Identification of a pocket factor that is critical to Zika virus assembly

Nadia M. DiNunno, Daniel J. Goetschius, Anoop Narayanan, Sydney A. Majowicz, Ibrahim Moustafa, Carol M. Bator, Susan L. Hafenstein and Joyce Jose ()
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Nadia M. DiNunno: The Pennsylvania State University
Daniel J. Goetschius: The Pennsylvania State University
Anoop Narayanan: The Pennsylvania State University
Sydney A. Majowicz: The Pennsylvania State University
Ibrahim Moustafa: The Pennsylvania State University
Carol M. Bator: The Pennsylvania State University
Susan L. Hafenstein: The Pennsylvania State University
Joyce Jose: The Pennsylvania State University

Nature Communications, 2020, vol. 11, issue 1, 1-8

Abstract: Abstract Zika virus (ZIKV) is an emerging mosquito borne flavivirus and a major public health concern causing severe disease. Due to the presence of a lipid membrane and structural heterogeneity, attaining an atomic resolution structure is challenging, but important to understand virus assembly and life cycle mechanisms that offer distinct targets for therapeutic intervention. We here use subvolume refinement to achieve a 3.4 Å resolution structure and identify two distinct lipid moieties. The first arises from the inner leaflet and is coordinated by hydrophobic residues of the M and E transmembrane helices that form a binding pocket not previously characterized. The second lipid arises from the outer leaflet coordinate between two E protein helices. Structure-based mutagenesis identifies critical hydrophobic interactions and their effect on the virus life cycle. Results show that lipids play an essential role in the ZIKV assembly pathway revealing a potential target of lipid based antiviral drug development.

Date: 2020
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-18747-4

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DOI: 10.1038/s41467-020-18747-4

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