The multipartite system that mediates entry of herpes simplex virus into the cell

@article{CampadelliFiume2007TheMS,
  title={The multipartite system that mediates entry of herpes simplex virus into the cell},
  author={G. Campadelli-Fiume and M. Amasio and E. Avitabile and Arianna Cerretani and Cristina Forghieri and T. Gianni and L. Menotti},
  journal={Reviews in Medical Virology},
  year={2007},
  volume={17}
}
The multipartite entry‐fusion system of herpes simplex virus is made of a quartet of glycoproteins—gD, gB, gH·gL—and three alternative gD receptors, herpesvirus entry mediator (HVEM), nectin1 and modified sites on heparan sulphate. This multipartite system recapitulates the basic steps of virus—cell fusion, i.e. receptor recognition, triggering of fusion and fusion execution. Specifically, in addition to serving as the receptor‐binding glycoprotein, gD triggers fusion through a specialised… Expand
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References

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Potential Nectin-1 Binding Site on Herpes Simplex Virus Glycoprotein D
TLDR
The results suggest that this region of gD is important for nectin-1 interaction and is distinct from but partially overlaps the site of HVEM binding. Expand
Structure of unliganded HSV gD reveals a mechanism for receptor‐mediated activation of virus entry
TLDR
It is proposed that a controlled displacement of the gD C‐terminus upon receptor binding is an essential feature of HSV entry, ensuring the timely activation of membrane fusion. Expand
The pro-fusion domain of herpes simplex virus glycoprotein D (gD) interacts with the gD N terminus and is displaced by soluble forms of viral receptors.
TLDR
This work proposes that gD adopts a "closed" conformation before receptor binding, gD modifies its conformation and the N and C termini are released from reciprocal interactions and enabled to trigger fusion, and shows that PFD bound soluble forms of gD, truncated at residue 260 (gD260t) or downstream. Expand
The soluble ectodomain of herpes simplex virus gD contains a membrane-proximal pro-fusion domain and suffices to mediate virus entry.
TLDR
It is reported that the gD ectodomain in soluble form was sufficient to rescue the infectivity of a gD-null HSV mutant, indicating that gD does not need to be anchored to the virion envelope to mediate entry. Expand
Different receptors binding to distinct interfaces on herpes simplex virus gD can trigger events leading to cell fusion and viral entry.
TLDR
This review summarizes recent findings on the structure and function of gD and indicates that gD may assume more than one conformation, one in the absence of receptor, another when gD is bound to the herpesvirus entry mediator, a member of the TNF receptor family, and a third when gB, gH and gL are bound to nectin-1. Expand
The novel receptors that mediate the entry of herpes simplex viruses and animal alphaherpesviruses into cells
TLDR
The first example of a mediator of HSV entry independent of a detectable interaction with gD is provided, and the human nectin1α‐δ is the promiscuous species non‐specific receptor activity towards the animal alphaherpesviruses, pseudorabies virus and bovine herpesvirus 1 (BHV‐1). Expand
Separation of receptor-binding and profusogenic domains of glycoprotein D of herpes simplex virus 1 into distinct interacting proteins
TLDR
Results indicate that codons 61-residue glycoprotein D do not encode executable functions required for viral entry into cells and suggest that the receptor-binding ligand must interact with but need not alter the structure of the residual portion of gD to effect virus entry. Expand
Entry of alphaherpesviruses into the cell
Herpes simplex virus (HSV) represents the most comprehensive example of virus-receptor interaction in the Herpesviridae family, and the prototype virus encoding multipartite entry genes. WhereasExpand
Structure-Based Mutagenesis of Herpes Simplex Virus Glycoprotein D Defines Three Critical Regions at the gD-HveA/HVEM Binding Interface
TLDR
Of the 35 gD and HveA contact residues that comprise the gD-HveA interface, only a handful are critical for complex formation, and this study shows that one gD residue that contacts CRD2 contributes to Hve a binding. Expand
Use of herpes simplex virus and pseudorabies virus chimeric glycoprotein D molecules to identify regions critical for membrane fusion.
TLDR
It is shown here that PRV gD, when coexpressed with HSV gB, gH, and gL, cannot substitute for HSVs gD in inducing fusion with target cells expressing nectin-1, and that chimeric gD molecules composed of HSV and PRV sequences can substitute, provided the first 285 aa are from HSv gD. Expand
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