Reference : In vivo importance of heparan sulfate-binding glycoproteins for murid herpesvirus-4 i...
Scientific journals : Article
Life sciences : Microbiology
In vivo importance of heparan sulfate-binding glycoproteins for murid herpesvirus-4 infection.
Gillet, Laurent mailto [Université de Liège - ULiège > > Immunologie et vaccinologie >]
May, Janet S [> > > >]
Stevenson, Philip G [> > > >]
Journal of General Virology
Society for General Microbiology
Pt 3
Yes (verified by ORBi)
United Kingdom
[en] Animals ; Cell Line ; Cricetinae ; Female ; Glycoproteins/genetics/metabolism ; Heparitin Sulfate/metabolism ; Kidney/cytology/virology ; Mice ; NIH 3T3 Cells ; Protein Binding ; Receptors, Virus/metabolism ; Rhadinovirus/genetics/metabolism/pathogenicity ; Viral Envelope Proteins/genetics/metabolism
[en] 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.

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