ArticleNature communications2025
Molecular mechanisms of the viral encoded chaperone 100K in capsid folding and assembly of adenovirus.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Structural Advances in Respiratory Syncytial Virus: Implications for Vaccine and Antiviral Development.Microorganisms · 2026Review
- The 100 K protein of adenovirus: character, location, and function.Archives of virology · 2026Review
- Nondestructive tracking of viral infections by viral protein-initiated fluorescent sensors.Journal of virology · 2026Article
- Development and characterization of neutralizing monoclonal antibodies against clinically relevant human adenovirus subgroup B serotypes.Virologica Sinica · 2026Article
- The changed endemic pattern of human adenovirus from species C to B among children in 2022-2024 in Shenzhen, China.Scientific reports · 2026Article
- C-reactive protein is a broad-spectrum capsule-binding receptor for hepatic capture of blood-borne bacteria.The EMBO journal · 2025Article
- Heterologous prime-boost immunization based on a human adenovirus 5 vectored containing Trichinella spiralis Cystatin-like protein elicits protective mucosal immunity in mice.PLoS neglected tropical diseases · 2025Article
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5 authors.
Funding
Abstract
Adenovirus is an icosahedral, non-enveloped DNA virus that infects humans and other animals. The capsid of adenovirus is mainly assembled by the major capsid protein hexon. Folding and assembly of hexon require the viral encoded chaperone 100K, of which the detailed structure and chaperoning mechanism remain unknown. Here, we report the cryoEM structure of 100K in complex with a pre-mature hexon trimer. The structure shows that 100K dimers bind to the bottom double jelly-roll domains of the pre-mature hexon, mainly through a hook-like domain and a loop extruded from the dimerization domain. Additionally, a groove formed at the dimerization interface of 100K accommodates the N-terminal fragment 49-53 of an adjacent hexon protomer. Mutagenesis studies indicate that the interactions at the jelly-roll domain and the N-terminus of hexon are all essential for the proper folding and assembly of hexon. 100K binds and stabilizes the partially folded hexon, preventing premature aggregation of hexon, promoting the folding of the hexon top insertion loops, and facilitating hexon trimerization.
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