scholarly journals Identification of a Set of Proteins (C′ and C) Encoded by the Bicistronic P Gene of the Indiana Serotype of Vesicular Stomatitis Virus and Analysis of Their Effect on Transcription by the Viral RNA Polymerase

Virology ◽  
1996 ◽  
Vol 218 (2) ◽  
pp. 335-342 ◽  
Author(s):  
RICHARD W. PELUSO ◽  
JAMES C. RICHARDSON ◽  
JULIE TALON ◽  
MARTIN LOCK
Keyword(s):  
Rna Polymerase ◽  
Vesicular Stomatitis Virus ◽  
Viral Rna ◽  
P Gene ◽  
Vesicular Stomatitis

scholarly journals Reviewing Chandipura: A Vesiculovirus in Human Epidemics

2007 ◽  
Vol 27 (4-5) ◽  
pp. 275-298 ◽  
Author(s):  
Soumen Basak ◽  
Arindam Mondal ◽  
Smarajit Polley ◽  
Subhradip Mukhopadhyay ◽  
Dhrubajyoti Chattopadhyay
Keyword(s):  
Life Cycle ◽  
Vesicular Stomatitis Virus ◽  
Drug Targets ◽  
Viral Rna ◽  
Virus Life Cycle ◽  
Chandipura Virus ◽  
Comprehensive Picture ◽  
Vesicular Stomatitis ◽  
Potential Drug Targets ◽  
Shed Light

Chandipura virus, a member of the rhabdoviridae family and vesiculovirus genera, has recently emerged as human pathogen that is associated with a number of outbreaks in different parts of India. Although, the virus closely resembles with the prototype vesiculovirus, Vesicular Stomatitis Virus, it could be readily distinguished by its ability to infect humans. Studies on Chandipura virus while shed light into distinct stages of viral infection; it may also allow us to identify potential drug targets for antiviral therapy. In this review, we have summarized our current understanding of Chandipura virus life cycle at the molecular detail with particular interest in viral RNA metabolisms, namely transcription, replication and packaging of viral RNA into nucleocapsid structure. Contemporary research on otherwise extensively studied family member Vesicular Stomatitis Virus has also been addressed to present a more comprehensive picture of vesiculovirus life cycle. Finally, we reveal examples of protein economy in Chandipura virus life-cycle whereby each viral protein has evolved complexity to perform multiple tasks.

Enhancement of vesicular stomatitis virus production by serum

1971 ◽  
Vol 17 (9) ◽  
pp. 1149-1155
Author(s):  
G. M. Kouroupis ◽  
L. R. Sabina
Keyword(s):  
Vesicular Stomatitis Virus ◽  
Virus Production ◽  
Viral Rna ◽  
Radioactive Label ◽  
Serum Free ◽  
Mdbk Cells ◽  
Time Of Infection ◽  
Vesicular Stomatitis ◽  
Free Media ◽  
Replicative Cycle

The production of vesicular stomatitis virus in MDBK cells has been shown to be markedly enhanced by the addition of whole serum to maintenance media. Maximum virus production occurred in the presence of human and fetal calf sera. When different serum protein fractions were tested, cultures nourished with medium containing bovine fraction IV-1 gave the highest infectivity, but fraction IV-1 did not completely substitute for whole serum. In contrast, fetuin was strongly inhibitory for the production of infectious virus. No loss of infectivity was observed if serum was added to cultures as late as 8 h postinfection. The incorporation of 3H-uridine into viral RNA of actinomycin D treated cultures nourished with serum or serum-free media proceeded at nearly similar rates from the time of infection up to 7 h postinfection. This result indicates that viral RNA synthesis was initiated with equal amounts of template. Late in the virus replicative cycle the incorporation rates of radioactive label were higher in serum-containing cultures than in serum-free cultures. The results of this investigation suggest that serum does not have a direct specific viral function but rather acts indirectly through the host cell to promote maximum virus production.

scholarly journals A Polyamide Inhibits Replication of Vesicular Stomatitis Virus by Targeting RNA in the Nucleocapsid

2018 ◽  
Vol 92 (8) ◽  
pp. e00146-18 ◽  
Author(s):  
Ryan H. Gumpper ◽  
Weike Li ◽  
Carlos H. Castañeda ◽  
M. José Scuderi ◽  
James K. Bashkin ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Vesicular Stomatitis Virus ◽  
Ebola Virus ◽  
Rna Viruses ◽  
Rna Virus ◽  
Viral Rna ◽  
Negative Strand ◽  
Double Stranded Dna ◽  
Vesicular Stomatitis ◽  
Syncytial Virus

ABSTRACTPolyamides have been shown to bind double-stranded DNA by complementing the curvature of the minor groove and forming various hydrogen bonds with DNA. Several polyamide molecules have been found to have potent antiviral activities against papillomavirus, a double-stranded DNA virus. By analogy, we reason that polyamides may also interact with the structured RNA bound in the nucleocapsid of a negative-strand RNA virus. Vesicular stomatitis virus (VSV) was selected as a prototype virus to test this possibility since its genomic RNA encapsidated in the nucleocapsid forms a structure resembling one strand of an A-form RNA duplex. One polyamide molecule, UMSL1011, was found to inhibit infection of VSV. To confirm that the polyamide targeted the nucleocapsid, a nucleocapsid-like particle (NLP) was incubated with UMSL1011. The encapsidated RNA in the polyamide-treated NLP was protected from thermo-release and digestion by RNase A. UMSL1011 also inhibits viral RNA synthesis in the intracellular activity assay for the viral RNA-dependent RNA polymerase. The crystal structure revealed that UMSL1011 binds the structured RNA in the nucleocapsid. The conclusion of our studies is that the RNA in the nucleocapsid is a viable antiviral target of polyamides. Since the RNA structure in the nucleocapsid is similar in all negative-strand RNA viruses, polyamides may be optimized to target the specific RNA genome of a negative-strand RNA virus, such as respiratory syncytial virus and Ebola virus.IMPORTANCENegative-strand RNA viruses (NSVs) include several life-threatening pathogens, such as rabies virus, respiratory syncytial virus, and Ebola virus. There are no effective antiviral drugs against these viruses. Polyamides offer an exceptional opportunity because they may be optimized to target each NSV. Our studies on vesicular stomatitis virus, an NSV, demonstrated that a polyamide molecule could specifically target the viral RNA in the nucleocapsid and inhibit viral growth. The target specificity of the polyamide molecule was proved by its inhibition of thermo-release and RNA nuclease digestion of the RNA bound in a model nucleocapsid, and a crystal structure of the polyamide inside the nucleocapsid. This encouraging observation provided the proof-of-concept rationale for designing polyamides as antiviral drugs against NSVs.

scholarly journals Crystal Structure of the Oligomerization Domain of the Phosphoprotein of Vesicular Stomatitis Virus

2006 ◽  
Vol 80 (6) ◽  
pp. 2808-2814 ◽  
Author(s):  
Haitao Ding ◽  
Todd J. Green ◽  
Shanyun Lu ◽  
Ming Luo
Keyword(s):  
Crystal Structure ◽  
Rna Polymerase ◽  
Vesicular Stomatitis Virus ◽  
Additional Stabilization ◽  
Vesicular Stomatitis ◽  
L Proteins ◽  
Α Helix ◽  
Nucleoprotein N ◽  
Β Sheet ◽  
Viral Nucleocapsid

ABSTRACT In the replication cycle of nonsegmented negative-strand RNA viruses, the viral RNA-dependent RNA polymerase (L) recognizes a nucleoprotein (N)-enwrapped RNA template during the RNA polymerase reaction. The viral phosphoprotein (P) is a polymerase cofactor essential for this recognition. We report here the 2.3-Å-resolution crystal structure of the central domain (residues 107 to 177) of P from vesicular stomatitis virus. The fold of this domain consists of a β hairpin, an α helix, and another β hairpin. The α helix provides the stabilizing force for forming a homodimer, while the two β hairpins add additional stabilization by forming a four-stranded β sheet through domain swapping between two molecules. This central dimer positions the N- and C-terminal domains of P to interact with the N and L proteins, allowing the L protein to specifically recognize the nucleocapsid-RNA template and to progress along the template while concomitantly assembling N with nascent RNA. The interdimer interactions observed in the noncrystallographic packing may offer insight into the mechanism of the RNA polymerase processive reaction along the viral nucleocapsid-RNA template.

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