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Biological Chemistry

ACS Meeting News: Hepatitis B virus protein contains unusual iron-sulfur cluster

by Jyllian Kemsley
April 5, 2017

HBV protein X likely incorporates an iron-sulfur cluster that interconverts between a [2Fe2S] and a [4Fe4S] form, although ligands bound to the cluster have not yet been identified.
Credit: Maria Eirini Pandelia/Brandeis U

In a step toward understanding how the hepatitis B virus (HBV) replicates and causes infection, a research team has determined that one of the virus’s four proteins may incorporate a unique iron-sulfur cluster. Team leader Maria Eirini Pandelia of Brandeis University reported this discovery on Tuesday at the American Chemical Society national meeting in San Francisco.

The protein, known simply as X, is only 154 amino acids long and is the least understood of the HBV proteins. HBV infects the liver and can cause short-term and chronic illness.

Biochemists know that X interacts with a number of proteins in host cells and that it plays a role in virus infectivity, replication, and ultimately cancer formation. However, the protein’s structure and mechanism have remained elusive.

Pandelia’s team started investigating X last year, after work by another group indicated that the protein incorporates iron. Elemental and spectroscopic analysis by Pandelia and colleagues show that the protein contains a [2Fe2S] cluster when isolated in the presence of oxygen. When reduced, the cluster converts to [4Fe4S], although exactly how the conversion occurs is unclear.

Other proteins known to interconvert between forms containing [2Fe2S] and [4Fe4S] play roles in iron-sulfur cluster assembly and gene transcription regulation

Research keeps revealing more about the diversity and importance of iron-sulfur clusters in biological chemistry, commented one of the symposium organizers, Joshua Telser of Roosevelt University. “It’s never-ending.”

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