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TitleHuman species D adenovirus hexon capsid protein mediates cell entry through a direct interaction with CD46.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 118, Issue 3, Year 2021
Publish dateJan 19, 2021
AuthorsB David Persson / Lijo John / Karim Rafie / Michael Strebl / Lars Frängsmyr / Monika Z Ballmann / Katja Mindler / Menzo Havenga / Angelique Lemckert / Thilo Stehle / Lars-Anders Carlson / Niklas Arnberg /
PubMed AbstractHuman adenovirus species D (HAdV-D) types are currently being explored as vaccine vectors for coronavirus disease 2019 (COVID-19) and other severe infectious diseases. The efficacy of such vector- ...Human adenovirus species D (HAdV-D) types are currently being explored as vaccine vectors for coronavirus disease 2019 (COVID-19) and other severe infectious diseases. The efficacy of such vector-based vaccines depends on functional interactions with receptors on host cells. Adenoviruses of different species are assumed to enter host cells mainly by interactions between the knob domain of the protruding fiber capsid protein and cellular receptors. Using a cell-based receptor-screening assay, we identified CD46 as a receptor for HAdV-D56. The function of CD46 was validated in infection experiments using cells lacking and overexpressing CD46, and by competition infection experiments using soluble CD46. Remarkably, unlike HAdV-B types that engage CD46 through interactions with the knob domain of the fiber protein, HAdV-D types infect host cells through a direct interaction between CD46 and the hexon protein. Soluble hexon proteins (but not fiber knob) inhibited HAdV-D56 infection, and surface plasmon analyses demonstrated that CD46 binds to HAdV-D hexon (but not fiber knob) proteins. Cryoelectron microscopy analysis of the HAdV-D56 virion-CD46 complex confirmed the interaction and showed that CD46 binds to the central cavity of hexon trimers. Finally, soluble CD46 inhibited infection by 16 out of 17 investigated HAdV-D types, suggesting that CD46 is an important receptor for a large group of adenoviruses. In conclusion, this study identifies a noncanonical entry mechanism used by human adenoviruses, which adds to the knowledge of adenovirus biology and can also be useful for development of adenovirus-based vaccine vectors.
External linksProc Natl Acad Sci U S A / PubMed:33384338 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.38201802428 - 5.11 Å
Structure data

EMDB-11593:
The structure of HAdV-D56
Method: EM (single particle) / Resolution: 4.82 Å

EMDB-11594:
The structure of HAdV-D56 in complex with CD46
Method: EM (single particle) / Resolution: 5.11 Å

PDB-7ajp:
Crystal Structure of Human Adenovirus 56 Fiber Knob
Method: X-RAY DIFFRACTION / Resolution: 1.38201802428 Å

Chemicals

ChemComp-GOL:
GLYCEROL / Glycerol

ChemComp-NO3:
NITRATE ION / Nitrate

ChemComp-EDO:
1,2-ETHANEDIOL / Ethylene glycol

ChemComp-PGE:
TRIETHYLENE GLYCOL / Polyethylene glycol

ChemComp-HOH:
WATER / Water

Source
  • Homo sapiens (human)
  • human adenovirus 56
KeywordsVIRAL PROTEIN / Human Adenovirus / Fiber Knob

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