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The antiviral protein viperin is a radical SAM enzyme.


ABSTRACT: Viperin, an interferon-inducible antiviral protein, is shown to bind an iron-sulfur cluster, based on iron analysis as well as UV-Vis and electron paramagnetic resonance spectroscopic data. The reduced protein contains a [4Fe-4S](1+) cluster whose g-values are altered upon addition of S-adenosylmethionine (SAM), consistent with SAM coordination to the cluster. Incubation of reduced viperin with SAM results in reductive cleavage of SAM to produce 5'-deoxyadenosine (5'-dAdo), a reaction characteristic of the radical SAM superfamily. The 5'-dAdo cleavage product was identified by a combination of HPLC and mass spectrometry analysis.

SUBMITTER: Duschene KS 

PROVIDER: S-EPMC3149979 | biostudies-literature | 2010 Mar

REPOSITORIES: biostudies-literature

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The antiviral protein viperin is a radical SAM enzyme.

Duschene Kaitlin S KS   Broderick Joan B JB  

FEBS letters 20100220 6


Viperin, an interferon-inducible antiviral protein, is shown to bind an iron-sulfur cluster, based on iron analysis as well as UV-Vis and electron paramagnetic resonance spectroscopic data. The reduced protein contains a [4Fe-4S](1+) cluster whose g-values are altered upon addition of S-adenosylmethionine (SAM), consistent with SAM coordination to the cluster. Incubation of reduced viperin with SAM results in reductive cleavage of SAM to produce 5'-deoxyadenosine (5'-dAdo), a reaction characteri  ...[more]

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