Congratulations to co-first authors, current graduate student Krista Meserve and lab alumnus Dr. Abe Qavi, for their latest publication! Their protocol paper explains the method they used for the detection of EBOV and SUDV sGP using the microring resonators. Check out the full protocol here.
Detection of biomarkers for filoviral infection with a silicon photonic resonator platform
Summary: This protocol describes the use of silicon photonic microring resonator sensors for detection of Ebola virus (EBOV) and Sudan virus (SUDV) soluble glycoprotein (sGP). This protocol encompasses biosensor functionalization of silicon microring resonator chips, detection of protein biomarkers in sera, preparing calibration standards for analytical validation, and quantification of the results from these experiments. This protocol is readily adaptable toward other analytes, including cytokines, chemokines, nucleic acids, and viruses.
In addition, congratulations to lab alumna, Dr. Colleen Riordan, for her contributions to a recently published paper in collaboration wtih the Marsh lab at UM! Check out the full publication here.
Purification of the full-length, membrane-associated form of the antiviral enzyme viperin utilizing nanodiscs
Abstract: Viperin is a radical S-adenosylmethionine enzyme that catalyzes the formation of the antiviral ribonucleotide, 3’-deoxy-3’,4’-didehydroCTP. The enzyme is conserved across all kingdoms of life, and in higher animals viperin is localized to the ER-membrane and lipid droplets through an N-terminal extension that forms an amphipathic helix. Evidence suggests that the N-terminal extension plays an important role in viperin’s interactions with other membrane proteins. These interactions serve to modulate the activity of various other enzymes that are important for viral replication and constitute another facet of viperin’s antiviral properties, distinct from its catalytic activity. However, the full-length form of the enzyme, which has proved refractory to expression in E. coli, has not been previously purified. Here we report the purification of the full-length form of viperin from HEK293T cells transfected with viperin. The purification method utilizes nanodiscs to maintain the protein in its membrane-bound state. Unexpectedly, the enzyme exhibits significantly lower catalytic activity once purified, suggesting that interactions with other ER-membrane components may be important to maintain viperin’s activity.