Author
Listed:
- Xiaoxuan Qi
(Biomedical Sciences Research Complex, School of Chemistry, University of St Andrews, North Haugh)
- Shuiyun Lan
(Emory University School of Medicine)
- Wenjian Wang
(The First Affiliated Hospital, Sun Yat-Sen University)
- Lisa McLay Schelde
(Emory University School of Medicine)
- Haohao Dong
(Biomedical Sciences Research Complex, School of Chemistry, University of St Andrews, North Haugh)
- Gregor D. Wallat
(Biomedical Sciences Research Complex, School of Chemistry, University of St Andrews, North Haugh)
- Hinh Ly
(Emory University School of Medicine)
- Yuying Liang
(Emory University School of Medicine)
- Changjiang Dong
(Biomedical Sciences Research Complex, School of Chemistry, University of St Andrews, North Haugh)
Abstract
Lassa virus, the causative agent of Lassa fever, causes thousands of deaths annually and is a biological threat agent, for which there is no vaccine and limited therapy. The nucleoprotein (NP) of Lassa virus has essential roles in viral RNA synthesis and immune suppression, the molecular mechanisms of which are poorly understood. Here we report the crystal structure of Lassa virus NP at 1.80 Å resolution, which reveals amino (N)- and carboxy (C)-terminal domains with structures unlike any of the reported viral NPs. The N domain folds into a novel structure with a deep cavity for binding the m7GpppN cap structure that is required for viral RNA transcription, whereas the C domain contains 3′–5′ exoribonuclease activity involved in suppressing interferon induction. To our knowledge this is the first X-ray crystal structure solved for an arenaviral NP, which reveals its unexpected functions and indicates unique mechanisms in cap binding and immune evasion. These findings provide great potential for vaccine and drug development.
Suggested Citation
Xiaoxuan Qi & Shuiyun Lan & Wenjian Wang & Lisa McLay Schelde & Haohao Dong & Gregor D. Wallat & Hinh Ly & Yuying Liang & Changjiang Dong, 2010.
"Cap binding and immune evasion revealed by Lassa nucleoprotein structure,"
Nature, Nature, vol. 468(7325), pages 779-783, December.
Handle:
RePEc:nat:nature:v:468:y:2010:i:7325:d:10.1038_nature09605
DOI: 10.1038/nature09605
Download full text from publisher
As the access to this document is restricted, you may want to search for a different version of it.
Corrections
All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:nature:v:468:y:2010:i:7325:d:10.1038_nature09605. See general information about how to correct material in RePEc.
If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.
We have no bibliographic references for this item. You can help adding them by using this form .
If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.
For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .
Please note that corrections may take a couple of weeks to filter through
the various RePEc services.