Mapping of Adenovirus of serotype 3 fibre interaction to desmoglein 2 revealed a novel 'non-classical' mechanism of viral receptor engagement

Scientific Reports
Emilie Vassal-StermannPascal Fender

Abstract

High-affinity binding of the trimeric fibre protein to a cell surface primary receptor is a common feature shared by all adenovirus serotypes. Recently, a long elusive species B adenovirus receptor has been identified. Desmoglein 2 (DSG2) a component of desmosomal junction, has been reported to interact at high affinity with Human adenoviruses HAd3, HAd7, HAd11 and HAd14. Little is known with respect to the molecular interactions of adenovirus fibre with the DSG2 ectodomain. By using different DSG2 ectodomain constructs and biochemical and biophysical experiments, we report that the third extracellular cadherin domain (EC3) of DSG2 is critical for HAd3 fibre binding. Unexpectedly, stoichiometry studies using multi-angle laser light scattering (MALLS) and analytical ultra-centrifugation (AUC) revealed a non-classical 1:1 interaction (one DSG2 per trimeric fibre), thus differentiating 'DSG2-interacting' adenoviruses from other protein receptor interacting adenoviruses in their infection strategy.

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Citations

Dec 5, 2019·Acta Crystallographica. Section F, Structural Biology Communications·Emilie Vassal-StermannWim P Burmeister
Jan 17, 2020·FEBS Letters·Michael A BarryShao-Chia Lu
Mar 14, 2019·Nature Communications·Emilie Vassal-StermannPascal Fender
Jun 3, 2021·International Journal of Molecular Sciences·José GallardoCarmen San Martín

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Datasets Mentioned

BETA
ABB17809.1

Methods Mentioned

BETA
glycosylation
surface plasmon resonance
size exclusion chromatography
Gel filtration
transfection
Affinity purification
electron microscopy
Light Scattering
light-scattering
X-ray

Software Mentioned

SEDNTERP
Astra
SE
SEDFIT
AUC

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