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.
Highlights
Attachment of human adenovirus (HAd) to the host cell is a critical step of infection
We recently demonstrated that HAd type 3 fibre knob (HAd3K) binds to desmoglein 2 (DSG2) by a non-classical mechanism involving mainly one receptor bound per trimeric fibre knob
The structural data confirm the biochemical data since clashes occur with three modules excluding the more commonly observed three-receptor per knob binding mode observed for other HAdreceptor complexes (Fig. 1d, e)
Summary
Attachment of human adenovirus (HAd) to the host cell is a critical step of infection. We report the cryo-electron microscopy (cryo-EM) structure of a
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