Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structure of Human adenovirus 7 virus-like particles, a platform for developing nanotherapeutics and studying capsid assembly.
Journal, issue, pages	Proc Natl Acad Sci U S A, Vol. 123, Issue 25, Page e2526969123, Year 2026
Publish date	Jun 23, 2026
Authors	Kiyano Madoo / Ryan Mazboudi / Zubaida Marufee Islam / Jonathan Luo / Robert A Kuschner / Paul Gottlieb / John J Dennehy / Rinat R Abzalimov / Jose M Galarza / Reza Khayat /
PubMed Abstract	Adenoviridae family members routinely infect humans, exhibit significant genetic diversity, and are associated with a variety of illnesses. Types 4 and 7 frequently circulate in the United States and ...Adenoviridae family members routinely infect humans, exhibit significant genetic diversity, and are associated with a variety of illnesses. Types 4 and 7 frequently circulate in the United States and are major causes of respiratory disease. Infections can result in hospitalization and, in severe cases, death. Although a live wild-type-virus vaccine targeting these two types exists, its use is restricted to military personnel due to concerns about viral-shedding and potential for genetic recombination. To overcome these limitations, we recently developed a virus-like particle (VLP) platform as an alternative vaccination strategy. These VLPs are stable, lack genomic material, and elicit a potent humoral immune response in mice, effectively neutralizing adenoviral infection. Here, we describe the cryo-EM structure of adenovirus 7 (AdV-7) VLPs. Structural insights are essential to ensure that neutralizing antigens displayed on the VLPs accurately mimic those of the virion, guide the design of particles with improved stability and efficacy, and enable engineering of VLPs with antigenic properties targeting multiple adenovirus types. The structure shows that hexon, penton, pIIIa, pVI, pVIII, and IX assemble comparable to AdV-5, hexon and penton neutralizing epitopes are appropriately displayed for antibody recognition, penton insertion into the hexon shell promotes cement protein pIIIa to increase its interaction with the peripentonal hexons, and presence of the core-genome is associated with increased interaction between cement protein pVIII and hexon. Finally, limited proteolysis and mass spectrometry demonstrate that VLP incorporated hexons digest more readily than virion incorporated hexons, indicating the greater dynamic nature of the VLP.
External links	Proc Natl Acad Sci U S A / PubMed:42301791 / PubMed Central
Methods	EM (single particle)
Resolution	3.7 - 6.2 Å
Structure data	EMDB-72771: Structure of the Adenovirus-7 PB-Fiber Method: EM (single particle) / Resolution: 6.2 Å 72772 9ych EMDB-72772, PDB-9ych: Structure of the Adenovirus-7 VLP, Class 4 Method: EM (single particle) / Resolution: 3.7 Å 72773 9yci EMDB-72773, PDB-9yci: Structure of the Adenovirus-7 VLP, Class 3 Method: EM (single particle) / Resolution: 3.9 Å 72774 9ycj EMDB-72774, PDB-9ycj: Structure of the Adenovirus-7 VLP, Class 2 Method: EM (single particle) / Resolution: 3.7 Å 72793 9yd0 EMDB-72793, PDB-9yd0: Structure of the Adenovirus-7 VLP, Class 1 Method: EM (single particle) / Resolution: 3.8 Å EMDB-72794: Structure of the Adenovirus-7 VLP Method: EM (single particle) / Resolution: 4.2 Å
Source	human adenovirus 7
Keywords	VIRUS LIKE PARTICLE / Adenovirus / vaccine / VLP