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Characterization of the Ebola virus nucleoprotein–RNA complex

When Ebola virus nucleoprotein (NP) is expressed in mammalian cells, it assembles into helical structures. Here, the recombinant NP helix purified from cells expressing NP was characterized biochemically and morphologically. We found that the recombinant NP helix is associated with non-viral RNA, wh...

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Detalles Bibliográficos
Autores principales: Noda, Takeshi, Hagiwara, Kyoji, Sagara, Hiroshi, Kawaoka, Yoshihiro
Formato: Texto
Lenguaje:English
Publicado: Society for General Microbiology 2010
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2878588/
https://www.ncbi.nlm.nih.gov/pubmed/20164259
http://dx.doi.org/10.1099/vir.0.019794-0
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author Noda, Takeshi
Hagiwara, Kyoji
Sagara, Hiroshi
Kawaoka, Yoshihiro
author_facet Noda, Takeshi
Hagiwara, Kyoji
Sagara, Hiroshi
Kawaoka, Yoshihiro
author_sort Noda, Takeshi
collection PubMed
description When Ebola virus nucleoprotein (NP) is expressed in mammalian cells, it assembles into helical structures. Here, the recombinant NP helix purified from cells expressing NP was characterized biochemically and morphologically. We found that the recombinant NP helix is associated with non-viral RNA, which is not protected from RNase digestion and that the morphology of the helix changes depending on the environmental salt concentration. The N-terminal 450 aa residues of NP are sufficient for these properties. However, digestion of the NP-associated RNA eliminates the plasticity of the helix, suggesting that this RNA is an essential structural component of the helix, binding to individual NP molecules via the N-terminal 450 aa. These findings enhance our knowledge of Ebola virus assembly and understanding of the Ebola virus life cycle.
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spelling pubmed-28785882011-06-01 Characterization of the Ebola virus nucleoprotein–RNA complex Noda, Takeshi Hagiwara, Kyoji Sagara, Hiroshi Kawaoka, Yoshihiro J Gen Virol Animal When Ebola virus nucleoprotein (NP) is expressed in mammalian cells, it assembles into helical structures. Here, the recombinant NP helix purified from cells expressing NP was characterized biochemically and morphologically. We found that the recombinant NP helix is associated with non-viral RNA, which is not protected from RNase digestion and that the morphology of the helix changes depending on the environmental salt concentration. The N-terminal 450 aa residues of NP are sufficient for these properties. However, digestion of the NP-associated RNA eliminates the plasticity of the helix, suggesting that this RNA is an essential structural component of the helix, binding to individual NP molecules via the N-terminal 450 aa. These findings enhance our knowledge of Ebola virus assembly and understanding of the Ebola virus life cycle. Society for General Microbiology 2010-06 /pmc/articles/PMC2878588/ /pubmed/20164259 http://dx.doi.org/10.1099/vir.0.019794-0 Text en Copyright © 2010, SGM
spellingShingle Animal
Noda, Takeshi
Hagiwara, Kyoji
Sagara, Hiroshi
Kawaoka, Yoshihiro
Characterization of the Ebola virus nucleoprotein–RNA complex
title Characterization of the Ebola virus nucleoprotein–RNA complex
title_full Characterization of the Ebola virus nucleoprotein–RNA complex
title_fullStr Characterization of the Ebola virus nucleoprotein–RNA complex
title_full_unstemmed Characterization of the Ebola virus nucleoprotein–RNA complex
title_short Characterization of the Ebola virus nucleoprotein–RNA complex
title_sort characterization of the ebola virus nucleoprotein–rna complex
topic Animal
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2878588/
https://www.ncbi.nlm.nih.gov/pubmed/20164259
http://dx.doi.org/10.1099/vir.0.019794-0
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