TY  - JOUR
AU  - Bogdanow, Boris
AU  - Gruska, Iris
AU  - Mühlberg, Lars
AU  - Protze, Jonas
AU  - Hohensee, Svea
AU  - Vetter, Barbara
AU  - Bosse, Jens B.
AU  - Lehmann, Martin
AU  - Sadeghi, Mohsen
AU  - Wiebusch, Lüder
AU  - Liu, Fan
TI  - Spatially resolved protein map of intact human cytomegalovirus virions
JO  - Nature microbiology
VL  - 8
IS  - 9
SN  - 2058-5276
CY  - London
PB  - Nature Publishing Group
M1  - PUBDB-2024-00334
SP  - 1732 - 1747
PY  - 2023
AB  - Herpesviruses assemble large enveloped particles that are difficult to characterize structurally due to their size, fragility and complex multilayered proteome with partially amorphous nature. Here we used crosslinking mass spectrometry and quantitative proteomics to derive a spatially resolved interactome map of intact human cytomegalovirus virions. This enabled the de novo allocation of 32 viral proteins into four spatially resolved virion layers, each organized by a dominant viral scaffold protein. The viral protein UL32 engages with all layers in an N-to-C-terminal radial orientation, bridging nucleocapsid to viral envelope. We observed the layer-specific incorporation of 82 host proteins, of which 39 are selectively recruited. We uncovered how UL32, by recruitment of PP-1 phosphatase, antagonizes binding to 14-3-3 proteins. This mechanism assures effective viral biogenesis, suggesting a perturbing role of UL32-14-3-3 interaction. Finally, we integrated these data into a coarse-grained model to provide global insights into the native configuration of virus and host protein interactions inside herpesvirions.
LB  - PUB:(DE-HGF)16
C6  - pmid:37550507
UR  - <Go to ISI:>//WOS:001043678400003
DO  - DOI:10.1038/s41564-023-01433-8
UR  - https://bib-pubdb1.desy.de/record/601641
ER  -