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Nat Commun. 2015 Apr 27;6:6985. doi: 10.1038/ncomms7985.

Heparanase is a host enzyme required for herpes simplex virus-1 release from cells.

Author information

1
Ocular Virology Laboratory, Department of Ophthalmology and Visual Sciences, University of Illinois at Chicago, 1855 West Taylor Street, M/C 648, Chicago, Illinois 60612, USA.
2
1] Ocular Virology Laboratory, Department of Ophthalmology and Visual Sciences, University of Illinois at Chicago, 1855 West Taylor Street, M/C 648, Chicago, Illinois 60612, USA [2] Department of Microbiology and Immunology, College of Medicine, University of Illinois at Chicago, E-704 Medical Sciences Building, M/C 790, 835 South Wolcott Avenue, Chicago, Illinois 60612, USA.
3
Department of Pathology, University of Alabama at Birmingham, 1720 2nd Avenue South, Birmingham, Alabama 35294, USA.

Abstract

Herpesviruses exemplified by herpes simplex virus-1 (HSV-1) attach to cell surface heparan sulfate (HS) for entry into host cells. However, during a productive infection, the HS moieties on parent cells can trap newly exiting viral progenies and inhibit their release. Here we demonstrate that a HS-degrading enzyme of the host, heparanase (HPSE), is upregulated through NF-kB and translocated to the cell surface upon HSV-1 infection for the removal of HS to facilitate viral release. We also find a significant increase in HPSE release in vivo during infection of murine corneas and that knockdown of HPSE in vivo inhibits virus shedding. Overall, we propose that HPSE acts as a molecular switch for turning a virus-permissive 'attachment mode' of host cells to a virus-deterring 'detachment mode'. Since many human viruses use HS as an attachment receptor, the HPSE-HS interplay may delineate a common mechanism for virus release.

PMID:
25912399
PMCID:
PMC4413471
DOI:
10.1038/ncomms7985
[Indexed for MEDLINE]
Free PMC Article

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