CryoEM structure of adenovirus type 3 fibre with desmoglein 2 shows an unusual mode of receptor engagement.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 30862836.
- Also identified by DOI 10.1038/s41467-019-09220-y and PMC identifier 6414520.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
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.
Medical subject headings
- Adenoviruses, Human
- Capsid Proteins
- Desmoglein 2
- Receptors, Virus
- Virus Attachment