In Vivo and in Vitro Translation of the RNAS of Alfalfa Mosaic Virus

1977 ◽  
pp. 387-411 ◽  
Author(s):  
L. van Vloten-Doting ◽  
J. Bol ◽  
L. Neeleman ◽  
T. Rutgers ◽  
D. van Dalen ◽  
...  
Keyword(s):  
Mosaic Virus ◽  
Alfalfa Mosaic Virus ◽  
In Vitro Translation

Ribosomes are stalled during in vitro translation of alfalfa mosaic virus RNA 1

1985 ◽  
Vol 152 (3) ◽  
pp. 625-631 ◽  
Author(s):  
Pim LINDHOUT ◽  
Lyda NEELEMAN ◽  
Hans TOL ◽  
Lous VLOTEN-DOTING
Keyword(s):  
Mosaic Virus ◽  
Alfalfa Mosaic Virus ◽  
In Vitro Translation ◽  
Virus Rna

Comparison of in vivo and in vitro translation of Cowpea Mosaic Virus RNAs

1981 ◽  
Vol 99 (1) ◽  
pp. 89-94 ◽  
Author(s):  
R.W. Goldbach ◽  
J.G. Schilthuis ◽  
G. Rezelman
Keyword(s):  
Mosaic Virus ◽  
In Vitro Translation ◽  
Cowpea Mosaic Virus

scholarly journals In Vitro and In Vivo Studies of the RNA Conformational Switch in Alfalfa Mosaic Virus

2009 ◽  
Vol 84 (3) ◽  
pp. 1423-1429 ◽  
Author(s):  
Shih-Cheng Chen ◽  
René C. L. Olsthoorn
Keyword(s):  
Mosaic Virus ◽  
Binding Affinity ◽  
Linear Array ◽  
Alfalfa Mosaic Virus ◽  
In Vivo Studies ◽  
Conformational Switch ◽  
Stem Loop ◽  
Viral Replicase

ABSTRACT The 3′ termini of Alfalfa mosaic virus (AMV) RNAs adopt two mutually exclusive conformations, a coat protein binding (CPB) and a tRNA-like (TL) conformer, which consist of a linear array of stem-loop structures and a pseudoknot structure, respectively. Previously, switching between CPB and TL conformers has been proposed as a mechanism to regulate the competing processes of translation and replication of the viral RNA (R. C. L. Olsthoorn et al., EMBO J. 18:4856-4864, 1999). In the present study, the switch between CPB and TL conformers was further investigated. First, we showed that recognition of the AMV 3′ untranslated region (UTR) by a tRNA-specific enzyme (CCA-adding enzyme) in vitro is more efficient when the distribution is shifted toward the TL conformation. Second, the recognition of the 3′ UTR by the viral replicase was similarly dependent on the ratio of CBP and TL conformers. Furthermore, the addition of CP, which is expected to shift the distribution toward the CPB conformer, inhibited recognition by the CCA-adding enzyme and the replicase. Finally, we monitored how the binding affinity to CP is affected by this conformational switch in the yeast three-hybrid system. Here, disruption of the pseudoknot enhanced the binding affinity to CP by shifting the balance in favor of the CPB conformer, whereas stabilizing the pseudoknot did the reverse. Together, the in vitro and in vivo data clearly demonstrate the existence of the conformational switch in the 3′ UTR of AMV RNAs.

Expression of Alfalfa Mosaic virus RNA 4 cDNA transcripts in Vitro and in Vivo

Virology ◽  
1985 ◽  
Vol 146 (2) ◽  
pp. 177-187 ◽  
Author(s):  
L. Sue Loesch-Fries ◽  
Nancy P. Jarvis ◽  
Karen J. Krahn ◽  
Steven E. Nelson ◽  
Timothy C. Hall
Keyword(s):  
Mosaic Virus ◽  
Alfalfa Mosaic Virus ◽  
Virus Rna

scholarly journals IN VITRO AND IN VIVO INACTIVATION OF TOP AND BOTTOM FRACTION OF ALFALFA MOSAIC VIRUS (AMV)

Uirusu ◽  
1969 ◽  
Vol 19 (4) ◽  
pp. 164-165
Author(s):  
Tsutomu MATSUMOTO ◽  
Daiki MURAYAMA
Keyword(s):  
Mosaic Virus ◽  
Alfalfa Mosaic Virus ◽  
Bottom Fraction

scholarly journals Preparation of an Antiserum against an in vitro Translation Product of Alfalfa Mosaic Virus RNA 3

1985 ◽  
Vol 66 (8) ◽  
pp. 1669-1678 ◽  
Author(s):  
A. Berna ◽  
T. Godefroy-Colburn ◽  
C. Stussi-Garaud
Keyword(s):  
Mosaic Virus ◽  
Alfalfa Mosaic Virus ◽  
In Vitro Translation ◽  
Translation Product ◽  
Virus Rna

Flow cytometric analysis of tobacco and cowpea protoplasts infected in vivo and in vitro with alfalfa mosaic virus

1983 ◽  
Vol 2 (1) ◽  
pp. 19-25 ◽  
Author(s):  
P. van Klaveren ◽  
J. Slats ◽  
J. Roosien ◽  
Lous van Vloten-Doting
Keyword(s):  
Mosaic Virus ◽  
Flow Cytometric Analysis ◽  
Alfalfa Mosaic Virus ◽  
Flow Cytometric ◽  
Cowpea Protoplasts

In vitro translation of alfalfa mosaic virus RNA

1967 ◽  
Vol 23 (3) ◽  
pp. 535-IN24 ◽  
Author(s):  
J.C. van Ravenswaay Claasen ◽  
A.B.J. van Leeuwen ◽  
G.A.H. Duijts ◽  
L. Bosch
Keyword(s):  
Mosaic Virus ◽  
Alfalfa Mosaic Virus ◽  
In Vitro Translation ◽  
Virus Rna

scholarly journals Towards plant resistance to viruses using protein-only RNase P

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Anthony Gobert ◽  
Yifat Quan ◽  
Mathilde Arrivé ◽  
Florent Waltz ◽  
Nathalie Da Silva ◽  
...  
Keyword(s):  
Mosaic Virus ◽  
Virus Replication ◽  
Yield Loss ◽  
Rnase P ◽  
Plant Viruses ◽  
Yellow Mosaic Virus ◽  
Resistance To Viruses ◽  
Target Plant

AbstractPlant viruses cause massive crop yield loss worldwide. Most plant viruses are RNA viruses, many of which contain a functional tRNA-like structure. RNase P has the enzymatic activity to catalyze the 5′ maturation of precursor tRNAs. It is also able to cleave tRNA-like structures. However, RNase P enzymes only accumulate in the nucleus, mitochondria, and chloroplasts rather than cytosol where virus replication takes place. Here, we report a biotechnology strategy based on the re-localization of plant protein-only RNase P to the cytosol (CytoRP) to target plant viruses tRNA-like structures and thus hamper virus replication. We demonstrate the cytosol localization of protein-only RNase P in Arabidopsis protoplasts. In addition, we provide in vitro evidences for CytoRP to cleave turnip yellow mosaic virus and oilseed rape mosaic virus. However, we observe varied in vivo results. The possible reasons have been discussed. Overall, the results provided here show the potential of using CytoRP for combating some plant viral diseases.

scholarly journals Topical Application of Double-Stranded RNA Targeting 2b and CP Genes of Cucumber mosaic virus Protects Plants against Local and Systemic Viral Infection

Plants ◽  
2021 ◽  
Vol 10 (5) ◽  
pp. 963
Author(s):  
Maria C. Holeva ◽  
Athanasios Sklavounos ◽  
Rajendran Rajeswaran ◽  
Mikhail M. Pooggin ◽  
Andreas E. Voloudakis
Keyword(s):  
Cucumber Mosaic Virus ◽  
Mosaic Virus ◽  
Topical Application ◽  
Plant Virus ◽  
Plant Protection ◽  
Post Inoculation ◽  
Tobacco Plants ◽  
Double Stranded Rna

Cucumber mosaic virus (CMV) is a destructive plant virus with worldwide distribution and the broadest host range of any known plant virus, as well as a model plant virus for understanding plant–virus interactions. Since the discovery of RNA interference (RNAi) as a major antiviral defense, RNAi-based technologies have been developed for plant protection against viral diseases. In plants and animals, a key trigger of RNAi is double-stranded RNA (dsRNA) processed by Dicer and Dicer-like (DCL) family proteins in small interfering RNAs (siRNAs). In the present study, dsRNAs for coat protein (CP) and 2b genes of CMV were produced in vitro and in vivo and applied onto tobacco plants representing a systemic solanaceous host as well as on a local host plant Chenopodium quinoa. Both dsRNA treatments protected plants from local and systemic infection with CMV, but not against infection with unrelated viruses, confirming sequence specificity of antiviral RNAi. Antiviral RNAi was effective when dsRNAs were applied simultaneously with or four days prior to CMV inoculation, but not four days post inoculation. In vivo-produced dsRNAs were more effective than the in vitro-produced; in treatments with in vivo dsRNAs, dsRNA-CP was more effective than dsRNA-2b, while the effects were opposite with in vitro dsRNAs. Illumina sequencing of small RNAs from in vivo dsRNA-CP treated and non-treated tobacco plants revealed that interference with CMV infection in systemic leaves coincides with strongly reduced accumulation of virus-derived 21- and 22-nucleotide (nt) siRNAs, likely generated by tobacco DCL4 and DCL2, respectively. While the 21-nt class of viral siRNAs was predominant in non-treated plants, 21-nt and 22-nt classes accumulated at almost equal (but low) levels in dsRNA treated plants, suggesting that dsRNA treatment may boost DCL2 activity. Taken together, our findings confirm the efficacy of topical application of dsRNA for plant protection against viruses and shed more light on the mechanism of antiviral RNAi.

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