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A Rapid Strategy for the Isolation of New Faustoviruses from Environmental Samples Using Vermamoeba vermiformis
Published on: June 4, 2016
The giant mimivirus 1.2 Mb genome is elegantly organized into a 30-nm diameter helical protein shield
Alejandro Villalta1, Alain Schmitt1, Leandro F Estrozi2
1Aix-Marseille University, Centre National de la Recherche Scientifique, Information Génomique & Structurale, Unité Mixte de Recherche 7256 (Institut de Microbiologie de la Méditerranée, FR3479, IM2B), Marseille, France.
Abstract:
Mimivirus is the prototype of the Mimiviridae family of giant dsDNA viruses. Little is known about the organization of the 1.2 Mb genome inside the membrane-limited nucleoid filling the ~0.5 µm icosahedral capsids. Cryo-electron microscopy, cryo-electron tomography, and proteomics revealed that it is encased into a ~30-nm diameter helical protein shell surprisingly composed of two GMC-type oxidoreductases, which also form the glycosylated fibrils decorating the capsid. The genome is arranged in 5- or 6-start left-handed super-helices, with each DNA-strand lining the central channel. This luminal channel of the nucleoprotein fiber is wide enough to accommodate oxidative stress proteins and RNA polymerase subunits identified by proteomics. Such elegant supramolecular organization would represent a remarkable evolutionary strategy for packaging and protecting the genome, in a state ready for immediate transcription upon unwinding in the host cytoplasm. The parsimonious use of the same protein in two unrelated substructures of the virion is unexpected for a giant virus with thousand genes at its disposal.
Insights
Mimivirus giant viruses package their DNA genome within a unique helical protein shell made of oxidoreductases. This structure protects the genome and primes it for transcription upon host entry.
Area of Science:
- Virology
- Structural Biology
- Genomics
Background:
- Mimivirus, a giant dsDNA virus, has a large genome (1.2 Mb) housed within an icosahedral capsid.
- The internal organization and packaging of the Mimivirus genome remain poorly understood.
Purpose of the Study:
- To elucidate the supramolecular organization of the Mimivirus genome and its protective shell.
- To investigate the protein composition and structural arrangement of the viral nucleoid.
Main Methods:
- Cryo-electron microscopy (cryo-EM)
- Cryo-electron tomography (cryo-ET)
- Proteomics analysis
Main Results:
- The Mimivirus genome is organized into left-handed super-helices within the capsid.
- A ~30-nm diameter helical protein shell, composed of GMC-type oxidoreductases, encases the genome.
- These oxidoreductases also form the glycosylated capsid fibrils.
- The genome's central channel accommodates oxidative stress proteins and RNA polymerase subunits.
Conclusions:
- Mimivirus employs an efficient genome packaging strategy using a single protein type for both the internal shell and external fibrils.
- This organization facilitates rapid genome transcription upon release into the host cytoplasm.
- The findings offer insights into viral evolution and genome management in giant viruses.
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