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TitleFunctional redundancy revealed by the deletion of the mimivirus GMC-oxidoreductase genes.
Journal, issue, pagesMicrolife, Vol. 5, Page uqae006, Year 2024
Publish dateApr 5, 2024
AuthorsJean-Marie Alempic / Hugo Bisio / Alejandro Villalta / Sébastien Santini / Audrey Lartigue / Alain Schmitt / Claire Bugnot / Anna Notaro / Lucid Belmudes / Annie Adrait / Olivier Poirot / Denis Ptchelkine / Cristina De Castro / Yohann Couté / Chantal Abergel /
PubMed AbstractThe 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 ...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 , suggesting this may be the major evolutionary force behind their giant genomes.
External linksMicrolife / PubMed:38659623 / PubMed Central
MethodsEM (helical sym.)
Resolution4.2 - 4.3 Å
Structure data

17125

8orh

EMDB-17125, PDB-8orh:
Knockout of GMC-oxidoreductase genes reveals that functional redundancy preserves mimivirus essential functions
Method: EM (helical sym.) / Resolution: 4.2 Å

17131

8ors

EMDB-17131, PDB-8ors:
Knockout of GMC-oxidoreductase genes reveals that functional redundancy preserves mimivirus essential functions
Method: EM (helical sym.) / Resolution: 4.3 Å

Chemicals

ChemComp-FAD:
FLAVIN-ADENINE DINUCLEOTIDE / FAD*YM / Flavin adenine dinucleotide

Source
  • mimivirus reunion
KeywordsSTRUCTURAL PROTEIN / GMC-oxidoreductase / genomic fiber / mimivirus

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