Soluble forms of herpes simplex virus glycoprotein D bind to a limited number of cell surface receptors and inhibit virus entry into cells

Johnson, David C.; Burke, Rae Lyn; Gregory, Timothy J.

doi:10.1128/jvi.64.6.2569-2576.1990

Cited by 167 publications

(142 citation statements)

References 35 publications

Supporting

Mentioning

127

Contrasting

Unclassified

Order By: Relevance

“…4). These observations are consistent with previous reports (41,57,58) and demonstrate a very similar mode of action of HSV-1 and HSV-2 gDs in nectin-1-mediated cell-cell fusion. Nectin-1 I80 is an important gD interaction residue.…”

Section: Resultssupporting

confidence: 93%

Crystal Structure of Herpes Simplex Virus 2 gD Bound to Nectin-1 Reveals a Conserved Mode of Receptor Recognition

Zhang

et al. 2014

J Virol

View full text Add to dashboard Cite

Herpes simplex virus 1 (HSV-1) and HSV-2 are among the most prevalent human pathogens. Both viruses can recognize, via the surface envelope glycoprotein D (gD), human nectin-1 as a functional receptor. Previous studies have successfully elucidated the molecular basis of the binding between HSV-1 gD and nectin-1 by cocrystallography. Despite a high sequence identity between HSV-1 and HSV-2 gDs, the atomic intermolecule details for the HSV-2-gD/nectin-1 interaction remain elusive. Here, we report the crystal structures of both the unbound and the nectin-1-bound HSV-2 gDs. The free-gD structure expectedly comprises an IgV-like core and the surface-exposed terminal extensions as observed in its HSV-1 counterpart but lacks traceable electron densities for a large portion of the terminal elements. These terminal residues were clearly traced in the complex structure as a definitive loop in the N terminus and an ␣-helix in the C terminus, thereby showing a conserved nectin-1-binding mode as reported for HSV-1 gD. The interface residues in nectin-1 were further mutated and tested for the gD interaction by surface plasmon resonance. The resultant binding patterns were similar for HSV-1 and HSV-2 gDs, further supporting a homologous receptor-binding basis by the two viruses for nectin-1. These data, together with a cell-based fusion assay showing a cross-inhibition of the gD/nectin-1-mediated cell-cell fusion by soluble HSV-1 and HSV-2 gDs, provided solid structural and functional evidence that HSV-1 and HSV-2 recognize nectin-1 via the same binding mode. Finally, we also demonstrated that nectin-1 I80 is an important residue involved in gD interaction. IMPORTANCEDespite intensified studies, a detailed picture of the molecular features in the HSV-2-gD/nectin-1 interaction remains unavailable. Previous work focused on HSV-1 gD, which folds into an IgV-like core with large terminal extensions and utilizes the extension elements to engage nectin-1. Here, we report the crystal structures of HSV-2 gD in both the free and the nectin-1-bound forms. The atomic intermolecule details for HSV-2-gD/nectin-1 interaction are clearly presented. The observed binding mode is identical to that reported for its HSV-1 counterpart. This structural observation was further supported by our comparative functional assays showing that nectin-1 mutations similarly affect the ligand-receptor interaction of both virus gDs. Taken together, we provide comprehensive structural and functional data demonstrating a conserved receptor-binding mode between HSV-1 and HSV-2 for nectin-1. Our results also indicate that the tropism difference between the two viruses likely arises from aspects other than the gD/nectin-1 binding features.

show abstract

Section: Resultssupporting

confidence: 93%

Crystal Structure of Herpes Simplex Virus 2 gD Bound to Nectin-1 Reveals a Conserved Mode of Receptor Recognition

Zhang

et al. 2014

J Virol

View full text Add to dashboard Cite

show abstract

“…Even when their heparin-binding regions are defined with monoclonal antibodies, site-specific mutants, and oligopeptides, polypeptides and microbes may have another "specific" eukaryotic ceU-binding sites. For example, heparin-inhibitable adsorption of HSV clearly involves two viral components (gB and gC) (37,38); but productive uptake of this virus depends on interaction of yet another viral glycoprotein (gD) with a non-HS host cell receptor (52,53), Whether Gc have an additional non-Opa molecule that promotes uptake by host cells is unknown.…”

Section: Distinguish Among Hs Molecules Of Differing Size and Sulfatimentioning

confidence: 99%

Adherence of pilus- Opa+ gonococci to epithelial cells in vitro involves heparan sulfate.

Chen

Belland

Wilson

et al. 1995

The Journal of Experimental Medicine

167

148

View full text Add to dashboard Cite

SummaryNeisseria gonorrhoeae attaches to host epithelial cells via pili and opacity-associated (Opa) outer membrane proteins. Pilus-gonococci (Gc) of strain MS11 adhere to both human and nonhuman cells, but only when particular Opa proteins are expressed; OpaA + variants adhere best, OpaC § variants are next best, and the seven other Opa + variants adhere poorly or not at all. The adherence of OpaA + Gc to Chinese hamster ovary (CHO) cells is inhibited by heparin or heparan sulfate (HS), but not by chondroitin sulfate. OpaA + Gc do not adhere to CHO cells devoid of HS proteoglycans; low concentrations of heparin restore OpaA + Gc adherence to these HS-deficient CHO cells and high concentrations inhibit it. 3H-heparin binding to whole Gc parallels their adherence abilities (OpaA § > OpaC + > OpaH § >> Opas B, D, E, F, G, I = Opa-= 0). Opa proteins separated by SDS-PAGE also bind 3H-heparin. These data suggest that adherence of pilus-, Opa + Gc involves HS-proteoglycan of eukaryotic cells.

show abstract

“…Abortive cells could be made resistant to HSV entry while retaining the ability to bind a virus by transfection with plasmid expressing HSV gD (Campadelli-Fiume et al, 1988;Johnson and Spear, 1989). Soluble forms of HSV gD inhibited virus entry into cells (Johnson et al, 1990). And recently, two other cell surface proteins named poliovirus receptor-related protein 1 (PRR1)/HveB and PRR2/HveC, were found to mediate HSV entry also by interaction with gD Warner et al, 1998).…”

Section: Discussionmentioning

confidence: 99%

Growth behavior of bovine herpesvirus-1 in permissive and semi-permissive cells

et al. 1999

View full text Add to dashboard Cite

Bovine herpesvirus-1 (BHV-1) can replicate well in bovine-derived cell lines such as Madin Darby bovine kidney (MDBK) but grows poorly in hamster lung (HmLu-1). Virus replication, DNA synthesis, and immediate-early gene expression are severely restricted in HmLu-1. We compared adsorption and penetration of BHV-1 in permissive MDBK and semi-permissive HmLu-1 cells. At a low multiplicity of infection, BHV-1 attached to permissive MDBK cells twice as much as to HmLu-1. The presence of heparin inhibited the attachment of BHV-1 to MDBK cells by about 60%, but over 90% of the attachment was inhibited in HmLu-1. To investigate the penetration of BHV-1, we performed the quantitative measurement of viral DNA by quantitative competitive (QC)PCR in infected cells. In MDBK cells, virions attached to the cell surface, penetrated into the cells and were transported to the nucleus. However in HmLu-1, only a small fraction of the virions attached to the cell surface were allowed to penetrate. Our results indicated that the replication of BHV-1 in semi-permissive HmLu-1 was not dramatically restricted at one certain point but at some various stages including adsorption and penetration.

show abstract

Soluble forms of herpes simplex virus glycoprotein D bind to a limited number of cell surface receptors and inhibit virus entry into cells

Cited by 167 publications

References 35 publications

Crystal Structure of Herpes Simplex Virus 2 gD Bound to Nectin-1 Reveals a Conserved Mode of Receptor Recognition

Crystal Structure of Herpes Simplex Virus 2 gD Bound to Nectin-1 Reveals a Conserved Mode of Receptor Recognition

Adherence of pilus- Opa+ gonococci to epithelial cells in vitro involves heparan sulfate.

Growth behavior of bovine herpesvirus-1 in permissive and semi-permissive cells

Contact Info

Product

Resources

About