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Preliminary crystallographic analysis of the Megavirus superoxide dismutase.

ABSTRACT: Megavirus chilensis, a close relative of the Mimivirus giant virus, is able to replicate in Acanthamoeba castellanii. The first step of viral infection involves the internalization of the virions in host vacuoles. It has been experimentally demonstrated that Mimivirus particles contain many proteins capable of resisting oxidative stress, as encountered in the phagocytic process. These proteins are conserved in Megavirus, which has an additional gene (Mg277) encoding a putative superoxide dismutase. The Mg277 ORF product was overexpressed in Escherichia coli, purified and crystallized. A SAD data set was collected to 2.24?Å resolution at the selenium peak wavelength on the BM30 beamline at the ESRF from a single crystal of selenomethionine-substituted recombinant superoxide dismutase protein.

SUBMITTER: Lartigue A

PROVIDER: S-EPMC3509988 | biostudies-other | 2012 Dec

REPOSITORIES: biostudies-other

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Preliminary crystallographic analysis of the Megavirus superoxide dismutase.

Lartigue Audrey A Philippe Nadège N Jeudy Sandra S Abergel Chantal C

Acta crystallographica. Section F, Structural biology and crystallization communications 20121128 Pt 12

Megavirus chilensis, a close relative of the Mimivirus giant virus, is able to replicate in Acanthamoeba castellanii. The first step of viral infection involves the internalization of the virions in host vacuoles. It has been experimentally demonstrated that Mimivirus particles contain many proteins capable of resisting oxidative stress, as encountered in the phagocytic process. These proteins are conserved in Megavirus, which has an additional gene (Mg277) encoding a putative superoxide dismuta ...[more]

PMID: 23192047

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