6FJO
Adenovirus species 26 knob protein, very high resolution
Summary for 6FJO
| Entry DOI | 10.2210/pdb6fjo/pdb |
| Related | 6FJN 6FJP 6FJQ 6HCN |
| Descriptor | Fiber, GLUTAMIC ACID, SULFATE ION, ... (5 entities in total) |
| Functional Keywords | fiber, fiber-knob, tropism determinant, high resolution, structure determination. adenovirus, mastadenovirus, viral protein |
| Biological source | Human adenovirus 26 |
| Total number of polymer chains | 1 |
| Total formula weight | 20983.48 |
| Authors | Rizkallah, P.J.,Parker, A.L.,Baker, A.T. (deposition date: 2018-01-22, release date: 2019-02-06, Last modification date: 2024-01-17) |
| Primary citation | Baker, A.T.,Mundy, R.M.,Davies, J.A.,Rizkallah, P.J.,Parker, A.L. Human adenovirus type 26 uses sialic acid-bearing glycans as a primary cell entry receptor. Sci Adv, 5:eaax3567-eaax3567, 2019 Cited by PubMed Abstract: Adenoviruses are clinically important agents. They cause respiratory distress, gastroenteritis, and epidemic keratoconjunctivitis. As non-enveloped, double-stranded DNA viruses, they are easily manipulated, making them popular vectors for therapeutic applications, including vaccines. Species D adenovirus type 26 (HAdV-D26) is both a cause of EKC and other diseases and a promising vaccine vector. HAdV-D26-derived vaccines are under investigation as protective platforms against HIV, Zika, and respiratory syncytial virus infections and are in phase 3 clinical trials for Ebola. We recently demonstrated that HAdV-D26 does not use CD46 or Desmoglein-2 as entry receptors, while the putative interaction with coxsackie and adenovirus receptor is low affinity and unlikely to represent the primary cell receptor. Here, we establish sialic acid as a primary entry receptor used by HAdV-D26. We demonstrate that removal of cell surface sialic acid inhibits HAdV-D26 infection, and provide a high-resolution crystal structure of HAdV-D26 fiber-knob in complex with sialic acid. PubMed: 31517055DOI: 10.1126/sciadv.aax3567 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.17 Å) |
Structure validation
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