Abstract
MxA protein is an interferon-induced GTPase of human cells that inhibits the multiplication of several RNA viruses, including influenza viruses and bunyaviruses. Studies on MxA transgenic mice have shown that MxA is a powerful antiviral agentin vivo.It has been suggested that this cellular protein also protects humans from viral disease, but the mechanism(s) by which MxA exerts its antiviral action is still poorly understood. Using anin vitrocosedimentation assay, we now demonstrate that MxA tightly interacts with components of the ribonucleoprotein complex of Thogoto virus, an influenza-like virus transmitted by ticks. This assay demonstrates for the first time a physical interaction between MxA GTPase and a viral target structure. It is based on three elements, namely, highly active MxA GTPases as effector molecules, viral ribonucleoprotein particles as viral targets, and GTPγS as a stabilizing factor. Furthermore, using a simple nuclear translocation assay, we show that human MxA protein forms oligomersin vivo.This assay provides a stringent test for tight association of partner molecules in intact mammalian cells. It not only will be useful for studying physical interactions of MxA with partner molecules, but may also be applicable to other studies on protein–protein interactions in living cells.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.