Phosphorylation-tuned condensation links HCMV tegument assembly to membrane recruitment
- 1Hannover Medical School
Abstract
Herpesviruses build complex infectious particles around a protein layer, the tegument, that lacks an ordered architecture. How this apparently amorphous material selectively assembles on the capsid and engages enveloping membranes remains unclear. Here we show that the capsid-anchored human cytomegalovirus protein pp150 forms liquid-like condensates when locally concentrated. Its disordered region recruits soluble tegument proteins and membrane-associated partners, providing a mechanism to couple assembly of the tegument layer to recruitment of the enclosing membrane. Phosphorylation tunes this condensation: phosphomimetic mutations prevent recovery of infectious virus, whereas loss of phosphorylation sites causes aberrant capsid-tegument assemblies and impairs viral replication. Together, these findings identify regulated condensation as a mechanism that couples tegument assembly to membrane recruitment and supports the production of infectious particles, highlighting condensate regulation as a potentially novel point of antiviral intervention.
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BibTeX
@misc{jensen2026phosphorylationtuned,
title = {{Phosphorylation-tuned condensation links HCMV tegument assembly to membrane recruitment}},
author = {Y. Jensen and L. Cortez Rayas and B. Bogdanow and I. B. Gruska and B. Vetter and E. Caragliano and L. Muehlberg and J. von Einem and L. Wiebusch and J. B. Bosse},
howpublished = {bioRxiv},
year = {2026},
month = aug,
doi = {10.64898/2026.08.05.743017},
url = {https://www.biorxiv.org/content/10.64898/2026.08.05.743017v2},
note = {CC BY-NC-ND},
}
RIS
TY - UNPB
TI - Phosphorylation-tuned condensation links HCMV tegument assembly to membrane recruitment
AU - Y. Jensen
AU - L. Cortez Rayas
AU - B. Bogdanow
AU - I. B. Gruska
AU - B. Vetter
AU - E. Caragliano
AU - L. Muehlberg
AU - J. von Einem
AU - L. Wiebusch
AU - J. B. Bosse
PY - 2026
DA - 2026/08/05
PB - bioRxiv
DO - 10.64898/2026.08.05.743017
UR - https://www.biorxiv.org/content/10.64898/2026.08.05.743017v2
AB - Herpesviruses build complex infectious particles around a protein layer, the tegument, that lacks an ordered architecture. How this apparently amorphous material selectively assembles on the capsid and engages enveloping membranes remains unclear. Here we show that the capsid-anchored human cytomegalovirus protein pp150 forms liquid-like condensates when locally concentrated. Its disordered region recruits soluble tegument proteins and membrane-associated partners, providing a mechanism to couple assembly of the tegument layer to recruitment of the enclosing membrane. Phosphorylation tunes this condensation: phosphomimetic mutations prevent recovery of infectious virus, whereas loss of phosphorylation sites causes aberrant capsid-tegument assemblies and impairs viral replication. Together, these findings identify regulated condensation as a mechanism that couples tegument assembly to membrane recruitment and supports the production of infectious particles, highlighting condensate regulation as a potentially novel point of antiviral intervention.
ER -