Structural Homology Between Nucleoproteins of ssRNA Viruses

Subcell Biochem. 2018:88:129-145. doi: 10.1007/978-981-10-8456-0_6.

Abstract

Our understanding of the viral world changed just after the first structures of icosahedral viral particles were unveiled. The structural similarities between capsid proteins of distant viral groups were not anticipated, and the findings suggested the existence of common ancestors for viruses with different host range, genomic structure and multiplication strategies. This way, diverse viruses with icosahedral particles can now be grouped based on the structural homology between their capsid proteins. In the last years, the presence of conserved folds between viral proteins in non-icosahedral viruses has also emerged. Viral particles with radically different morphologies, ranging from naked and filamentous to enveloped and pleomorphic, have shown structural homology between the nucleoproteins that bind directly to their genomes. This chapter overviews recent findings regarding the similar structure found between nucleoproteins of eukaryotic ssRNA viruses. The structural homology includes the coat proteins from all known families of flexible filamentous plant viruses, a group with monopartite (+)ssRNA genomes. Their coat proteins share a core domain with nucleoproteins of previously unrelated families of enveloped viruses that have segmented (-)ssRNA genomes. This last group consists of mostly animals viruses, including influenza virus.

Keywords: Capsid proteins; Icosahedral particles; Non-icosahedral particles; Nucleoproteins; Structural homology; ssRNA viruses.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Nucleoproteins / chemistry*
  • Nucleoproteins / genetics
  • Protein Domains
  • RNA Viruses / chemistry*
  • RNA Viruses / genetics
  • Structural Homology, Protein
  • Viral Proteins / chemistry*
  • Viral Proteins / genetics

Substances

  • Nucleoproteins
  • Viral Proteins