Cryo-EM Structure of Chikungunya Virus in Complex with the Mxra8 Receptor

Katherine Basore, Arthur S. Kim, Christopher A. Nelson, Rong Zhang, Brittany K. Smith, Carla Uranga, Lo Vang, Ming Cheng, Michael L. Gross, Jonathan Smith, Michael S. Diamond, Daved H. Fremont

Research output: Contribution to journalArticlepeer-review

52 Scopus citations


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 languageEnglish
Pages (from-to)1725-1737.e16
Issue number7
StatePublished - Jun 13 2019


  • HDX mass spectrometry
  • alphavirus
  • cryo-electron microscopy
  • infection
  • protein crystallography
  • surface plasmon resonance
  • virus receptor


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