Transient Structural Ordering of the RNA-Binding Domain of Carnation Mottle Virus p7 Movement Protein Modulates Nucleic Acid Binding

ChemBioChem ◽  
2005 ◽  
Vol 6 (8) ◽  
pp. 1391-1396 ◽  
Author(s):  
Marçal Vilar ◽  
Ana Saurí ◽  
Jose F. Marcos ◽  
Ismael Mingarro ◽  
Enrique Pérez-Payá
Keyword(s):  
Nucleic Acid ◽  
Rna Binding ◽  
Movement Protein ◽  
Binding Domain ◽  
Mottle Virus ◽  
Nucleic Acid Binding ◽  
Structural Ordering ◽  
Rna Binding Domain ◽  
Carnation Mottle Virus

scholarly journals Structural Properties of Carnation Mottle Virus p7 Movement Protein and Its RNA-binding Domain

2001 ◽  
Vol 276 (21) ◽  
pp. 18122-18129 ◽  
Author(s):  
Marçal Vilar ◽  
Vicent Esteve ◽  
Vicente Pallás ◽  
Jose F. Marcos ◽  
Enrique Pérez-Payá
Keyword(s):  
Structural Properties ◽  
Rna Binding ◽  
Movement Protein ◽  
Binding Domain ◽  
Mottle Virus ◽  
Rna Binding Domain ◽  
Carnation Mottle Virus

scholarly journals Mapping the RNA-binding domain on the Apple chlorotic leaf spot virus movement protein

2005 ◽  
Vol 86 (1) ◽  
pp. 225-229 ◽  
Author(s):  
Masamichi Isogai ◽  
Nobuyuki Yoshikawa
Keyword(s):  
Leaf Spot ◽  
Rna Binding ◽  
Movement Protein ◽  
Binding Domain ◽  
Sequence Specificity ◽  
Nucleic Acid Binding ◽  
Spot Virus ◽  
Uv Crosslinking ◽  
Chlorotic Leaf ◽  
Rna Binding Domain

The RNA-binding properties of the cell-to-cell movement protein (MP) of Apple chlorotic leaf spot virus were analysed. MP was expressed in Escherichia coli and was used in UV-crosslinking analysis, using a digoxigenin–UTP-labelled RNA probe and gel-retardation analysis. The analyses demonstrated that MP bound cooperatively to single-stranded RNA (ssRNA). When analysed for NaCl dependence of the RNA-binding activity, the majority of the MP could bind ssRNA even in binding buffer with 1 M NaCl. Furthermore, competition binding experiments showed that the MP bound preferentially to ssRNA and single-stranded DNA without sequence specificity. MP deletion mutants were used to identify the RNA-binding domain by UV-crosslinking analysis. Amino acid residues 82–126 and 127–287 potentially contain two independently active, single-stranded nucleic acid-binding domains.

scholarly journals The Solution Structure of the S1 RNA Binding Domain: A Member of an Ancient Nucleic Acid–Binding Fold

Cell ◽  
1997 ◽  
Vol 88 (2) ◽  
pp. 235-242 ◽  
Author(s):  
Mark Bycroft ◽  
Tim J.P Hubbard ◽  
Mark Proctor ◽  
Stefan M.V Freund ◽  
Alexey G Murzin
Keyword(s):  
Nucleic Acid ◽  
Solution Structure ◽  
Rna Binding ◽  
Binding Domain ◽  
Nucleic Acid Binding ◽  
Rna Binding Domain

scholarly journals Mutational analysis of the RNA-binding domain of the Prunus necrotic ringspot virus (PNRSV) movement protein reveals its requirement for cell-to-cell movement

Virology ◽  
2005 ◽  
Vol 339 (1) ◽  
pp. 31-41 ◽  
Author(s):  
Ma Carmen Herranz ◽  
Jesús-Angel Sanchez-Navarro ◽  
Ana Saurí ◽  
Ismael Mingarro ◽  
Vicente Pallás
Keyword(s):  
Rna Binding ◽  
Mutational Analysis ◽  
Movement Protein ◽  
Cell Movement ◽  
Binding Domain ◽  
Ringspot Virus ◽  
Prunus Necrotic Ringspot Virus ◽  
Rna Binding Domain

scholarly journals Tagging and Capturing of Lentiviral Vectors Using Short RNAs

2021 ◽  
Vol 22 (19) ◽  
pp. 10263
Author(s):  
Martin Panigaj ◽  
Michael P. Marino ◽  
Jakob Reiser
Keyword(s):  
Nucleic Acid ◽  
Rna Binding ◽  
Binding Domain ◽  
Rna Aptamer ◽  
Rna Sequences ◽  
Rna Binding Domain ◽  
Transgene Delivery ◽  
Vector Particles ◽  
Nucleic Acid Sequences

Lentiviral (LV) vectors have emerged as powerful tools for transgene delivery ex vivo but in vivo gene therapy applications involving LV vectors have faced a number of challenges, including the low efficiency of transgene delivery, a lack of tissue specificity, immunogenicity to both the product encoded by the transgene and the vector, and the inactivation of the vector by the human complement cascade. To mitigate these issues, several engineering approaches, involving the covalent modification of vector particles or the incorporation of specific protein domains into the vector’s envelope, have been tested. Short synthetic oligonucleotides, including aptamers bound to the surface of LV vectors, may provide a novel means with which to retarget LV vectors to specific cells and to shield these vectors from neutralization by sera. The purpose of this study was to develop strategies to tether nucleic acid sequences, including short RNA sequences, to LV vector particles in a specific and tight fashion. To bind short RNA sequences to LV vector particles, a bacteriophage lambda N protein-derived RNA binding domain (λN), fused to the measles virus hemagglutinin protein, was used. The λN protein bound RNA sequences bearing a boxB RNA hairpin. To test this approach, we used an RNA aptamer specific to the human epidermal growth factor receptor (EGFR), which was bound to LV vector particles via an RNA scaffold containing a boxB RNA motif. The results obtained confirmed that the EGFR-specific RNA aptamer bound to cells expressing EGFR and that the boxB containing the RNA scaffold was bound specifically to the λN RNA binding domain attached to the vector. These results show that LV vectors can be equipped with nucleic acid sequences to develop improved LV vectors for in vivo applications.

scholarly journals Mapping of the RNA-binding domain of the cucumber mosaic virus movement protein.

1997 ◽  
Vol 78 (8) ◽  
pp. 2095-2099 ◽  
Author(s):  
C Vaquero ◽  
J N√§hring ◽  
Y C Liao ◽  
R Fischer
Keyword(s):  
Cucumber Mosaic Virus ◽  
Mosaic Virus ◽  
Rna Binding ◽  
Movement Protein ◽  
Binding Domain ◽  
Virus Movement ◽  
Rna Binding Domain
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