National Institutes of Health/National Institute of Dental and Craniofacial Research (NIH/NIDCR)
DE028583
United States
National Institutes of Health/National Institute of Dental and Craniofacial Research (NIH/NIDCR)
DE025567
United States
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)
AI094386
United States
National Institutes of Health/Office of the Director
1S10OD018111
United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
1U24GM116792
United States
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)
R01AI103182
United States
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)
R33AI119721
United States
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)
AI007323
United States
National Science Foundation (NSF, United States)
DBI-1338135
United States
National Science Foundation (NSF, United States)
DMR-1548924
United States
Citation
Journal: mBio / Year: 2021 Title: Atomic Structure of the Trichomonas vaginalis Double-Stranded RNA Virus 2. Authors: Alexander Stevens / Katherine Muratore / Yanxiang Cui / Patricia J Johnson / Z Hong Zhou / Abstract: , the causative pathogen for the most common nonviral sexually transmitted infection worldwide, is itself frequently infected with one or more of the four types of small double-stranded RNA (dsRNA) ..., the causative pathogen for the most common nonviral sexually transmitted infection worldwide, is itself frequently infected with one or more of the four types of small double-stranded RNA (dsRNA) viruses (TVV1 to 4, genus , family ). Each TVV encloses a nonsegmented genome within a single-layered capsid and replicates entirely intracellularly, like many dsRNA viruses, and unlike those in the family. Here, we have determined the structure of TVV2 by cryo-electron microscopy (cryoEM) at 3.6 Å resolution and derived an atomic model of its capsid. TVV2 has an icosahedral, T = 2*, capsid comprised of 60 copies of the icosahedral asymmetric unit (a dimer of the two capsid shell protein [CSP] conformers, CSP-A and CSP-B), typical of icosahedral dsRNA virus capsids. However, unlike the robust CSP-interlocking interactions such as the use of auxiliary "clamping" proteins among , only lateral CSP interactions are observed in TVV2, consistent with an assembly strategy optimized for TVVs' intracellular-only replication cycles within their protozoan host. The atomic model reveals both a mostly negatively charged capsid interior, which is conducive to movement of the loosely packed genome, and channels at the 5-fold vertices, which we suggest as routes of mRNA release during transcription. Structural comparison of TVV2 to the L-A virus reveals a conserved helix-rich fold within the CSP and putative guanylyltransferase domain along the capsid exterior, suggesting conserved mRNA maintenance strategies among This first atomic structure of a TVV provides a framework to guide future biochemical investigations into the interplay between and its viruses. viruses (TVVs) are double-stranded RNA (dsRNA) viruses that cohabitate in , the causative pathogen of trichomoniasis, the most common nonviral sexually transmitted disease worldwide. Featuring an unsegmented dsRNA genome encoding a single capsid shell protein (CSP), TVVs contrast with multisegmented dsRNA viruses, such as the diarrhea-causing rotavirus, whose larger genome is split into 10 dsRNA segments encoding 5 unique capsid proteins. To determine how TVVs incorporate the requisite functionalities for viral replication into their limited proteome, we derived the atomic model of TVV2, a first for TVVs. Our results reveal the intersubunit interactions driving CSP association for capsid assembly and the properties that govern organization and maintenance of the viral genome. Structural comparison between TVV2 capsids and those of distantly related dsRNA viruses indicates conserved strategies of nascent RNA release and a putative viral guanylyltransferase domain implicated in the cytoplasmic maintenance of viral messenger and genomic RNA.
Average exposure time: 0.2 sec. / Electron dose: 17 e/Å2 / Detector mode: SUPER-RESOLUTION / Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Num. of real images: 2177
EM imaging optics
Energyfilter name: GIF Quantum LS / Energyfilter slit width: 20 eV
Image scans
Width: 3838 / Height: 3710 / Movie frames/image: 30
-
Processing
EM software
ID
Name
Version
Category
1
RELION
3.1
particleselection
2
SerialEM
imageacquisition
4
CTFFIND
4
CTFcorrection
10
RELION
3.1
initialEulerassignment
11
RELION
3.1
finalEulerassignment
12
RELION
3.1
classification
13
RELION
3.1
3Dreconstruction
CTF correction
Type: PHASE FLIPPING AND AMPLITUDE CORRECTION
Particle selection
Num. of particles selected: 5076
Symmetry
Point symmetry: I (icosahedral)
3D reconstruction
Resolution: 4 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 29916 / Num. of class averages: 1 / Symmetry type: POINT
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