8OFP
Human adenovirus type 24 fiber-knob protein
Summary for 8OFP
Entry DOI | 10.2210/pdb8ofp/pdb |
Descriptor | Fiber (1 entity in total) |
Functional Keywords | adenovirus, fiber knob, ad24, viral protein |
Biological source | Human adenovirus 24 |
Total number of polymer chains | 6 |
Total formula weight | 132748.90 |
Authors | Rizkallah, P.J.,Parker, A.L.,Mundy, R.M.,Baker, A.T. (deposition date: 2023-03-16, release date: 2023-09-20, Last modification date: 2024-10-23) |
Primary citation | Mundy, R.M.,Baker, A.T.,Bates, E.A.,Cunliffe, T.G.,Teijeira-Crespo, A.,Moses, E.,Rizkallah, P.J.,Parker, A.L. Broad sialic acid usage amongst species D human adenovirus. Npj Viruses, 1:1-1, 2023 Cited by PubMed Abstract: Human adenoviruses (HAdV) are widespread pathogens causing usually mild infections. The Species D (HAdV-D) cause gastrointestinal tract infections and epidemic keratoconjunctivitis (EKC). Despite being significant pathogens, knowledge around HAdV-D mechanism of cell infection is lacking. Sialic acid (SA) usage has been proposed as a cell infection mechanism for EKC causing HAdV-D. Here we highlight an important role for SA engagement by many HAdV-D. We provide apo state crystal structures of 7 previously undetermined HAdV-D fiber-knob proteins, and structures of HAdV-D25, D29, D30 and D53 fiber-knob proteins in complex with SA. Biologically, we demonstrate that removal of cell surface SA reduced infectivity of HAdV-C5 vectors pseudotyped with HAdV-D fiber-knob proteins, whilst engagement of the classical HAdV receptor CAR was variable. Our data indicates variable usage of SA and CAR across HAdV-D. Better defining these interactions will enable improved development of antivirals and engineering of the viruses into refined therapeutic vectors. PubMed: 38665237DOI: 10.1038/s44298-023-00001-5 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.1 Å) |
Structure validation
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