ArticlePLoS pathogens2025
Eph receptor tyrosine kinases are functional entry receptors for murine gammaherpesvirus 68.
Article in PLoS pathogens, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
1 citing paper in PubMed.
Corrections and comments
- Update of
Authors and funding
3 authors.
Funding
Abstract
Interactions between viral glycoproteins and cellular receptors determine virus tropism and represent promising targets for vaccines. Eph receptor tyrosine kinases are conserved receptors for the human oncogenic gammaherpesviruses, Kaposi sarcoma herpesvirus (KSHV) and Epstein-Barr virus (EBV), and mediate entry into target cells by interaction with the viral gH/gL glycoprotein complex. To evaluate the use of murine gammaherpesvirus 68 (MHV68), a natural pathogen of rodents, as an in vivo model system for early events in gammaherpesvirus infection, we characterized the interaction of the MHV68 gH/gL complex with Eph receptors. We demonstrate a direct interaction of MHV68 gH/gL with EphA4 and EphB3, that is conserved between human and murine receptors. Pre-incubation of MHV68 inocula with soluble decoy receptors decreased infection of permissive fibroblasts. Ectopic expression of EphA4 and EphB3 enabled MHV68 to infect otherwise non-permissive human B cells, demonstrating EphA4 and EphB3 receptor function. Targeted mutations informed by protein structure predictions demonstrate that the MHV68 gH/gL-Eph interaction is determined by domain I (D-I) and follows structural motifs previously described in the KSHV gH/gL-EphA2 complex. The importance of gH D-I is further highlighted by the analysis of gH-targeting neutralizing antibodies. Antibody adsorption via the full gH ectodomain or gH D-I led to comparable reductions in neutralization capacity of serum from WT infected mice, indicating the Eph-binding domain is a major target for gH/gL-directed neutralizing antibodies. Our study characterizes Eph receptors as novel interaction partners and entry receptors for MHV68. Conservation of entry mechanisms provides the basis for future in vivo analyses of the contribution of Eph receptors to cell-type dependent MHV68 infection, as well as targeted strategies to prevent transmission and diseases associated with chronic infection.
Indexed as
Identifiers
What Socratic holds
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 Socratic graph.