7RD1
The Capsid Structure of the ChAdOx1 viral vector/chimpanzee adenovirus Y25
This is a non-PDB format compatible entry.
Summary for 7RD1
| Entry DOI | 10.2210/pdb7rd1/pdb |
| EMDB information | 24408 |
| Descriptor | Pre-protein VI, Hexon protein, Penton protein, ... (6 entities in total) |
| Functional Keywords | adenovirus, simian adenovirus, chimpanzee adenovirus, vaccine vector, dna virus, adv, chadv-y25, adenovirus y25, y25, viral vector, chadox1, chimp ad, dsdna virus, icosahedral, chimpanzee adenovirus y25, y-25, y 25, chadv, virus |
| Biological source | Chimpanzee adenovirus Y25 More |
| Total number of polymer chains | 32 |
| Total formula weight | 1821969.96 |
| Authors | Baker, A.T.,Boyd, R.J.,Sarkar, D.,Vermaas, J.V.,Williams, D.,Singharoy, A. (deposition date: 2021-07-08, release date: 2021-12-15, Last modification date: 2024-06-05) |
| Primary citation | Baker, A.T.,Boyd, R.J.,Sarkar, D.,Teijeira-Crespo, A.,Chan, C.K.,Bates, E.,Waraich, K.,Vant, J.,Wilson, E.,Truong, C.D.,Lipka-Lloyd, M.,Fromme, P.,Vermaas, J.,Williams, D.,Machiesky, L.,Heurich, M.,Nagalo, B.M.,Coughlan, L.,Umlauf, S.,Chiu, P.L.,Rizkallah, P.J.,Cohen, T.S.,Parker, A.L.,Singharoy, A.,Borad, M.J. ChAdOx1 interacts with CAR and PF4 with implications for thrombosis with thrombocytopenia syndrome. Sci Adv, 7:eabl8213-eabl8213, 2021 Cited by PubMed Abstract: Vaccines derived from chimpanzee adenovirus Y25 (ChAdOx1), human adenovirus type 26 (HAdV-D26), and human adenovirus type 5 (HAdV-C5) are critical in combatting the severe acute respiratory coronavirus 2 (SARS-CoV-2) pandemic. As part of the largest vaccination campaign in history, ultrarare side effects not seen in phase 3 trials, including thrombosis with thrombocytopenia syndrome (TTS), a rare condition resembling heparin-induced thrombocytopenia (HIT), have been observed. This study demonstrates that all three adenoviruses deployed as vaccination vectors versus SARS-CoV-2 bind to platelet factor 4 (PF4), a protein implicated in the pathogenesis of HIT. We have determined the structure of the ChAdOx1 viral vector and used it in state-of-the-art computational simulations to demonstrate an electrostatic interaction mechanism with PF4, which was confirmed experimentally by surface plasmon resonance. These data confirm that PF4 is capable of forming stable complexes with clinically relevant adenoviruses, an important step in unraveling the mechanisms underlying TTS. PubMed: 34851659DOI: 10.1126/sciadv.abl8213 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.07 Å) |
Structure validation
Download full validation report
