Proteomics

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Mass spectrometry-based proteomic analysis of virions and fibrils from Mimiviridae

ABSTRACT: Mimivirus 1.2Mb genome is organized into a 30 nm nucleocapsid-like structure made of two closely related GMC-oxidoreductases, also composing the fibrils decorating its virions. In this work, we used MS-proteomics to characterize the protein content of virions and fibrils from different members of the Mimiviridae family (clade A: Mimivirus reunion -Mr- and Mimivirus M4 -M4, clade B: Moumouvirus australiensis -Ma- and Moumouvirus maliensis -Mm, clade C: Megavirus chilensis -Mc- and Megavirus vitis -Mv). Furthermore, we analyzed fractions purified from Mr mutants devoid of one of the two GMC-oxidoreductases (Mr_KOqu_143 and Mr_KOqu_946), or of both GMC-oxidoreductases (Mr_2KO) with or without expression of the GFP fused to the N-terminus of one GMC-oxidoreductase (Mr_2KO-GFP). Our results show the versatility of the protein content of the fibrils, with fibrils composed of different proteins inter- and even intra-clade, clades B and C viruses presenting fibrils with a protein composition closer to each other than that of clade A viruses.

INSTRUMENT(S): Q Exactive HF, Q Exactive

ORGANISM(S): Mimivirus Acanthamoeba Castellanii

SUBMITTER: Yohann Couté  

LAB HEAD: Yohann Couté

PROVIDER: PXD041298 | Pride | 2024-06-16

REPOSITORIES: Pride

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Dataset's files

Source:
Action DRS
M4_Fibrils.mgf Mgf
M4_Fibrils.raw Raw
M4_Results.mzid.gz Mzid
M4_Virion.mgf Mgf
M4_Virion.raw Raw
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Publications

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 fibril  ...[more]

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