The nucleocapsid protein of human coronavirus NL63.
Human coronavirus (HCoV) NL63 was first described in 2004 and is associated with respiratory tract disease of varying severity. At the genetic and structural level, HCoV-NL63 is similar to other members of the Coronavirinae subfamily, especially human coronavirus 229E (HCoV-229E). Detailed analysis,...
| Main Authors: | , , , , , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Public Library of Science (PLoS)
2015-01-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC4336326?pdf=render |
| _version_ | 1818589889024753664 |
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| author | Kaja Zuwała Anna Golda Wojciech Kabala Michał Burmistrz Michal Zdzalik Paulina Nowak Sylwia Kedracka-Krok Mirosław Zarebski Jerzy Dobrucki Dominik Florek Sławomir Zeglen Jacek Wojarski Jan Potempa Grzegorz Dubin Krzysztof Pyrc |
| author_facet | Kaja Zuwała Anna Golda Wojciech Kabala Michał Burmistrz Michal Zdzalik Paulina Nowak Sylwia Kedracka-Krok Mirosław Zarebski Jerzy Dobrucki Dominik Florek Sławomir Zeglen Jacek Wojarski Jan Potempa Grzegorz Dubin Krzysztof Pyrc |
| author_sort | Kaja Zuwała |
| collection | DOAJ |
| description | Human coronavirus (HCoV) NL63 was first described in 2004 and is associated with respiratory tract disease of varying severity. At the genetic and structural level, HCoV-NL63 is similar to other members of the Coronavirinae subfamily, especially human coronavirus 229E (HCoV-229E). Detailed analysis, however, reveals several unique features of the pathogen. The coronaviral nucleocapsid protein is abundantly present in infected cells. It is a multi-domain, multi-functional protein important for viral replication and a number of cellular processes. The aim of the present study was to characterize the HCoV-NL63 nucleocapsid protein. Biochemical analyses revealed that the protein shares characteristics with homologous proteins encoded in other coronaviral genomes, with the N-terminal domain responsible for nucleic acid binding and the C-terminal domain involved in protein oligomerization. Surprisingly, analysis of the subcellular localization of the N protein of HCoV-NL63 revealed that, differently than homologous proteins from other coronaviral species except for SARS-CoV, it is not present in the nucleus of infected or transfected cells. Furthermore, no significant alteration in cell cycle progression in cells expressing the protein was observed. This is in stark contrast with results obtained for other coronaviruses, except for the SARS-CoV. |
| first_indexed | 2024-12-16T09:47:49Z |
| format | Article |
| id | doaj.art-bf5cef55310749e5820ee1887427fad2 |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-16T09:47:49Z |
| publishDate | 2015-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-bf5cef55310749e5820ee1887427fad22022-12-21T22:36:07ZengPublic Library of Science (PLoS)PLoS ONE1932-62032015-01-01102e011783310.1371/journal.pone.0117833The nucleocapsid protein of human coronavirus NL63.Kaja ZuwałaAnna GoldaWojciech KabalaMichał BurmistrzMichal ZdzalikPaulina NowakSylwia Kedracka-KrokMirosław ZarebskiJerzy DobruckiDominik FlorekSławomir ZeglenJacek WojarskiJan PotempaGrzegorz DubinKrzysztof PyrcHuman coronavirus (HCoV) NL63 was first described in 2004 and is associated with respiratory tract disease of varying severity. At the genetic and structural level, HCoV-NL63 is similar to other members of the Coronavirinae subfamily, especially human coronavirus 229E (HCoV-229E). Detailed analysis, however, reveals several unique features of the pathogen. The coronaviral nucleocapsid protein is abundantly present in infected cells. It is a multi-domain, multi-functional protein important for viral replication and a number of cellular processes. The aim of the present study was to characterize the HCoV-NL63 nucleocapsid protein. Biochemical analyses revealed that the protein shares characteristics with homologous proteins encoded in other coronaviral genomes, with the N-terminal domain responsible for nucleic acid binding and the C-terminal domain involved in protein oligomerization. Surprisingly, analysis of the subcellular localization of the N protein of HCoV-NL63 revealed that, differently than homologous proteins from other coronaviral species except for SARS-CoV, it is not present in the nucleus of infected or transfected cells. Furthermore, no significant alteration in cell cycle progression in cells expressing the protein was observed. This is in stark contrast with results obtained for other coronaviruses, except for the SARS-CoV.http://europepmc.org/articles/PMC4336326?pdf=render |
| spellingShingle | Kaja Zuwała Anna Golda Wojciech Kabala Michał Burmistrz Michal Zdzalik Paulina Nowak Sylwia Kedracka-Krok Mirosław Zarebski Jerzy Dobrucki Dominik Florek Sławomir Zeglen Jacek Wojarski Jan Potempa Grzegorz Dubin Krzysztof Pyrc The nucleocapsid protein of human coronavirus NL63. PLoS ONE |
| title | The nucleocapsid protein of human coronavirus NL63. |
| title_full | The nucleocapsid protein of human coronavirus NL63. |
| title_fullStr | The nucleocapsid protein of human coronavirus NL63. |
| title_full_unstemmed | The nucleocapsid protein of human coronavirus NL63. |
| title_short | The nucleocapsid protein of human coronavirus NL63. |
| title_sort | nucleocapsid protein of human coronavirus nl63 |
| url | http://europepmc.org/articles/PMC4336326?pdf=render |
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