PUBLICATION

Comprehensive Analysis of Herpes Simplex Virus 1 (HSV-1) Entry Mediated by Zebrafish 3-O-Sulfotransferase Isoforms: Implications for the Development of a Zebrafish Model of HSV-1 Infection

Authors
Yakoub, A., Rawal, N., Maus, E., Baldwin, J., Shukla, D., Tiwari, V.
ID
ZDB-PUB-140822-5
Date
2014
Source
Journal of virology   88(21): 12915-22 (Journal)
Registered Authors
Tiwari, Vaibhav
Keywords
none
MeSH Terms
  • Animals
  • Heparitin Sulfate/metabolism*
  • Herpesvirus 1, Human/physiology*
  • Protein Isoforms/metabolism
  • Receptors, Virus/metabolism*
  • Sulfotransferases/metabolism*
  • Virus Internalization*
  • Zebrafish/virology*
PubMed
25142596 Full text @ J. Virol.
Abstract
Binding of herpes simplex virus type-1 (HSV-1) envelope glycoprotein D (gD) to the receptor 3-O-sulfated heparan sulfate (3-OS HS) mediates viral entry. 3-O-sulfation of HS is catalyzed by 3-O-sulfotransferase (3-OST) enzyme. Multiple isoforms of 3-OST are differentially expressed in tissues in Zebrafish (ZF) embryos. Here, we performed a comprehensive analysis of the role of ZF 3-OST isoforms-1, -5, -6 and -7 in HSV-1 entry. We found that a group of 3-OST gene family (3-OST-2, -3, -4, and -6 isoforms) with conserved catalytic and substrate-binding residues of the enzyme mediates HSV-1 entry and spread, while the other group (3-OST-1, -5, and -7) lack these properties. These results demonstrate that HSV-1 entry can be recapitulated by certain ZF 3-OST enzymes, a significant step towards the establishment of a ZF model of HSV-1 infection and tissue-specific tropism.
Genes / Markers
Figures
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Antibodies
Orthology
Engineered Foreign Genes
Mapping