ArticlemicroLife2024
Functional redundancy revealed by the deletion of the mimivirus GMC-oxidoreductase genes.
Article in microLife, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 13 citations in OpenAlex.
- Vicennial metagenomic time series unveils evolutionary dynamics of giant viruses in a freshwater ecosystem.Nature communications · 2026Article
- Elucidating the protein interaction network of one of the largest icosahedral capsids in the virosphere.The EMBO journal · 2026Article
- A newly isolated giant virus, ushikuvirus, is closely related to clandestinovirus and shows a unique capsid surface structure and host cell interactions.Journal of virology · 2025Article
- HyperdCas12a-based multiplexed genetic regulation in Candida albicans.Nucleic acids research · 2025Article
- Evolutionarily conserved grammar rules viral factories of amoeba-infecting members of the hyperdiverseProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Melbournevirus encodes a shorter H2B-H2A doublet histone variant that forms structurally distinct nucleosome structures.Nature communications · 2025Article
- Cellular souvenirs in viral luggage.Nature reviews. Microbiology · 2025Article
- 20 years of research on giant viruses.Npj viruses · 2025Review
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Authors and funding
15 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The mimivirus 1.2 Mb genome was shown to be organized into a nucleocapsid-like genomic fiber encased in the nucleoid compartment inside the icosahedral capsid. The genomic fiber protein shell is composed of a mixture of two GMC-oxidoreductase paralogs, one of them being the main component of the glycosylated layer of fibrils at the surface of the virion. In this study, we determined the effect of the deletion of each of the corresponding genes on the genomic fiber and the layer of surface fibrils. First, we deleted the GMC-oxidoreductase, the most abundant in the genomic fiber, and determined its structure and composition in the mutant. As expected, it was composed of the second GMC-oxidoreductase and contained 5- and 6-start helices similar to the wild-type fiber. This result led us to propose a model explaining their coexistence. Then we deleted the GMC-oxidoreductase, the most abundant in the layer of fibrils, to analyze its protein composition in the mutant. Second, we showed that the fitness of single mutants and the double mutant were not decreased compared with the wild-type viruses under laboratory conditions. Third, we determined that deleting the GMC-oxidoreductase genes did not impact the glycosylation or the glycan composition of the layer of surface fibrils, despite modifying their protein composition. Because the glycosylation machinery and glycan composition of members of different clades are different, we expanded the analysis of the protein composition of the layer of fibrils to members of the B and C clades and showed that it was different among the three clades and even among isolates within the same clade. Taken together, the results obtained on two distinct central processes (genome packaging and virion coating) illustrate an unexpected functional redundancy in members of the family
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