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, Joyce Jose

Research output: Contribution to journalArticlepeer-review

26 Scopus citations


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.

Original languageEnglish (US)
Article number4953
JournalNature communications
Issue number1
StatePublished - Dec 1 2020

All Science Journal Classification (ASJC) codes

  • General Chemistry
  • General Biochemistry, Genetics and Molecular Biology
  • General Physics and Astronomy


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