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

Satvik R. Hadigal, Alex M. Agelidis, Ghadah A. Karasneh, Thessicar E. Antoine, Abraam M. Yakoub, Vishnu C. Ramani, Ali R. Djalilian, Ralph D. Sanderson and Deepak Shukla ()
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Satvik R. Hadigal: Ocular Virology Laboratory, University of Illinois at Chicago
Alex M. Agelidis: Ocular Virology Laboratory, University of Illinois at Chicago
Ghadah A. Karasneh: Ocular Virology Laboratory, University of Illinois at Chicago
Thessicar E. Antoine: Ocular Virology Laboratory, University of Illinois at Chicago
Abraam M. Yakoub: Ocular Virology Laboratory, University of Illinois at Chicago
Vishnu C. Ramani: University of Alabama at Birmingham
Ali R. Djalilian: Ocular Virology Laboratory, University of Illinois at Chicago
Ralph D. Sanderson: University of Alabama at Birmingham
Deepak Shukla: Ocular Virology Laboratory, University of Illinois at Chicago

Nature Communications, 2015, vol. 6, issue 1, 1-11

Abstract: 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.

Date: 2015
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DOI: 10.1038/ncomms7985

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