Nucleocytoplasmic shuttling of BEFV M protein-modulated by lamin A/C and chromosome maintenance region 1 through a transcription-, carrier- and energy-dependent pathway
Copyright © 2024 Elsevier B.V. All rights reserved..
This study demonstrates for the first time that the matrix (M) protein of BEFV is a nuclear targeting protein that shuttles between the nucleus and the cytoplasm in a transcription-, carrier-, and energy-dependent manner. Experiments performed in both intact cells and digitonin-permeabilized cells revealed that M protein targets the nucleolus and requires carrier, cytosolic factors or energy input. By employing sequence and mutagenesis analyses, we have determined both nuclear localization signal (NLS) 6KKGKSK11 and nuclear export signal (NES) 98LIITSYL TI106 of M protein that are important for the nucleocytoplasmic shuttling of M protein. Furthermore, we found that both lamin A/C and chromosome maintenance region 1 (CRM-1) proteins could be coimmunoprecipitated and colocalized with the BEFV M protein. Knockdown of lamin A/C by shRNA and inhibition of CRM-1 by leptomycin B significantly reduced virus yield. Collectively, this study provides novel insights into nucleocytoplasmic shuttling of the BEFV M protein modulated by lamin A/C and CRM-1 and by a transcription- and carrier- and energy-dependent pathway.
Medienart: |
E-Artikel |
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Erscheinungsjahr: |
2024 |
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Erschienen: |
2024 |
Enthalten in: |
Zur Gesamtaufnahme - volume:291 |
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Enthalten in: |
Veterinary microbiology - 291(2024) vom: 01. März, Seite 110026 |
Sprache: |
Englisch |
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Beteiligte Personen: |
Chang, Yu-Kang [VerfasserIn] |
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Links: |
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Anmerkungen: |
Date Completed 13.03.2024 Date Revised 29.03.2024 published: Print-Electronic Citation Status MEDLINE |
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doi: |
10.1016/j.vetmic.2024.110026 |
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funding: |
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Förderinstitution / Projekttitel: |
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PPN (Katalog-ID): |
NLM368545377 |
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520 | |a Copyright © 2024 Elsevier B.V. All rights reserved. | ||
520 | |a This study demonstrates for the first time that the matrix (M) protein of BEFV is a nuclear targeting protein that shuttles between the nucleus and the cytoplasm in a transcription-, carrier-, and energy-dependent manner. Experiments performed in both intact cells and digitonin-permeabilized cells revealed that M protein targets the nucleolus and requires carrier, cytosolic factors or energy input. By employing sequence and mutagenesis analyses, we have determined both nuclear localization signal (NLS) 6KKGKSK11 and nuclear export signal (NES) 98LIITSYL TI106 of M protein that are important for the nucleocytoplasmic shuttling of M protein. Furthermore, we found that both lamin A/C and chromosome maintenance region 1 (CRM-1) proteins could be coimmunoprecipitated and colocalized with the BEFV M protein. Knockdown of lamin A/C by shRNA and inhibition of CRM-1 by leptomycin B significantly reduced virus yield. Collectively, this study provides novel insights into nucleocytoplasmic shuttling of the BEFV M protein modulated by lamin A/C and CRM-1 and by a transcription- and carrier- and energy-dependent pathway | ||
650 | 4 | |a Journal Article | |
650 | 4 | |a Bovine ephemeral fever virus | |
650 | 4 | |a CRM-1 | |
650 | 4 | |a Lamin A/C | |
650 | 4 | |a Matrix (M) protein | |
650 | 4 | |a Nuclear export signal (NES) | |
650 | 4 | |a Nuclear localization signal (NLS) | |
650 | 7 | |a Lamin Type A |2 NLM | |
650 | 7 | |a Nuclear Localization Signals |2 NLM | |
650 | 7 | |a Viral Structural Proteins |2 NLM | |
700 | 1 | |a Lin, Yi-Jyum |e verfasserin |4 aut | |
700 | 1 | |a Cheng, Ching-Yuan |e verfasserin |4 aut | |
700 | 1 | |a Tsai, Pei-Chien |e verfasserin |4 aut | |
700 | 1 | |a Wang, Chi-Young |e verfasserin |4 aut | |
700 | 1 | |a Nielsen, Brent L |e verfasserin |4 aut | |
700 | 1 | |a Liu, Hung-Jen |e verfasserin |4 aut | |
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