| Autor: |
Alfadhli A; Vollum Institute and Department of Microbiology, Oregon Health Sciences University, Portland, Oregon 97201-3098, USA., Love Z, Arvidson B, Seeds J, Willey J, Barklis E |
| Jazyk: |
angličtina |
| Zdroj: |
Journal of virology [J Virol] 2001 Feb; Vol. 75 (4), pp. 2019-23. |
| DOI: |
10.1128/JVI.75.4.2019-2023.2001 |
| Abstrakt: |
Hantaviruses are enveloped, negative-strand RNA viruses which can be lethal to humans, causing either a hemorrhagic fever with renal syndrome or a hantaviral pulmonary syndrome. The viral genomes consist of three RNA segments: the L segment encodes the viral polymerase, the M segment encodes the viral surface glycoproteins G1 and G2, and the S segment encodes the nucleocapsid (N) protein. The N protein is a 420- to 430-residue, 50-kDa protein which appears to direct hantavirus assembly, although mechanisms of N protein oligomerization, RNA encapsidation, budding, and release are poorly understood. We have undertaken a biochemical and genetic analysis of N protein oligomerization. Bacterially expressed N proteins were found by gradient fractionation to associate not only as large multimers or aggregates but also as dimers or trimers. Chemical cross-linking of hantavirus particles yielded N protein cross-link products with molecular masses of 140 to 150 kDa, consistent with the size of an N trimer. We also employed a genetic, yeast two-hybrid method for monitoring N protein interactions. Analyses showed that the C-terminal half of the N protein plus the N-terminal 40 residues permitted association with a full-length N protein fusion. These N-terminal 40 residues of seven different hantavirus strains were predicted to form trimeric coiled coils. Our results suggest that coiled-coil motifs contribute to N protein trimerization and that nucleocapsid protein trimers are hantavirus particle assembly intermediates. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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