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

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 trim...

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Autores principales: Vassal-Stermann, Emilie, Effantin, Gregory, Zubieta, Chloe, Burmeister, Wim, Iseni, Frédéric, Wang, Hongjie, Lieber, André, Schoehn, Guy, Fender, Pascal
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2019
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6414520/
https://www.ncbi.nlm.nih.gov/pubmed/30862836
http://dx.doi.org/10.1038/s41467-019-09220-y
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author Vassal-Stermann, Emilie
Effantin, Gregory
Zubieta, Chloe
Burmeister, Wim
Iseni, Frédéric
Wang, Hongjie
Lieber, André
Schoehn, Guy
Fender, Pascal
author_facet Vassal-Stermann, Emilie
Effantin, Gregory
Zubieta, Chloe
Burmeister, Wim
Iseni, Frédéric
Wang, Hongjie
Lieber, André
Schoehn, Guy
Fender, Pascal
author_sort Vassal-Stermann, Emilie
collection PubMed
description 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.
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spelling pubmed-64145202019-03-14 CryoEM structure of adenovirus type 3 fibre with desmoglein 2 shows an unusual mode of receptor engagement Vassal-Stermann, Emilie Effantin, Gregory Zubieta, Chloe Burmeister, Wim Iseni, Frédéric Wang, Hongjie Lieber, André Schoehn, Guy Fender, Pascal Nat Commun Article 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. Nature Publishing Group UK 2019-03-12 /pmc/articles/PMC6414520/ /pubmed/30862836 http://dx.doi.org/10.1038/s41467-019-09220-y Text en © The Author(s) 2019 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Vassal-Stermann, Emilie
Effantin, Gregory
Zubieta, Chloe
Burmeister, Wim
Iseni, Frédéric
Wang, Hongjie
Lieber, André
Schoehn, Guy
Fender, Pascal
CryoEM structure of adenovirus type 3 fibre with desmoglein 2 shows an unusual mode of receptor engagement
title CryoEM structure of adenovirus type 3 fibre with desmoglein 2 shows an unusual mode of receptor engagement
title_full CryoEM structure of adenovirus type 3 fibre with desmoglein 2 shows an unusual mode of receptor engagement
title_fullStr CryoEM structure of adenovirus type 3 fibre with desmoglein 2 shows an unusual mode of receptor engagement
title_full_unstemmed CryoEM structure of adenovirus type 3 fibre with desmoglein 2 shows an unusual mode of receptor engagement
title_short CryoEM structure of adenovirus type 3 fibre with desmoglein 2 shows an unusual mode of receptor engagement
title_sort cryoem structure of adenovirus type 3 fibre with desmoglein 2 shows an unusual mode of receptor engagement
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6414520/
https://www.ncbi.nlm.nih.gov/pubmed/30862836
http://dx.doi.org/10.1038/s41467-019-09220-y
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