Joseph P. Klaus

TL;DR: Evidence is presented that suggests M can adopt two conformations and that membrane curvature is regulated by one M conformer, providing insight into how M protein functions to promote virus assembly.

TL;DR: A higher-resolution functional domain architecture for nsp3 is proposed that determines the interaction capacity of this protein, which is intimately associated with viral RNA in its role as a virion component.

TL;DR: A class of pathogen-derived ERG IC-53 ligands, a lectin-independent basis for their association with ERGIC-53, and a role for ERGic-53 in the propagation of several highly pathogenic RNA virus families are identified.

TL;DR: It is shown that neither the PPXY late domain encoded within the lymphocytic choriomeningitis virus (LCMV) matrix protein nor a functional endosomal sorting complex transport (ESCRT) pathway is absolutely required for the generation of standard infectious virus particles, and it is indicated that this posttranslational modification may regulate DI particle formation.

TL;DR: To better understand the molecular mechanism of ESCRT recruitment by the PPXY late domain, affinity purification-mass spectrometry was used to identify host proteins that interact with the Z proteins of the Old World mammarenaviruses LCMV and Lassa virus and it was demonstrated that Nedd4 family E3 ubiquitin ligases directly ubiquitinateLCMV Z and mapped the specific lysine residues modified.