Cap binding and immune evasion revealed by Lassa nucleoprotein structure

Xiaoxuan Qi, Shuiyun Lan, Wenjian Wang, Lisa McLay Schelde, Haohao Dong, Gregor D. Wallat, Hinh Ly (), Yuying Liang () and Changjiang Dong ()
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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

Nature, 2010, vol. 468, issue 7325, 779-783

Abstract: 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.

Date: 2010
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DOI: 10.1038/nature09605

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