scholarly journals Inhibitory Effect of Osthole from Cnidium monnieri on Tobacco Mosaic Virus (TMV) Infection in Nicotiana glutinosa

Molecules ◽  
2019 ◽  
Vol 25 (1) ◽  
pp. 65 ◽  
Author(s):  
Ya-Han Chen ◽  
Dong-Sheng Guo ◽  
Mei-Huan Lu ◽  
Jian-Ying Yue ◽  
Yan Liu ◽  
...  
Keyword(s):  
Coat Protein ◽  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Plant Virus ◽  
Inhibitory Effect ◽  
Nicotiana Glutinosa ◽  
1H And 13C Nmr ◽  
Virus Activity ◽  
Viral Particles ◽  
Coumarin Compound

The coumarin compound of osthole was extracted from Cnidium monnieri and identified by LC-MS and 1H- and 13C-NMR. Osthole was tested for anti-virus activity against tobacco mosaic virus (TMV) using the half-leaf method. The results showed that stronger antiviral activity on TMV infection appeared in Nicotiana glutinosa than that of eugenol and ningnanmycin, with inhibitory, protective, and curative effects of 72.57%, 70.26%, and 61.97%, respectively. Through observation of the TMV particles, we found that osthole could directly affect the viral particles. Correspondingly, the level of coat protein detected by Western blot was significantly reduced when the concentrations of osthole increased in tested plants compared to that of the control. These results suggest that osthole has anti-TMV activity and may be used as a biological reagent to control the plant virus in the half-leaf method.

scholarly journals The near-atomic cryoEM structure of a flexible filamentous plant virus shows homology of its coat protein with nucleoproteins of animal viruses

eLife ◽  
2015 ◽  
Vol 4 ◽  
Author(s):  
Xabier Agirrezabala ◽  
Eduardo Méndez-López ◽  
Gorka Lasso ◽  
M Amelia Sánchez-Pina ◽  
Miguel Aranda ◽  
...  
Keyword(s):  
Gene Transfer ◽  
Coat Protein ◽  
Mosaic Virus ◽  
Plant Virus ◽  
Plant Pathogens ◽  
Viral Rna ◽  
Electron Cryomicroscopy ◽  
Pepino Mosaic Virus ◽  
Viral Particles

Flexible filamentous viruses include economically important plant pathogens. Their viral particles contain several hundred copies of a helically arrayed coat protein (CP) protecting a (+)ssRNA. We describe here a structure at 3.9 Å resolution, from electron cryomicroscopy, of Pepino mosaic virus (PepMV), a representative of the genus Potexvirus (family Alphaflexiviridae). Our results allow modeling of the CP and its interactions with viral RNA. The overall fold of PepMV CP resembles that of nucleoproteins (NPs) from the genus Phlebovirus (family Bunyaviridae), a group of enveloped (-)ssRNA viruses. The main difference between potexvirus CP and phlebovirus NP is in their C-terminal extensions, which appear to determine the characteristics of the distinct multimeric assemblies – a flexuous, helical rod or a loose ribonucleoprotein. The homology suggests gene transfer between eukaryotic (+) and (-)ssRNA viruses.

A comparative differential scanning calorimetric study of tobacco mosaic virus and of its coat protein ts mutant

FEBS Letters ◽  
1998 ◽  
Vol 433 (3) ◽  
pp. 307-311 ◽  
Author(s):  
V.N. Orlov ◽  
S.V. Kust ◽  
P.V. Kalmykov ◽  
V.P. Krivosheev ◽  
E.N. Dobrov ◽  
...  
Keyword(s):  
Coat Protein ◽  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Differential Scanning Calorimetric ◽  
Calorimetric Study ◽  
Ts Mutant

Preparation and properties of recombinant DNA derived tobacco mosaic virus coat protein

Biochemistry ◽  
1990 ◽  
Vol 29 (21) ◽  
pp. 5119-5126 ◽  
Author(s):  
Steven J. Shire ◽  
Patrick McKay ◽  
David W. Leung ◽  
George J. Cachianes ◽  
Eugene Jackson ◽  
...  
Keyword(s):  
Coat Protein ◽  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Recombinant Dna ◽  
Virus Coat Protein ◽  
Virus Coat

The award of medals by the President, Sir Andrew Huxley, O.M., at the Anniversary Meeting, 30 November 1985

1986 ◽  
Vol 405 (1829) ◽  
pp. 181-184
Keyword(s):  
Electron Microscopy ◽  
Image Reconstruction ◽  
Coat Protein ◽  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Deep Insight ◽  
Living Matter ◽  
Fourier Image ◽  
Reconstruction Methods ◽  
Insight Into

The Copley Medal is awarded to Dr A. Klug, F. R. S., in recognition of his outstanding contributions to our understanding of complex biological structures and the methods used for determining them. Together with D. Kaspar, Klug developed a theory that predicted the arrangement of sub-units in the protein shells of spherical viruses. This theory brought order and understanding into a confused field ; nearly all the observed structures of small spherical viruses, many of them elucidated by Klug and his collaborators, are consistent with it. After more than 20 years’ work on tobacco mosaic virus Klug and his colleagues solved the structure of its coat protein in atomic detail. They also elucidated the mechanisms by which the helical virus particle assembles itself from its RNA and its 2130 protein sub-units. Recently his group succeeded in crystallizing chromatin, and solved its structure at a resolution sufficient to see the double-helical DNA coiled around the spool of histone. Many of Klug’s successes were made possible by his introduction of Fourier image reconstruction methods into electron microscopy. Klug’s work is characterized by deep insight into the physics of diffraction and image formation and the intricate geometry of living matter.

Kazakh strains of tobacco mosaic virus: two strains with potentially destabilizing amino acid substitutions in the coat protein

2000 ◽  
Vol 56 (2) ◽  
pp. 71-77 ◽  
Author(s):  
VICTOR K. NOVIKOV ◽  
EKATERINA V. BELENOVICH ◽  
EVGENY N. DOBROV ◽  
SERGEI K. ZAVRIEV
Keyword(s):  
Amino Acid ◽  
Coat Protein ◽  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Amino Acid Substitutions
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