NEDD4 family ubiquitin ligases associate with LCMV Z’s PPXY domain and are required for virus budding, but not via direct ubiquitination of Z

Autoři: Christopher M. Ziegler aff001;  Loan Dang aff001;  Philip Eisenhauer aff001;  Jamie A. Kelly aff001;  Benjamin R. King aff001;  Joseph P. Klaus aff001;  Inessa Manuelyan aff001;  Ethan B. Mattice aff002;  David J. Shirley aff003;  Marion E. Weir aff004;  Emily A. Bruce aff001;  Bryan A. Ballif aff004;  Jason Botten aff001
Působiště autorů: Department of Medicine, Division of Immunobiology, University of Vermont, Burlington, Vermont, United States of America aff001;  Cellular, Molecular and Biomedical Sciences Graduate Program, University of Vermont, Burlington, Vermont, United States of America aff002;  Ixis LLC, Data Science Division, Burlington, Vermont, United States of America aff003;  Department of Biology, University of Vermont, Burlington, Vermont, United States of America aff004;  Department of Microbiology and Molecular Genetics, University of Vermont, Burlington, Vermont, United States of America aff005
Vyšlo v časopise: NEDD4 family ubiquitin ligases associate with LCMV Z’s PPXY domain and are required for virus budding, but not via direct ubiquitination of Z. PLoS Pathog 15(11): e32767. doi:10.1371/journal.ppat.1008100
Kategorie: Research Article


Viral late domains are used by many viruses to recruit the cellular endosomal sorting complex required for transport (ESCRT) to mediate membrane scission during viral budding. Unlike the P(S/T)AP and YPX(1–3)L late domains, which interact directly with the ESCRT proteins Tsg101 and ALIX, the molecular linkage connecting the PPXY late domain to ESCRT proteins is unclear. The mammarenavirus lymphocytic choriomeningitis virus (LCMV) matrix protein, Z, contains only one late domain, PPXY. We previously found that this domain in LCMV Z, as well as the ESCRT pathway, are required for the release of defective interfering (DI) particles but not infectious virus. 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. Several Nedd4 family E3 ubiquitin ligases interact with these matrix proteins and in the case of LCMV Z, the interaction was PPXY-dependent. We demonstrated that these ligases directly ubiquitinate LCMV Z and mapped the specific lysine residues modified. A recombinant LCMV containing a Z that cannot be ubiquitinated maintained its ability to produce both infectious virus and DI particles, suggesting that direct ubiquitination of LCMV Z alone is insufficient for recruiting ESCRT proteins to mediate virus release. However, Nedd4 ligases appear to be important for DI particle release suggesting that ubiquitination of targets other than the Z protein itself is required for efficient viral ESCRT recruitment.

Klíčová slova:

Interaction networks – Lysine – Membrane proteins – Protein domains – Small interfering RNAs – Ubiquitination – Virions – Ubiquitin ligases


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