Well Put Together—A Guide to Accessorizing with the Herpesvirus gH/gL Complexes
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TLDR
It is proposed that the intrinsic structural plasticity of gH/gL enables it to function as a signal integration machine that can accept diverse regulatory inputs and convert them into a “trigger” signal that activates the fusogenic ability of gB.Abstract:
Herpesviruses are enveloped, double-stranded DNA viruses that infect a variety of hosts across the animal kingdom. Nine of these establish lifelong infections in humans, for which there are no cures and few vaccine or treatment options. Like all enveloped viruses, herpesviruses enter cells by fusing their lipid envelopes with a host cell membrane. Uniquely, herpesviruses distribute the functions of receptor engagement and membrane fusion across a diverse cast of glycoproteins. Two glycoprotein complexes are conserved throughout the three herpesvirus subfamilies: the trimeric gB that functions as a membrane fusogen and the heterodimeric gH/gL, the role of which is less clearly defined. Here, we highlight the conserved and divergent functions of gH/gL across the three subfamilies of human herpesviruses by comparing its interactions with a broad range of accessory viral proteins, host cell receptors, and neutralizing or inhibitory antibodies. We propose that the intrinsic structural plasticity of gH/gL enables it to function as a signal integration machine that can accept diverse regulatory inputs and convert them into a “trigger” signal that activates the fusogenic ability of gB.read more
Citations
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Journal ArticleDOI
A surface pocket in the cytoplasmic domain of the herpes simplex virus fusogen gB controls membrane fusion
TL;DR: In this paper , the authors identified two new regulatory elements within gB and gH from the prototypical herpes simplex virus 1: a surface pocket within the intraviral domain (gBCTD) and residue V831 within the gH cytoplasmic tail.
Journal ArticleDOI
Herpes Simplex Virus 1 Entry Glycoproteins Form Complexes before and during Membrane Fusion
TL;DR: Using a quantitative split-luciferase approach, it is found that pairwise HSV-1 glycoproteins form receptor-independent complexes and interact at a steady level, and do not depend on the presence of the cellular receptor.
Posted ContentDOI
A surface pocket in the cytoplasmic domain of the herpes simplex virus fusogen gB controls membrane fusion
TL;DR: In this paper , a surface pocket within the intraviral domain (gB CTD) and residue V831 within the gH cytoplasmic tail were identified as regulatory elements for HSV-1 membrane fusion.
Posted ContentDOI
Multiple sites on glycoprotein H (gH) functionally interact with the gB fusion protein to promote fusion during herpes simplex virus (HSV) entry
TL;DR: In this paper , the authors examined the functional interaction between gH/gL-gB interaction using HSV-1 mutants that displayed reduced virus entry due to changes in gH.
Journal ArticleDOI
Multiple Sites on Glycoprotein H (gH) Functionally Interact with the gB Fusion Protein to Promote Fusion during Herpes Simplex Virus (HSV) Entry
TL;DR: In this article , the authors examined the functional interaction between gH/gL-gB interaction using HSV-1 mutants that displayed reduced virus entry due to changes in gH.
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