Oligomerization of Hantavirus Nucleocapsid Protein: Analysis of the N-terminal Coiled-coil Domain.
From: Department of Virology, Haartman Institute, P.O. Box 21, FIN-00014 University of Helsinki, Helsinki, Finland.
Journal of virology
- Publish Date: Sep 2006
- ISSN: 0022-538X
- Volume: 80
- Issue: 18
- Pages: 9073-81
- Medium: Print
- Language: English
- Citation (JAMA): Alminaite Agne, Halttunen Vera, Kumar Vibhor, et al. Oligomerization of Hantavirus Nucleocapsid Protein: Analysis of the N-terminal Coiled-coil Domain.. J. Virol. Sep 2006;80:9073-81
Abstract
Hantaviruses constitute a genus in the family Bunyaviridae. They are enveloped negative-strand RNA viruses with a tripartite genome encoding the nucleocapsid (N) protein, the two surface glycoproteins Gn and Gc, and an RNA-dependent RNA polymerase. The N protein is the most abundant component of the virion; it encapsidates genomic RNA segments forming ribonucleoproteins and participates in genome transcription and replication as well as virus assembly. In the course of RNA encapsidation, N protein forms intermediate trimers via head-to-head and tail-to-tail interactions. We analyzed the amino-terminal trimerization domain (amino acid residues 1 to 77) of Tula hantavirus using computer modeling, mammalian two-hybrid assay, and immunofluorescence assay. The results obtained were consistent with the existence of an antiparallel coiled-coil stabilized by interactions between hydrophobic residues. Residues L44, V51, and L58 were important for the N-N interaction; other residues, e.g., L25 and V32, also made a contribution, albeit a modest one. Our alignments of the N-terminal domain of the hantaviral N proteins suggest the coiled-coil structure, and hence the mode of N-protein oligomerization, is conserved among hantaviruses.
Mesh Headings (Keywords): Amino Acid Sequence, Animals, COS Cells, Cercopithecus aethiops, Dimerization, Hantavirus, Hela Cells, Humans, Molecular Sequence Data, Nucleocapsid Proteins, Protein Conformation, Protein Structure, Secondary, Protein Structure, Tertiary, Sequence Homology, Amino Acid
Check for Full Text / PubMed Unique Identifier (PMID): 16940519
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