ArticleNature communications2024
Structure-derived insights from blood factors binding to the surfaces of different adenoviruses.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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Who cites it
5 citing papers in PubMed.
- Structural requirements of blood factors binding to soluble hexon trimers with implications for adenovirus cell targeting and immune evasion.PLoS pathogens · 2026Article
- Therapeutic targeting of blood-derived protein infiltration to modulate neuroinflammation in cerebellar ataxia.Journal of neuroinflammation · 2026Article
- Immune shielding of viral vectors via capsid engineering with genetically encoded zwitterionic peptides.Molecular therapy. Advances · 2026Article
- Developing the next-generation of adenoviral vector vaccines.Human vaccines & immunotherapeutics · 2025Review
- Red Blood Cell-Associated Features of Adenoviral Vector-Linked Venous Thrombosis.International journal of molecular sciences · 2025Article
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
The tropism of adenoviruses (Ads) is significantly influenced by the binding of various blood factors. To investigate differences in their binding, we conducted cryo-EM analysis on complexes of several human adenoviruses with human platelet factor-4 (PF4), coagulation factors FII (Prothrombin), and FX. While we observed EM densities for FII and FX bound to all the species-C adenoviruses examined, no densities were seen for PF4, even though PF4 can co-pellet with various Ads. Similar to FX, the γ-carboxyglutamic acid (Gla) domain of FII binds within the surface cavity of hexon trimers. While FII binds equally to species-C Ads: Ad5, Ad6, and Ad657, FX exhibits significantly better binding to Ad5 and Ad657 compared to Ad6. Although only the FX-Gla domain is observed at high-resolution (3.7 Å), the entire FX is visible at low-resolution bound to Ad5 in three equivalent binding modes consistent with the 3-fold symmetric hexon. Only the Gla and kringle-1 domains of FII are visible on all the species-C adenoviruses, where the rigid FII binds in an upright fashion, in contrast to the flexible and bent FX. These data suggest that differential binding of FII and FX may shield certain species-C adenoviruses differently against immune molecules, thereby modulating their tropism.
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