Abstract
Basore et al. describe an X-ray crystal structure of Mxra8, an entry receptor for arthritogenic alphaviruses, and cryo-EM structures of Mxra8 bound to CHIKV. Mxra8 has an unusual Ig-like domain architecture with a head-to-head arrangement, with domain 1 emanating from a loop of domain 2. Mxra8 binds into a complex quaternary cleft formed between two E2-E1 heterodimers within a trimeric spike, while also contacting E1 from a neighboring spike. Mxra8 occupancy is lower when E3 protein is retained on the virion.
Original language | English |
---|---|
Pages (from-to) | 1725-1737.e16 |
Journal | Cell |
Volume | 177 |
Issue number | 7 |
DOIs | |
State | Published - Jun 13 2019 |
Keywords
- HDX mass spectrometry
- alphavirus
- cryo-electron microscopy
- infection
- protein crystallography
- surface plasmon resonance
- virus receptor