National Institutes of Health/National Institute of Dental and Craniofacial Research (NIH/NIDCR)
DE028583
United States
National Institutes of Health/National Institute of Arthritis and Musculoskeletal and Skin Diseases (NIH/NIAMS)
T32AR071307
United States
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)
P30 AI152501
United States
James B. Pendleton Charitable Trust (to the UCLA AIDS Institute)
United States
McCarthy Family Foundation (to the UCLA AIDS Institute)
United States
National Institutes of Health/Office of the Director
1S10RR23057
United States
National Institutes of Health/Office of the Director
1S10OD018111
United States
National Science Foundation (NSF, United States)
DBI-1338135
United States
National Science Foundation (NSF, United States)
DMR-1548924
United States
Citation
Journal: Sci Adv / Year: 2024 Title: The incredible bulk: Human cytomegalovirus tegument architectures uncovered by AI-empowered cryo-EM. Authors: Jonathan Jih / Yun-Tao Liu / Wei Liu / Z Hong Zhou / Abstract: The compartmentalization of eukaryotic cells presents considerable challenges to the herpesvirus life cycle. The herpesvirus tegument, a bulky proteinaceous aggregate sandwiched between ...The compartmentalization of eukaryotic cells presents considerable challenges to the herpesvirus life cycle. The herpesvirus tegument, a bulky proteinaceous aggregate sandwiched between herpesviruses' capsid and envelope, is uniquely evolved to address these challenges, yet tegument structure and organization remain poorly characterized. We use deep-learning-enhanced cryogenic electron microscopy to investigate the tegument of human cytomegalovirus virions and noninfectious enveloped particles (NIEPs; a genome packaging-aborted state), revealing a portal-biased tegumentation scheme. We resolve atomic structures of portal vertex-associated tegument (PVAT) and identify multiple configurations of PVAT arising from layered reorganization of pUL77, pUL48 (large tegument protein), and pUL47 (inner tegument protein) assemblies. Analyses show that pUL77 seals the last-packaged viral genome end through electrostatic interactions, pUL77 and pUL48 harbor a head-linker-capsid-binding motif conducive to PVAT reconfiguration, and pUL47/48 dimers form 45-nm-long filaments extending from the portal vertex. These results provide a structural framework for understanding how herpesvirus tegument facilitates and evolves during processes spanning viral genome packaging to delivery.
Shell ID: 1 / Name: Virion capsid / T number (triangulation number): 16
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Experimental details
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Structure determination
Method
cryo EM
Processing
single particle reconstruction
Aggregation state
particle
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Sample preparation
Buffer
pH: 7.4
Vitrification
Cryogen name: ETHANE / Instrument: FEI VITROBOT MARK IV
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Electron microscopy
Microscope
FEI TITAN KRIOS
Image recording
Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: SUPER-RESOLUTION / Average exposure time: 8.0 sec. / Average electron dose: 47.2 e/Å2
Electron beam
Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
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