National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
R35GM122510
United States
Citation
Journal: Virus Evol / Year: 2020 Title: Structure of a filamentous virus uncovers familial ties within the archaeal virosphere. Authors: Fengbin Wang / Diana P Baquero / Zhangli Su / Tomasz Osinski / David Prangishvili / Edward H Egelman / Mart Krupovic / Abstract: Viruses infecting hyperthermophilic archaea represent one of the most enigmatic parts of the global virome, with viruses from different families showing no genomic relatedness to each other or to ...Viruses infecting hyperthermophilic archaea represent one of the most enigmatic parts of the global virome, with viruses from different families showing no genomic relatedness to each other or to viruses of bacteria and eukaryotes. Tristromaviruses, which build enveloped filamentous virions and infect hyperthermophilic neutrophiles of the order Thermoproteales, represent one such enigmatic virus families. They do not share genes with viruses from other families and have been believed to represent an evolutionarily independent virus lineage. A cryo-electron microscopic reconstruction of the tristromavirus Pyrobaculum filamentous virus 2 at 3.4 Å resolution shows that the virion is constructed from two paralogous major capsid proteins (MCP) which transform the linear dsDNA genome of the virus into A-form by tightly wrapping around it. Unexpectedly, the two MCP are homologous to the capsid proteins of other filamentous archaeal viruses, uncovering a deep evolutionary relationship within the archaeal virosphere.
1: A-DNA 2: A-DNA A: Structural protein VP1 B: Structural protein VP1 C: Structural protein VP1 D: Structural protein VP1 E: Structural protein VP1 F: Structural protein VP1 G: Structural protein VP1 H: Structural protein VP1 I: Structural protein VP1 J: Structural protein VP1 K: Structural protein VP1 L: Structural protein VP1 M: Structural protein VP1 N: Structural protein VP1 O: Structural protein VP1 P: Structural protein VP1 Q: Structural protein VP1 R: Structural protein VP1 S: Structural protein VP1 T: Structural protein VP1 U: Structural protein VP1 V: Structural protein VP1 W: Structural protein VP1 a: Structural protein VP2 b: Structural protein VP2 c: Structural protein VP2 d: Structural protein VP2 e: Structural protein VP2 f: Structural protein VP2 g: Structural protein VP2 h: Structural protein VP2 i: Structural protein VP2 j: Structural protein VP2 k: Structural protein VP2 l: Structural protein VP2 m: Structural protein VP2 n: Structural protein VP2 o: Structural protein VP2 p: Structural protein VP2 q: Structural protein VP2 r: Structural protein VP2 s: Structural protein VP2 t: Structural protein VP2 u: Structural protein VP2 v: Structural protein VP2 w: Structural protein VP2
Evidence: microscopy, helical filament was observed by negative staining and Cryo-EM
Type
Name
Symmetry operation
Number
identity operation
1_555
1
Buried area
316570 Å2
ΔGint
-1463 kcal/mol
Surface area
240570 Å2
Symmetry
Helical symmetry: (Circular symmetry: 1 / Dyad axis: no / N subunits divisor: 1 / Num. of operations: 23 / Rise per n subunits: 2.864 Å / Rotation per n subunits: 22.9482 °)
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Components
#1: DNA chain
A-DNA
Mass: 99669.547 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Pyrobaculum filamentous virus 1
#2: DNA chain
A-DNA
Mass: 99660.539 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Pyrobaculum filamentous virus 1
#3: Protein
... StructuralproteinVP1
Mass: 14986.418 Da / Num. of mol.: 23 / Source method: isolated from a natural source / Source: (natural) Pyrobaculum filamentous virus 1 / References: UniProt: A0A140F3K6
#4: Protein
... StructuralproteinVP2
Mass: 15326.556 Da / Num. of mol.: 23 / Source method: isolated from a natural source / Source: (natural) Pyrobaculum filamentous virus 1 / References: UniProt: A0A140F3K7
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Experimental details
-
Experiment
Experiment
Method: ELECTRON MICROSCOPY
EM experiment
Aggregation state: FILAMENT / 3D reconstruction method: helical reconstruction
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