Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
6143478 | Virus Research | 2011 | 12 Pages |
Abstract
Tobacco mosaic virus mutants were engineered to alter either the stability or surface chemistry of the virion: within the coat protein, glutamic acid was exchanged for glutamine in a buried portion to enhance the inter-subunit binding stability (E50Q), or a hexahistidine tract was fused to the surface-exposed carboxy terminus of the coat protein (6xHis). Both mutant viruses were expected to possess specific metal ion affinities. They accumulated to high titers in plants, induced distinct phenotypes, and their physical properties during purification differed from each other and from wild type (wt) virus. Whereas 6xHis and wt virions contained RNA, the majority of E50Q protein assembled essentially without RNA into rods which frequently exceeded 2 μm in length. Electroless deposition of nickel metallized the outer surface of 6xHis virions, but the central channel of E50Q rods, with significantly more nanowires of increased length in comparison to those formed in wtTMV.
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Authors
Anan Kadri, Edgar MaiÃ, Nadja Amsharov, Alexander M. Bittner, Sinan Balci, Klaus Kern, Holger Jeske, Christina Wege,