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In vivo importance of heparan sulfate-binding glycoproteins for murid herpesvirus-4 infection

Laurent Gillet

Division of Virology, Department of Pathology, University of Cambridge, UK

Correspondence
Philip G. Stevenson
pgs27{at}cam.ac.uk

Many herpesviruses bind to heparan sulfate (HS). Murid herpesvirus-4 (MuHV-4) does so via its envelope glycoproteins gp70 and gH/gL. MuHV-4 gp150 further regulates an HS-independent interaction to make that HS-dependent too. Cell binding by MuHV-4 virions is consequently strongly HS-dependent. Gp70 and gH/gL show some in vitro redundancy: an antibody-mediated blockade of HS binding by one is well tolerated, whereas a blockade of both severely impairs infection. In order to understand the importance of HS binding for MuHV-4 in vivo, we generated mutants lacking both gL and gp70. As expected, gL^–gp70^– MuHV-4 showed very poor cell binding. It infected mice at high dose but not at low dose, indicating defective host entry. But once entry occurred, host colonization, which for MuHV-4 is relatively independent of the infection dose, was remarkably normal. The gL^–gp70^– entry deficit was much greater than that of gL^– or gp70^– single knockouts. And gp150 disruption, which allows HS-independent cell binding, largely rescued the gL^–gp70^– cell binding and host entry deficits. Thus, it appeared that MuHV-4 HS binding is important in vivo, principally for efficient host entry.

Present address: Immunology-Vaccinology, Faculty of Veterinary Medicine, University of Liège, Liège, Belgium

This article has been cited by other articles:

				P. G. Stevenson, J. P. Simas, and S. Efstathiou Immune control of mammalian gamma-herpesviruses: lessons from murid herpesvirus-4 J. Gen. Virol., October 1, 2009; 90(10): 2317 - 2330. [Abstract] [Full Text] [PDF]