Insights into Paramyxovirus Nucleocapsids from Diverse Assemblies

• Published in: Viruses Vol. 13; no. 12; p. 2479
• Main Authors: Li, Tianhao, Shen, Qing-Tao
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 10.12.2021; MDPI
• Subjects: clam-shaped structure; Crystallography; double-headed nucleocapsids; Genomes; Life cycles; Models, Molecular; Mumps; Newcastle disease; NMR; Nuclear magnetic resonance; nucleocapsid; Nucleocapsid - chemistry; Nucleocapsid Proteins - chemistry; Nucleocapsid Proteins - genetics; Nucleocapsid Proteins - metabolism; Nucleocapsids; nucleoprotein; Nucleoproteins; Paramyxoviridae; Paramyxovirinae - chemistry; Paramyxovirinae - classification; Paramyxovirinae - genetics; Protein Conformation; Protein Domains; Protein Structure, Quaternary; Protein Subunits - chemistry; Review; Ribonucleic acid; RNA; Spectrum analysis; Transcription; Viruses; nucleocapsid; nucleoprotein; double-headed nucleocapsids; clam-shaped structure; Paramyxoviridae
• ISSN: 1999-4915; 1999-4915
• DOI: 10.3390/v13122479

All paramyxoviruses, which include the mumps virus, measles virus, Nipah virus, Newcastle disease virus, and Sendai virus, have non-segmented single-stranded negative-sense RNA genomes. These RNA genomes are enwrapped throughout the viral life cycle by nucleoproteins, forming helical nucleocapsids. In addition to these helical structures, recombinant paramyxovirus nucleocapsids may occur in other assembly forms such as rings, clam-shaped structures, and double-headed nucleocapsids; the latter two are composed of two single-stranded helices packed in a back-to-back pattern. In all of these assemblies, the neighboring nucleoprotein protomers adopt the same domain-swapping mode via the N-terminal arm, C-terminal arm, and recently disclosed N-hole. An intrinsically disordered region in the C-terminal domain of the nucleoproteins, called the N-tail, plays an unexpected role in regulating the transition among the different assembly forms that occurs with other viral proteins, especially phosphoprotein. These structures, together with the helical nucleocapsids, significantly enrich the structural diversity of the paramyxovirus nucleocapsids and help explain the functions of these diverse assemblies, including RNA genome protection, transcription, and replication, as well as encapsulation.