Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 616, Issue -, Pages 82-88Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2022.05.059
Keywords
Lloviu virus; VP30; NP; Crystal structure; Interaction
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Funding
- National key R&D Program of China [2018YFD1000501]
- National Natural Science Foundation of China [32070267, 31622007, 31670237]
- Shandong Provincial Natural Science Foundation, China [ZR2019ZD48, ZR2020QC057]
- Taishan Scholars Project [tsqn201812079]
- Higher Educational Science and Technology Program of Jinan City [2020GXRC058]
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The interactions between the VP30 C-terminal domain (CTD) of Lloviu virus (LLOV) and its nucleoprotein (NP) fragment were confirmed, and the crystal structure of the chimeric dimeric LLOV NP-VP30 CTD was determined. This provides a preliminary model for investigating interactions between LLOV VP30 and NP and suggests a potential target for anti-filovirus drug development.
The family Filoviridae comprises many notorious viruses, such as Ebola virus (EBOV) and Marburg virus (MARV), that can infect humans and nonhuman primates. Lloviu virus (LLOV), a less well studied filovirus, is considered a potential pathogen for humans. The VP30 C-terminal domain (CTD) of these filoviruses exhibits nucleoprotein (NP) binding and plays an essential role in viral transcription, replication and assembly. In this study, we confirmed the interactions between LLOV VP30 CTD and its NP fragment, and also determined the crystal structure of the chimeric dimeric LLOV NP-VP30 CTD at 2.50 A resolution. The structure is highly conserved across the family Filoviridae. While in the dimer structure, only one VP30 CTD binds the NP fragment, which indicates that the interaction between LLOV VP30 CTD and NP is not strong. Our work provides a preliminary model to investigate the interactions between LLOV VP30 and NP and suggests a potential target for anti-filovirus drug development. (C) 2022 Elsevier Inc. All rights reserved.
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