Toxin delivery by the coat protein of an aphid-vectored plant virus provides plant resistance to aphids

2013 ◽  
Vol 32 (1) ◽  
pp. 102-105 ◽  
Author(s):  
Bryony C Bonning ◽  
Narinder Pal ◽  
Sijun Liu ◽  
Zhaohui Wang ◽  
S Sivakumar ◽  
...  
2013 ◽  
Vol 10 (1) ◽  
pp. 262 ◽  
Author(s):  
Daniel Mendes Ardisson-Araújo ◽  
Juliana Rocha ◽  
Márcio Hedil da Costa ◽  
Anamélia Bocca ◽  
André Dusi ◽  
...  

Molecules ◽  
2019 ◽  
Vol 25 (1) ◽  
pp. 65 ◽  
Author(s):  
Ya-Han Chen ◽  
Dong-Sheng Guo ◽  
Mei-Huan Lu ◽  
Jian-Ying Yue ◽  
Yan Liu ◽  
...  

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.


eLife ◽  
2015 ◽  
Vol 4 ◽  
Author(s):  
Xabier Agirrezabala ◽  
Eduardo Méndez-López ◽  
Gorka Lasso ◽  
M Amelia Sánchez-Pina ◽  
Miguel Aranda ◽  
...  

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.


2021 ◽  
Author(s):  
Shifan Wang ◽  
Huijuan Guo ◽  
Keyan Zhu-Salzman ◽  
Feng Ge ◽  
Yucheng Sun

AbstractApoptosis and autophagy are two most prominent forms of programmed cell deaths (PCD) that have been implicated in antiviral immunity in vertebrate and plant hosts. Arboviruses are able to coexist with its arthropod vectors by coordinating the PCD immunity, but the regulatory mechanism involved is largely unknown. We found that the coat protein (CP) of an insect-borne plant virus TYLCV directly interacted with a phosphatidylethanolamine-binding protein (PEBP) of its insect vector whitefly to negatively influence the MAPK signaling cascade. As a result, the apoptosis was activated in whitefly which increased viral loading. Simultaneously, the PEBP4-CP interaction liberated ATG8, the hallmark of autophagy initiation, and eliminates arbovirus. Furthermore, apoptosis-promoted virus loading was compromised by agonist-induced autophagy, but autophagy-associated suppression on virus loading was unaffected by apoptosis agonist or inhibitor, suggesting that virus loading was predominantly determined by autophagy rather than by apoptosis. Our results demonstrated that maintaining a mild immune response by coordinating apoptosis and autophagy processes presumably could facilitate coexistence of the arbovirus and its insect vector. Taken together, immune homeostasis shaped by two types of PCD may facilitate the arbovirus preservation within the insect vector.Graphical abstractHighlightsInteraction between whitefly PEBP4 and TYLCV CP suppresses phosphorylation of MAPK cascade, activating apoptosisTYLCV CP liberates PEBP4-bound ATG8, resulting in lipidation of ATG8 and initiation of autophagy.PEBP4 balances apoptosis and autophagy in viruliferous whitefly to optimize virus loading without obvious fitness cost.


2008 ◽  
Vol 19 (4) ◽  
pp. 354-364 ◽  
Author(s):  
Silvia Massa ◽  
Paola Simeone ◽  
Antonio Muller ◽  
Eugenio Benvenuto ◽  
Aldo Venuti ◽  
...  

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