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Nat Commun. 2019 Mar 12;10(1):1181. doi: 10.1038/s41467-019-09220-y.

CryoEM structure of adenovirus type 3 fibre with desmoglein 2 shows an unusual mode of receptor engagement.

Author information

1
Institut de Biologie Structurale (IBS), Université Grenoble Alpes, CNRS, CEA, 71 Avenue des Martyrs, 38042, Grenoble, France.
2
Laboratoire de Physiologie Cellulaire et Végétale, Biosciences and Biotechnology Institute of Grenoble, UMR5168, CNRS/CEA/INRA/UGA, 17 Rue des Martyrs, 38054, Grenoble, France.
3
Unité de Virologie, Institut de Recherche Biomédicale des Armées, BP 73, 91223, Brétigny-sur-Orge Cedex, France.
4
Department of Medicine, Division of Medical Genetics, University of Washington, Box 357720, Seattle, WA, 98195, USA.
5
Department of Medicine, Division of Medical Genetics, University of Washington, Box 357720, Seattle, WA, 98195, USA. lieber00@u.washington.edu.
6
Institut de Biologie Structurale (IBS), Université Grenoble Alpes, CNRS, CEA, 71 Avenue des Martyrs, 38042, Grenoble, France. pascal.fender@ibs.fr.

Abstract

Attachment of human adenovirus (HAd) to the host cell is a critical step of infection. Initial attachment occurs via the adenoviral fibre knob protein and a cellular receptor. Here we report the cryo-electron microscopy (cryo-EM) structure of a <100 kDa non-symmetrical complex comprising the trimeric HAd type 3 fibre knob (HAd3K) and human desmoglein 2 (DSG2). The structure reveals a unique stoichiometry of 1:1 and 2:1 (DSG2: knob trimer) not previously observed for other HAd-receptor complexes. We demonstrate that mutating Asp261 in the fibre knob is sufficient to totally abolish receptor binding. These data shed new light on adenovirus infection strategies and provide insights for adenoviral vector development and structure-based design.

PMID:
30862836
DOI:
10.1038/s41467-019-09220-y
Free PMC Article

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