression des gènes</term><term>Réplication virale</term><term>Transduction du signal</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">BST2 is an antiviral factor that inhibits the release of enveloped virus at the plasma membrane via an unusual topology in which its N-terminal is in the cytosol while its C-terminal is anchored by glycophosphatidylinositol (GPI). BST2-deficient cells showed substantially higher release of virions than wild type cells. Influenza-infected BST2-deficient cells showed greatly reduced cytopathic effect (CPE) than wild type cells despite their generally robust virus production. This finding prompted us to determine whether BST2 was involved in the apoptotic process of virus-infected host cells. Our results revealed that BST2 might be involved in IRE1α-mediated ER stress pathway by increasing spliced form XBP-1. Consequently, levels of cytochrome C, caspase-3, caspase-9, and PARP as representative molecules of apoptosis were significantly increased in wild type cells than those in BST2-deficient cells. These results suggest that BST2 might participate in innate host defense by augmenting ER-stress-induced apoptotic signaling to inhibit the replication and spread of virus.</div></front></TEI><affiliations><list><country><li>Corée du Sud</li></country><region><li>Région capitale de Séoul</li></region><settlement><li>Séoul</li></settlement></list><tree><country name="Corée du Sud"><region name="Région capitale de Séoul"><name sortKey="Yi, Eunbi" sort="Yi, Eunbi" uniqKey="Yi E" first="Eunbi" last="Yi">Eunbi Yi</name></region><name sortKey="Kang, Hye Ri" sort="Kang, Hye Ri" uniqKey="Kang H" first="Hye-Ri" last="Kang">Hye-Ri Kang</name><name sortKey="Oh, Jinsoo" sort="Oh, Jinsoo" uniqKey="Oh J" first="Jinsoo" last="Oh">Jinsoo Oh</name><name sortKey="Park, Se Ho" sort="Park, Se Ho" uniqKey="Park S" first="Se-Ho" last="Park">Se-Ho Park</name><name sortKey="Song, Moon Jung" sort="Song, Moon Jung" uniqKey="Song M" first="Moon Jung" last="Song">Moon Jung Song</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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