Glycosylation of zika virus is important in host–virus interaction and pathogenic potential

Nanda Kishore Routhu, Sylvain D. Lehoux, Emily A. Rouse, Mehdi R.M. Bidokhti, Leila B. Giron, Alitzel Anzurez, St Patrick Reid, Mohamed Abdel-Mohsen, Richard D. Cummings, Siddappa N. Byrareddy

Research output: Contribution to journalArticlepeer-review

6 Scopus citations


Zika virus (ZIKV) is a global public health issue due to its association with severe developmental disorders in infants and neurological disorders in adults. ZIKV uses glycosylation of its envelope (E) protein to interact with host cell receptors to facilitate entry; these interactions could also be important for designing therapeutics and vaccines. Due to a lack of proper information about Asn-linked (N-glycans) on ZIKV E, we analyzed ZIKV E of various strains derived from different cells. We found ZIKV E proteins being extensively modified with oligomannose, hybrid and complex N-glycans of a highly heterogeneous nature. Host cell surface glycans correlated strongly with the glycomic features of ZIKV E. Mechanistically, we observed that ZIKV N-glycans might play a role in viral pathogenesis, as mannose-specific C-type lectins DC-SIGN and L-SIGN mediate host cell entry of ZIKV. Our findings represent the first detailed mapping of N-glycans on ZIKV E of various strains and their functional significance.

Original languageEnglish (US)
Article number5206
JournalInternational journal of molecular sciences
Issue number20
StatePublished - Oct 2019


  • Envelope (E) protein
  • Glycoprotein
  • Host
  • Host cell surface glycans
  • Lectin array
  • Mass spectrometry
  • N-linked glycans
  • Virus interactions
  • Zika virus

ASJC Scopus subject areas

  • Catalysis
  • Molecular Biology
  • Spectroscopy
  • Computer Science Applications
  • Physical and Theoretical Chemistry
  • Organic Chemistry
  • Inorganic Chemistry


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