Summary for 9R78
| Entry DOI | 10.2210/pdb9r78/pdb |
| EMDB information | 53655 53736 |
| Descriptor | Pre-protein VI, Hexon protein, Penton protein, ... (6 entities in total) |
| Functional Keywords | virus, adenovirus, capsid, conjunctivitis |
| Biological source | Human adenovirus D10 More |
| Total number of polymer chains | 28 |
| Total formula weight | 1704806.69 |
| Authors | Waraich, K.,Mundy, R.M.,Bates, E.A.,da Fonseca, P.,Morris, E.,Rizkallah, P.J.,Baker, A.T.,Young, M.T.,Parker, A.L.,Bhella, D. (deposition date: 2025-05-14, release date: 2025-12-17, Last modification date: 2026-05-13) |
| Primary citation | Mundy, R.M.,Waraich, K.,Bates, E.A.,Rizkallah, P.J.,Baker, A.T.,Young, M.T.,Morris, E.,da Fonseca, P.C.A.,Bliss, C.M.,Matthews, D.,Bhella, D.,Parker, A.L. Identification of a novel fiber shaft structural motif and overexpression of key transcripts elucidated in human adenovirus D 10. Plos Pathog., 22:e1014182-e1014182, 2026 Cited by PubMed Abstract: Adenoviruses are widely used as vectors for subunit vaccines and oncolytic therapies. Efficient vectors must infect target cells and deliver therapeutic transgenes at high levels. Species D adenoviruses, such as human adenovirus type 10 (HAdV-D10), are promising candidates due to low seroprevalence in humans. Here, we present the cryo-electron microscopy structure of the HAdV-D10 capsid alongside transcriptomic profiling of infected cells to inform vector development. The fiber shaft, essential for cell entry, was resolved at 10 Å, revealing a previously uncharacterized 'umbrella' motif. Viral transcript analysis using an ORF-centric pipeline uncovered key differences from HAdV-C5, including abundant expression of a transcript encoding a protein equivalent to mature protein VII. These findings highlight the importance of detailed vector characterization prior to clinical translation and support the advancement of HAdV-D10 as a next-generation platform for gene delivery and vaccine development. PubMed: 42048387DOI: 10.1371/journal.ppat.1014182 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.3 Å) |
Structure validation
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