8OFU

Human adenovirus type 53 fiber-knob protein

Summary for 8OFU

• Entry DOI: 10.2210/pdb8ofu/pdb
• Descriptor: Fiber protein, SULFATE ION, 1,2-ETHANEDIOL, ... (5 entities in total)
• Functional Keywords: adenovirus, fiber knob, ad25, viral protein
• Biological source: Human adenovirus 53
• Total number of polymer chains: 6
• Total formula weight: 129835.01

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: 2024-05-08)

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

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: 38665237
DOI: 10.1038/s44298-023-00001-5

Experimental method

X-RAY DIFFRACTION (1.61 Å)