Dalia Jukneliene

TL;DR: The identification and characterization of a 316-amino-acid catalytic core domain of PLpro that can efficiently cleave replicase substrates in trans-cleavage assays and peptide substrate in fluorescent resonance energy transfer-based protease assays is reported.

TL;DR: This work identifies SARS coronavirus amino-terminal replicase products nsp1, nsp2, and nsp3 and describes trans-cleavage assays that characterize the protease activity required to generate these products and revealed that PLpro can cleave in trans at the three predicted cleavage sites and that it requires membrane association to process the nSP3/4 cleavage site.

TL;DR: The PathoSystems Resource Integration Center (PATRIC) is a data and analysis resource for selected NIAID priority pathogens, specifically proteobacteria of the genera Brucella, Rickettsia and Coxiella, and corona-, calici- and lyssaviruses and viruses associated with hepatitis A and E.

TL;DR: The membrane topology of nsp3-TM was determined and it was shown that TM-mediated tethering of PLP2 is important for processing at cleavage site 3 and that nsp2-TM is sufficient in mediating ER membrane association of a cytosolic protein.

TL;DR: It is demonstrated that PLpro has the ability to cleave ubiquitinated substrates and the characterization of a PLpro catalytic core will facilitate structural studies as well as high-throughput assays to identify antiviral compounds.