BST2 inhibits infection of influenza A virus by promoting apoptosis of infected cells
Copyright © 2018 The Authors. Published by Elsevier Inc. All rights reserved..
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.
Medienart: |
E-Artikel |
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Erscheinungsjahr: |
2019 |
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Erschienen: |
2019 |
Enthalten in: |
Zur Gesamtaufnahme - volume:509 |
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Enthalten in: |
Biochemical and biophysical research communications - 509(2019), 2 vom: 05. Feb., Seite 414-420 |
Sprache: |
Englisch |
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Beteiligte Personen: |
Yi, Eunbi [VerfasserIn] |
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Links: |
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Anmerkungen: |
Date Completed 22.10.2019 Date Revised 04.12.2021 published: Print-Electronic Citation Status MEDLINE |
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doi: |
10.1016/j.bbrc.2018.12.110 |
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funding: |
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Förderinstitution / Projekttitel: |
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PPN (Katalog-ID): |
NLM292234945 |
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520 | |a Copyright © 2018 The Authors. Published by Elsevier Inc. All rights reserved. | ||
520 | |a 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 | ||
650 | 4 | |a Journal Article | |
650 | 4 | |a Research Support, Non-U.S. Gov't | |
650 | 4 | |a Apoptosis | |
650 | 4 | |a BST2 | |
650 | 4 | |a ER stress | |
650 | 4 | |a Influenza virus | |
650 | 4 | |a Tetherin | |
650 | 7 | |a Antigens, CD |2 NLM | |
650 | 7 | |a BST2 protein, human |2 NLM | |
650 | 7 | |a GPI-Linked Proteins |2 NLM | |
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700 | 1 | |a Song, Moon Jung |e verfasserin |4 aut | |
700 | 1 | |a Park, Se-Ho |e verfasserin |4 aut | |
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