RT Journal Article
SR Electronic
T1 Glycosylation of Zika Virus Is Important in Host-Virus Interaction and Pathogenesis
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 564542
DO 10.1101/564542
A1 Nanda Kishore Routhu
A1 Sylvain D. Lehoux
A1 Emily A. Rouse
A1 Mehdi R. M. Bidokhti
A1 Leila B. Giron
A1 Alit Anzurez
A1 St Patrick Reid
A1 Mohamed Abdel-Mohsen
A1 Richard D. Cummings
A1 Siddappa N. Byrareddy
YR 2019
UL http://biorxiv.org/content/early/2019/03/01/564542.abstract
AB Zika virus (ZIKV) is a global public health issue due to its association with severe developmental disorders in infants and neurological disorders in adults. Because 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 information about Asn-linked (N-glycans) on ZIKV E, we analyzed ZIKV E of various strains derived from different cells. ZIKV E proteins are 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 discovered that ZIKV N-glycans are important in viral pathogenesis, as mannose-specific C-type lectins DC-SIGN and L-SIGN mediate cell entry of ZIKV. Our findings represent the first detailed mapping of N-glycans on ZIKV E of various strains and their functional significance.