ArticleThe Journal of experimental medicine2021
HVEM structures and mutants reveal distinct functions of binding to LIGHT and BTLA/CD160.
Article in The Journal of experimental medicine, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
20 citing papers in PubMed, 28 citations in OpenAlex.
- Complete disruption of gD binding to HVEM alters virus replication and host receptor homeostasis.PLoS pathogens · 2026Article
- Article
- The BTLA/HVEM axis as a key regulator for stratified functional cure in chronic hepatitis B.Frontiers in immunology · 2026Review
- Evaluation of LIGHT-derived peptides to disrupt the HVEM/LIGHT immune checkpoint.Scientific reports · 2025Article
- TNFSF14 (LIGHT) in intestinal inflammation: balancing immune activation and resolution in IBD.Frontiers in immunology · 2025Review
- Internal regulation between constitutively expressed T cell co-inhibitory receptors BTLA and CD5 and tolerance in recent thymic emigrants.Open biology · 2024Article
- Therapeutic targets of armored chimeric antigen receptor T cells navigating the tumor microenvironment.Experimental hematology & oncology · 2024Review
- Proteomic Investigation of Immune Checkpoints and Some of Their Inhibitors.International journal of molecular sciences · 2024Review
- Article
- Multilayered Computational Framework for Designing Peptide Inhibitors of HVEM-LIGHT Interaction.The journal of physical chemistry. B · 2024Article
- The role of the BTLA-HVEM complex in the pathogenesis of breast cancer.Breast cancer (Tokyo, Japan) · 2024Review
- Investigation of LGALS2 expression in the TCGA database reveals its clinical relevance in breast cancer immunotherapy and drug resistance.Scientific reports · 2023Article
- Review
- T cell co-stimulatory and co-inhibitory pathways in atopic dermatitis.Frontiers in immunology · 2023Review
- Causal effects and immune cell mediators between prescription analgesic use and risk of infectious diseases: a Mendelian randomization study.Frontiers in immunology · 2023Article
- Immune activation of the p75 neurotrophin receptor: implications in neuroinflammation.Frontiers in molecular neuroscience · 2023Article
- Expression of HPV-16 E6 and E7 oncoproteins altersFrontiers in cellular and infection microbiology · 2023Article
- Epithelial HVEM maintains intraepithelial T cell survival and contributes to host protection.Science immunology · 2022Article
- Realigning the LIGHT signaling network to control dysregulated inflammation.The Journal of experimental medicine · 2022Article
- The Neonatal Innate Immune Response to Sepsis: Checkpoint Proteins as Novel Mediators of This Response and as Possible Therapeutic/Diagnostic Levers.Frontiers in immunology · 2022Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
14 authors at 3 institutions in 2 countries.
Funding
Abstract
HVEM is a TNF (tumor necrosis factor) receptor contributing to a broad range of immune functions involving diverse cell types. It interacts with a TNF ligand, LIGHT, and immunoglobulin (Ig) superfamily members BTLA and CD160. Assessing the functional impact of HVEM binding to specific ligands in different settings has been complicated by the multiple interactions of HVEM and HVEM binding partners. To dissect the molecular basis for multiple functions, we determined crystal structures that reveal the distinct HVEM surfaces that engage LIGHT or BTLA/CD160, including the human HVEM-LIGHT-CD160 ternary complex, with HVEM interacting simultaneously with both binding partners. Based on these structures, we generated mouse HVEM mutants that selectively recognized either the TNF or Ig ligands in vitro. Knockin mice expressing these muteins maintain expression of all the proteins in the HVEM network, yet they demonstrate selective functions for LIGHT in the clearance of bacteria in the intestine and for the Ig ligands in the amelioration of liver inflammation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.