ArticleJournal of virology2013
Coagulation factor binding orientation and dimerization may influence infectivity of adenovirus-coagulation factor complexes.
Article in Journal of virology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 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.
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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.
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Who cites it
21 citing papers in PubMed, 31 citations in OpenAlex.
- Cryogenic electron microscopy and coagulation factors.Current opinion in hematology · 2026Review
- Molecular mechanism of cleavage at R271 during prothrombin activation revealed by cryo-EM.Blood · 2026Article
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- Structure-derived insights from blood factors binding to the surfaces of different adenoviruses.Nature communications · 2024Article
- The Prothrombin-Prothrombinase Interaction.Sub-cellular biochemistry · 2024Review
- Cryo-EM structure of coagulation factor V short.Blood · 2023Article
- Binding of adenovirus species C hexon to prothrombin and the influence of hexon on vector properties in vitro and in vivo.PLoS pathogens · 2022Article
- To clot or not to clot? Ad is the question-Insights on mechanisms related to vaccine-induced thrombotic thrombocytopenia.Journal of thrombosis and haemostasis : JTH · 2021Article
- The Inflammatory and Fibrotic Patterns of Hepatic Stellate Cells Following Coagulation Factors (VII or X)-Shielded Adenovirus Infection.Current microbiology · 2021Article
- Chorioallantoic Membrane Tumor Model for Evaluating Oncolytic Viruses.Human gene therapy · 2020Article
- The superior role of coagulation factor FX over FVII in adenoviral-mediated innate immune induction of the hepatocyte: anClinical and experimental hepatology · 2020Article
- Innate immunity to adenovirus: lessons from mice.FEBS letters · 2019Review
- Adenovirus flow in host cell networks.Open biology · 2019Review
- Gene Therapy Leaves a Vicious Cycle.Frontiers in oncology · 2019Review
- Hexons from adenovirus serotypes 5 and 48 differentially protect adenovirus vectors from neutralization by mouse and human serum.PloS one · 2018Article
- Defining a Novel Role for the Coxsackievirus and Adenovirus Receptor in Human Adenovirus Serotype 5 TransductionJournal of virology · 2017Article
- Recent advances in genetic modification of adenovirus vectors for cancer treatment.Cancer science · 2017Review
- Oncolytic Adenovirus: Strategies and Insights for Vector Design and Immuno-Oncolytic Applications.Viruses · 2015Review
- Manipulating adenovirus hexon hypervariable loops dictates immune neutralisation and coagulation factor X-dependent cell interaction in vitro and in vivo.PLoS pathogens · 2015Article
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
Abstract
Adenoviruses (Ads) are promising vectors for therapeutic interventions in humans. When injected into the bloodstream, Ad vectors can bind several vitamin K-dependent blood coagulation factors, which contributes to virus sequestration in the liver by facilitating transduction of hepatocytes. Although both coagulation factors FVII and FX bind the hexon protein of human Ad serotype 5 (HAdv5) with a very high affinity, only FX appears to play a role in mediating Ad-hepatocyte transduction in vivo. To understand the discrepancy between efficacy of FVII binding to hexon and its apparently poor capacity for supporting virus cell entry, we analyzed the HAdv5-FVII complex by using high-resolution cryo-electron microscopy (cryo-EM) followed by molecular dynamic flexible fitting (MDFF) simulations. The results indicate that although hexon amino acids T423, E424, and T425, identified earlier as critical for FX binding, are also involved in mediating binding of FVII, the FVII GLA domain sits within the surface-exposed hexon trimer depression in a different orientation from that found for FX. Furthermore, we found that when bound to hexon, two proximal FVII molecules interact via their serine protease (SP) domains and bury potential heparan sulfate proteoglycan (HSPG) receptor binding residues within the dimer interface. In contrast, earlier cryo-EM studies of the Ad-FX interaction showed no evidence of dimer formation. Dimerization of FVII bound to Ad may be a contributing mechanistic factor for the differential infectivity of Ad-FX and Ad-FVII complexes, despite high-affinity binding of both these coagulation factors to the virus.
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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.