Crystal structure of the Měnglà virus VP30 C-terminal domain.

@article{Dong2020CrystalSO,
  title={Crystal structure of the Měngl{\`a} virus VP30 C-terminal domain.},
  author={Shishang Dong and Kangning Wen and Hongguan Chu and Hui Li and Qian-qian Yu and Changhui Wang and Xiaochun Qin},
  journal={Biochemical and biophysical research communications},
  year={2020}
}
  • S. Dong, K. Wen, X. Qin
  • Published 22 February 2020
  • Biology
  • Biochemical and biophysical research communications
1 Citations
Structural insights into the interactions between lloviu virus VP30 and nucleoprotein.

References

SHOWING 1-10 OF 24 REFERENCES
The Ebola Virus VP30-NP Interaction Is a Regulator of Viral RNA Synthesis
TLDR
Describing the interactions of Ebola, Sudan and Marburg virus VP30 with NP using in vitro biochemistry, structural biology and cell-based mini-replicon assays suggests that the VP30-NP interaction plays both essential and inhibitory roles in Ebola virus RNA synthesis.
Ebola Virus Transcription Activator VP30 Is a Zinc-Binding Protein
ABSTRACT Ebola virus VP30 is an essential activator of viral transcription. In viral particles, VP30 is closely associated with the nucleocapsid complex. A conspicuous structural feature of VP30 is
Crystal structure of the C-terminal domain of Ebola virus VP30 reveals a role in transcription and nucleocapsid association
TLDR
The structure and mutagenesis results reveal a potential pocket for small-molecule inhibitors that might prevent VP30 activity and thus virus propagation as it has been shown previously by peptides, which interfere with VP30 homooligomerization.
Characterization of a filovirus (Měnglà virus) from Rousettus bats in China
TLDR
The characterization of a phylogenetically distinct bat filovirus, named Měnglà virus (MLAV), whose genome shares 32–54% nucleotide sequence identity with known filoviruses, indicates a broad species cell tropism with a high risk of interspecies spillover transmission.
Ebola virus VP30 and nucleoprotein interactions modulate viral RNA synthesis
TLDR
A model where the eVP30–eNP interaction plays a critical role in transcription initiation and provides a novel target for the development of antiviral therapy is supported.
Oligomerization of Ebola Virus VP30 Is Essential for Viral Transcription and Can Be Inhibited by a Synthetic Peptide*
TLDR
The essential role of homo-oligomerization for the function of VP30 was corroborated by the finding that mixed VP30 oligomers consisting ofVP30 and transcriptionally inactive VP30 mutants were impaired in their ability to support EBOV transcription.
Characterization of the Envelope Glycoprotein of a Novel Filovirus, Lloviu Virus
TLDR
Interestingly, LLOV GP-pseudotyped VSV infected particular bat cell lines more efficiently than viruses bearing other filovirus GPs, suggesting that LLOV mediates cellular entry in a manner similar to that of the otherfiloviruses while showing preferential tropism for some bat cells.
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