scholarly journals Negative-Strand RNA Virus L Proteins: One Machine, Many Activities

Cell ◽  
2015 ◽  
Vol 162 (2) ◽  
pp. 239-241 ◽  
Author(s):  
Kalyan Das ◽  
Eddy Arnold
Keyword(s):  
Rna Virus ◽  
Negative Strand ◽  
L Proteins ◽  
One Machine

scholarly journals Structure and Function of the N-Terminal Domain of the Vesicular Stomatitis Virus RNA Polymerase

2015 ◽  
Vol 90 (2) ◽  
pp. 715-724 ◽  
Author(s):  
Shihong Qiu ◽  
Minako Ogino ◽  
Ming Luo ◽  
Tomoaki Ogino ◽  
Todd J. Green
Keyword(s):  
Vesicular Stomatitis Virus ◽  
Rna Viruses ◽  
Rna Virus ◽  
Three Dimensional ◽  
Viral Transcription ◽  
Content Type ◽  
Negative Strand ◽  
Terminal Domain ◽  
Vesicular Stomatitis ◽  
L Proteins

ABSTRACTViruses have various mechanisms to duplicate their genomes and produce virus-specific mRNAs. Negative-strand RNA viruses encode their own polymerases to perform each of these processes. For the nonsegmented negative-strand RNA viruses, the polymerase is comprised of the large polymerase subunit (L) and the phosphoprotein (P). L proteins from members of theRhabdoviridae,Paramyxoviridae, andFiloviridaeshare sequence and predicted secondary structure homology. Here, we present the structure of the N-terminal domain (conserved region I) of the L protein from a rhabdovirus, vesicular stomatitis virus, at 1.8-Å resolution. The strictly and strongly conserved residues in this domain cluster in a single area of the protein. Serial mutation of these residues shows that many of the amino acids are essential for viral transcription but not for mRNA capping. Three-dimensional alignments show that this domain shares structural homology with polymerases from other viral families, including segmented negative-strand RNA and double-stranded RNA (dsRNA) viruses.IMPORTANCENegative-strand RNA viruses include a diverse set of viral families that infect animals and plants, causing serious illness and economic impact. The members of this group of viruses share a set of functionally conserved proteins that are essential to their replication cycle. Among this set of proteins is the viral polymerase, which performs a unique set of reactions to produce genome- and subgenome-length RNA transcripts. In this article, we study the polymerase of vesicular stomatitis virus, a member of the rhabdoviruses, which has served in the past as a model to study negative-strand RNA virus replication. We have identified a site in the N-terminal domain of the polymerase that is essential to viral transcription and that shares sequence homology with members of the paramyxoviruses and the filoviruses. Newly identified sites such as that described here could prove to be useful targets in the design of new therapeutics against negative-strand RNA viruses.

Engineered Resistance to Tomato Spotted Wilt Virus, a Negative-Strand RNA Virus

1993 ◽  
pp. 386-386
Author(s):  
Jan J. L. Gielen ◽  
Peter de Haan ◽  
Mart Q. J. M. van Grinsven ◽  
Rob Goldbach ◽  
André W. Schram
Keyword(s):  
Tomato Spotted Wilt Virus ◽  
Rna Virus ◽  
Negative Strand ◽  
Tomato Spotted Wilt ◽  
Engineered Resistance ◽  
Wilt Virus

De novo generation of a non-segmented negative strand RNA virus with a bicistronic gene

2009 ◽  
Vol 140 (1-2) ◽  
pp. 40-48 ◽  
Author(s):  
Olivier Touzelet ◽  
Noureddine Loukili ◽  
Thierry Pelet ◽  
Derek Fairley ◽  
Joseph Curran ◽  
...  
Keyword(s):  
De Novo ◽  
Rna Virus ◽  
Negative Strand
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