Details
| Originalsprache | Englisch |
|---|---|
| Seiten (von - bis) | 35-46 |
| Seitenumfang | 12 |
| Fachzeitschrift | Virus research |
| Jahrgang | 157 |
| Ausgabenummer | 1 |
| Publikationsstatus | Veröffentlicht - 8 Feb. 2011 |
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.
ASJC Scopus Sachgebiete
- Biochemie, Genetik und Molekularbiologie (insg.)
- Krebsforschung
- Immunologie und Mikrobiologie (insg.)
- Virologie
- Medizin (insg.)
- Infektionskrankheiten
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in: Virus research, Jahrgang 157, Nr. 1, 08.02.2011, S. 35-46.
Publikation: Beitrag in Fachzeitschrift › Artikel › Forschung › Peer-Review
}
TY - JOUR
T1 - Engineered Tobacco mosaic virus mutants with distinct physical characteristics in planta and enhanced metallization properties
AU - Kadri, Anan
AU - Maiß, Edgar
AU - Amsharov, Nadja
AU - Bittner, Alexander M.
AU - Balci, Sinan
AU - Kern, Klaus
AU - Jeske, Holger
AU - Wege, Christina
N1 - Funding Information: The authors thank the gardeners for taking care of the plants, Sigrid Kober and Sylvia Pfeiffer for excellent technical assistance, and Katharina Kittelmann, Robert G. Milne and Carl Krill for critically reading the manuscript. This work was funded by the Baden-Wuerttemberg-Stiftung, “Kompetenznetz Funktionelle Nanostrukturen”, and subsidiarily supported by the DFG-SPP1165.
PY - 2011/2/8
Y1 - 2011/2/8
N2 - 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.
AB - 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.
KW - Coat protein
KW - Metallization
KW - Mutation
KW - Nanotechnology
KW - Tobacco mosaic virus (TMV)
UR - http://www.scopus.com/inward/record.url?scp=79953027043&partnerID=8YFLogxK
U2 - 10.1016/j.virusres.2011.01.014
DO - 10.1016/j.virusres.2011.01.014
M3 - Article
C2 - 21310199
AN - SCOPUS:79953027043
VL - 157
SP - 35
EP - 46
JO - Virus research
JF - Virus research
SN - 0168-1702
IS - 1
ER -