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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.

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posted on 2016-01-27, 00:00 authored by A.M. Yakoub, N. Rawal, E. Maus, J. Baldwin, D. Shukla, V. Tiwari
Binding of herpes simplex virus 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 the 3-O-sulfotransferase (3-OST) enzyme. Multiple isoforms of 3-OST are differentially expressed in tissues of zebrafish (ZF) embryos. Here, we performed a comprehensive analysis of the role of ZF 3-OST isoforms (3-OST-1, 3-OST-5, 3-OST-6, and 3-OST-7) in HSV-1 entry. We found that a group of 3-OST gene family isoforms (3-OST-2, -3, -4, and -6) 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) lacks these properties. These results demonstrate that HSV-1 entry can be recapitulated by certain ZF 3-OST enzymes, a significant step toward the establishment of a ZF model of HSV-1 infection and tissue-specific tropism.


This work was supported by NIH grants to V.T. (AI088429-01A1) and D.S. (AI081869). J.B. and N.R. (10-2014-8172) were supported by Midwestern University (Downers Grove, IL)-sponsored Kenneth A. Suarez Summer Research Fellowships. We appreciate the University of Illinois (UIC) ophthalmology core facility (core grant number EY001792) for confocal imaging


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This is a copy of an article published in the Journal of Virology © 2014 American Society for Microbiology Publications.


American Society for Microbiology



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