gD x TNFRSF14

Last update 08 May 2025

Basic Info

Related Targets

gDTNFRSF14

100 Clinical Results associated with gD x TNFRSF14

100 Translational Medicine associated with gD x TNFRSF14

0 Patents (Medical) associated with gD x TNFRSF14

Literatures (Medical) associated with gD x TNFRSF14

01 Nov 2023·Microbial biotechnology

A critical review on antiviral peptides derived from viral glycoproteins and host receptors to decoy herpes simplex virus.

Review

Author: Rahangdale, Rakesh ; Balireddy, Sridevi ; Pasupuleti, Mukesh ; Hariharapura, Raghu Chandrashekar ; Goswami, Kamini ; Tender, Tenzin

The health of the human population has been continuously challenged by viral infections. Herpes simplex virus (HSV) is one of the common causes of illness and can lead to death in immunocompromised patients. Existing anti-HSV therapies are not completely successful in eliminating the infection due to anti-viral drug resistance, ineffectiveness against the latent virus and high toxicity over prolonged use. There is a need to update our knowledge of the current challenges faced in anti-HSV therapeutics and realize the necessity of developing alternative treatment approaches. Protein therapeutics are now being explored as a novel approach due to their high specificity and low toxicity. This review highlights the significance of HSV viral glycoproteins and host receptors in the pathogenesis of HSV infection. Proteins or peptides derived from HSV glycoproteins gC, gB, gD, gH and host cell receptors (HSPG, nectin and HVEM) that act as decoys to inhibit HSV attachment, entry, or fusion have been discussed. Few researchers have tried to improve the efficacy and stability of the identified peptides by modifying them using a peptidomimetic approach. With these efforts, we think developing an alternative treatment option for immunocompromised patients and drug-resistant organisms is not far off.

01 Sep 2023·PLoS pathogens

Binding of herpesvirus entry mediator (HVEM) and HSV-1 gD affect reactivation but not latency levels.

Article

Author: Wang, Shaohui ; Mott, Kevin R ; Ghiasi, Homayon ; Jaggi, Ujjaldeep

Previously we reported that the HSV-1 latency associated transcript (LAT) specifically upregulates the cellular herpesvirus entry mediator (HVEM) but no other known HSV-1 receptors. HSV-1 glycoprotein D (gD) binds to HVEM but the effect of this interaction on latency-reactivation is not known. We found that the levels of latent viral genomes were not affected by the absence of gD binding to HVEM. However, reactivation of latent virus in trigeminal ganglia explant cultures was blocked in the absence of gD binding to HVEM. Neither differential HSV-1 replication and spread in the eye nor levels of latency influenced reactivation. Despite similar levels of latency, reactivation in the absence of gD binding to HVEM correlated with reduced T cell exhaustion. Our results indicate that HVEM-gD signaling plays a significant role in HSV-1 reactivation but not in ocular virus replication or levels of latency. The results presented here identify gD binding to HVEM as an important target that influences reactivation and survival of ganglion resident T cells but not levels of latency. This concept may also apply to other herpesviruses that engages HVEM.

11 Apr 2023·International journal of molecular sciences

HSV-1 Glycoprotein D and Its Surface Receptors: Evaluation of Protein-Protein Interaction and Targeting by Triazole-Based Compounds through In Silico Approaches.

Article

Author: Barreca, Marilia ; Barraja, Paola ; Alcaro, Stefano ; Montalbano, Alessandra ; Romeo, Isabella ; Bivacqua, Roberta

Protein-protein interactions (PPI) represent attractive targets for drug design.Thus, aiming at a deeper insight into the HSV-1 envelope glycoprotein D (gD), protein-protein docking and dynamic simulations of gD-HVEM and gD-Nectin-1 complexes were performed.The most stable complexes and the pivotal key residues useful for gD to anchor human receptors were identified and used as starting points for a structure-based virtual screening on a library of both synthetic and designed 1,2,3-triazole-based compoundsTheir binding properties vs. gD interface with HVEM and Nectin-1 along with their structure-activity relationships (SARs) were evaluated.Four [1,2,3]triazolo[4,5-b]pyridines were identified as potential HSV-1 gD inhibitors, for their good theor. affinity towards all conformations of HSV-1 gD.Overall, this study suggests promising basis for the design of new antiviral agents targeting gD as a valuable strategy to prevent viral attachment and penetration into the host cell.

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