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 journalArticle

Abstract

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
Volume20
Issue number20
DOIs
StatePublished - Oct 2019

Fingerprint

Glycosylation
viruses
Viruses
Polysaccharides
interactions
cells
entry
Mannose-Binding Lectins
Glycomics
disorders
vaccines
C-Type Lectins
proteins
Proteins
Zika Virus
public health
pathogenesis
Vaccines
Public health
Mannose

Keywords

  • 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

Cite this

Glycosylation of zika virus is important in host–virus interaction and pathogenic potential. / Routhu, Nanda Kishore; Lehoux, Sylvain D.; Rouse, Emily A.; Bidokhti, Mehdi R.M.; Giron, Leila B.; Anzurez, Alitzel; Reid, St Patrick; Abdel-Mohsen, Mohamed; Cummings, Richard D.; Byrareddy, Siddappa N.

In: International journal of molecular sciences, Vol. 20, No. 20, 5206, 10.2019.

Research output: Contribution to journalArticle

Routhu, NK, Lehoux, SD, Rouse, EA, Bidokhti, MRM, Giron, LB, Anzurez, A, Reid, SP, Abdel-Mohsen, M, Cummings, RD & Byrareddy, SN 2019, 'Glycosylation of zika virus is important in host–virus interaction and pathogenic potential', International journal of molecular sciences, vol. 20, no. 20, 5206. https://doi.org/10.3390/ijms20205206
Routhu, Nanda Kishore ; Lehoux, Sylvain D. ; Rouse, Emily A. ; Bidokhti, Mehdi R.M. ; Giron, Leila B. ; Anzurez, Alitzel ; Reid, St Patrick ; Abdel-Mohsen, Mohamed ; Cummings, Richard D. ; Byrareddy, Siddappa N. / Glycosylation of zika virus is important in host–virus interaction and pathogenic potential. In: International journal of molecular sciences. 2019 ; Vol. 20, No. 20.
@article{9c0f87a61895471eafc8516c2874f2ee,
title = "Glycosylation of zika virus is important in host–virus interaction and pathogenic potential",
abstract = "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.",
keywords = "Envelope (E) protein, Glycoprotein, Host, Host cell surface glycans, Lectin array, Mass spectrometry, N-linked glycans, Virus interactions, Zika virus",
author = "Routhu, {Nanda Kishore} and Lehoux, {Sylvain D.} and Rouse, {Emily A.} and Bidokhti, {Mehdi R.M.} and Giron, {Leila B.} and Alitzel Anzurez and Reid, {St Patrick} and Mohamed Abdel-Mohsen and Cummings, {Richard D.} and Byrareddy, {Siddappa N.}",
year = "2019",
month = "10",
doi = "10.3390/ijms20205206",
language = "English (US)",
volume = "20",
journal = "International Journal of Molecular Sciences",
issn = "1661-6596",
publisher = "Multidisciplinary Digital Publishing Institute (MDPI)",
number = "20",

}

TY - JOUR

T1 - Glycosylation of zika virus is important in host–virus interaction and pathogenic potential

AU - Routhu, Nanda Kishore

AU - Lehoux, Sylvain D.

AU - Rouse, Emily A.

AU - Bidokhti, Mehdi R.M.

AU - Giron, Leila B.

AU - Anzurez, Alitzel

AU - Reid, St Patrick

AU - Abdel-Mohsen, Mohamed

AU - Cummings, Richard D.

AU - Byrareddy, Siddappa N.

PY - 2019/10

Y1 - 2019/10

N2 - 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.

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. 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.

KW - Envelope (E) protein

KW - Glycoprotein

KW - Host

KW - Host cell surface glycans

KW - Lectin array

KW - Mass spectrometry

KW - N-linked glycans

KW - Virus interactions

KW - Zika virus

UR - http://www.scopus.com/inward/record.url?scp=85073709331&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85073709331&partnerID=8YFLogxK

U2 - 10.3390/ijms20205206

DO - 10.3390/ijms20205206

M3 - Article

C2 - 31640124

AN - SCOPUS:85073709331

VL - 20

JO - International Journal of Molecular Sciences

JF - International Journal of Molecular Sciences

SN - 1661-6596

IS - 20

M1 - 5206

ER -