It has recently been shown that MXRA8 acts as a viral entry receptor for multiple arthritogenic alphaviruses that cause debilitating acute and chronic musculoskeletal disease in humans, including Chikungunya virus (CHIKV), Mayaro virus and O’nyong’nyong virus. Blocking this interaction with antibodies has been shown to reduce the severity of infection with these viruses in mouse models, and therefore MXRA8 is now receiving attention as a possible therapeutic target. X-ray crystal structure (2.2 Å) and cryo-electron microscopy (4-5 Å) reconstructions of MXRA8 bound to chikungunya (CHIKV) virus-like particles and infectious virus have shown that MXRA8 has an unusual Ig-like fold topology and complex quaternary binding site that spans the CHIKV E2 and E1 proteins. Two binding modes were observed with the fully mature CHIKV VLP, with one MXRA8 binding with unique contacts. Only the high-affinity binding mode was observed in the complex with infectious CHIKV, as viral maturation and the presence of E3 appeared to affect the mode of MXRA8 binding (Basore et al., 2019). We are pleased to make available highly purified recombinant MXRA8 produced in our mammalian expression system using HEK293 cells. Alongside our recombinant alphavirus proteins, this reagent offers an excellent model for studying alphavirus infection. We have demonstrated that recombinant MXRA8 binds to our recombinant Chikungunya Virus-like particles, mimicking the natural interaction during viral infection, and therefore providing a simple to use in vitro model to assess potential therapeutic molecules that block the virus receptor interaction (Basore et al., 2019).
Recombinant protein corresponding to aa1-341 of human MXRA8, fused to a C-terminal 9aa glycine-serine linker followed by a mouse IgG2a Fc-tag, expressed in HEK293 cells.
Molecular Weight:~25kD
Storage and Stability:Aliquot to avoid repeated freezing and thawing and store at -70°C. Aliquots are stable for 6 months after receipt. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
