The nucleocapsid protein of human coronavirus NL63

PLoS One. 2015 Feb 20;10(2):e0117833. doi: 10.1371/journal.pone.0117833. eCollection 2015.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Calorimetry, Differential Scanning
  • Cell Cycle Checkpoints
  • Cell Line
  • Cloning, Molecular
  • Coronavirus NL63, Human / metabolism*
  • Coronavirus Nucleocapsid Proteins
  • HEK293 Cells
  • Humans
  • Macaca mulatta
  • Microscopy, Fluorescence
  • Nucleocapsid Proteins / chemistry
  • Nucleocapsid Proteins / genetics
  • Nucleocapsid Proteins / metabolism*
  • Protein Binding
  • Protein Multimerization
  • Protein Stability
  • RNA / chemistry
  • RNA / metabolism
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics


  • Coronavirus Nucleocapsid Proteins
  • Nucleocapsid Proteins
  • Recombinant Proteins
  • RNA

Grant support

This work was supported by the LIDER grant from the National Centre for Research and Development (Lider/27/55/L-2/10/2011) (KP) and Iuventus Plus grant from the Ministry of Science and Higher Education, Poland (IP 2010 033870 and IP2011 044371) (KP) and grants from the National Science Center (UMO-2012/05/B/NZ4/02428 (SKK), UMO-2011/01/D/NZ1/01169 (GD) and UMO-2012/07/E/NZ6/01712 (KP)). The Faculty of Biochemistry, Biophysics and Biotechnology of the Jagiellonian University is a beneficiary of the structural funds from the European Union (grant No: POIG.02.01.00-12-064/08 – “Molecular biotechnology for health”). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.