ArticlePLoS pathogens2022
Binding of adenovirus species C hexon to prothrombin and the influence of hexon on vector properties in vitro and in vivo.
Article in PLoS pathogens, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 11 citations in OpenAlex.
- Structural requirements of blood factors binding to soluble hexon trimers with implications for adenovirus cell targeting and immune evasion.PLoS pathogens · 2026Article
- Current use of pre-clinical models for evaluation of human adenovirus-based cancer therapeutics.Molecular therapy. Oncology · 2026Review
- Immune shielding of viral vectors via capsid engineering with genetically encoded zwitterionic peptides.Molecular therapy. Advances · 2026Article
- Novel adenovirus vaccine vectors lacking thrombosis-associated interactions with platelet factor 4.iScience · 2026Article
- ADEVO: Proof-of-concept of adenovirus-directed EVOlution by random peptide display on the fiber knob.Molecular therapy. Oncology · 2024Article
- An oncolytic HAdV-5 with reduced surface charge combines diminished toxicity and improved tumor targeting.Molecular therapy. Oncology · 2024Article
- Structure-derived insights from blood factors binding to the surfaces of different adenoviruses.Nature communications · 2024Article
- HDAd6/35++ - A new helper-dependent adenovirus vector platform forMolecular therapy. Methods & clinical development · 2023Article
- Review
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The majority of adenovirus (Ad) vectors are based on human Ad type 5, which is a member of Ad species C. Species C also includes the closely-related types 1, 2, 6, 57 and 89. It is known that coagulation factors bind to Ad5 hexon and play a key role in the liver tropism of Ad5 vectors, but it is unclear how coagulation factors affect vectors derived from other species C Ads. We evaluated species C Ad vectors both in vitro and following intravenous injection in mice. To assess the impact of hexon differences, we constructed chimeric Ad5 vectors that contain the hexon hypervariable regions from other species C types, including vectors with hexon mutations that decreased coagulation factor binding. After intravenous injection into mice, vectors with Ad5 or Ad6 hexon had strong liver tropism, while vectors with chimeric hexon from other Ad types had weaker liver tropism due to inhibition by natural antibodies and complement. In addition, we discovered a novel ability of hexon to bind prothrombin, which is the most abundant coagulation factor in blood, and we found striking differences in the affinity of Ads for human, mouse and bovine coagulation factors. When compared to Ad5, vectors with non-Ad5 species C hexons had considerably higher affinity for both human and mouse prothrombin. Most of the vectors tested were strongly dependent on coagulation factors for liver transduction, but vectors with chimeric Ad6 hexon showed much less dependence on coagulation factors than other vectors. We found that in vitro neutralization experiments with mouse serum predicted in vivo behavior of Ad5 vectors, but in vitro experiments did not predict the in vivo behavior of vectors based on other Ad types. In sum, hexons from different human Ad species C viruses confer diverse properties on vectors, including differing abilities to target the liver.
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