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Journal of Virology, March 2008, p. 2305-2312, Vol. 82, No. 5
0022-538X/08/$08.00+0     doi:10.1128/JVI.02147-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Inhibition of Hepadnavirus Reverse Transcriptase-{varepsilon} RNA Interaction by Porphyrin Compounds{triangledown}

Li Lin and Jianming Hu*

Department of Microbiology and Immunology, College of Medicine, Pennsylvania State University, Hershey, Pennsylvania 17033

Received 29 September 2007/ Accepted 10 December 2007

The hepatitis B virus (HBV) reverse transcriptase (RT) plays a multitude of fundamental roles in the viral life cycle and is the key target in the development of anti-HBV chemotherapy. We report here that the endogenous small molecule iron protoporphyrin IX (hemin) and several related porphyrin compounds potently blocked a critical RT interaction with the viral RNA packaging signal/origin of replication, called {varepsilon}. As RT-{varepsilon} interaction is essential for the initiation of viral reverse transcription, which is primed by RT itself (protein priming), the porphyrin compounds dramatically suppressed the protein-priming reaction. Further studies demonstrated that these compounds could target the unique N-terminal domain of the RT protein, the so-called terminal protein. Hemin and related porphyrin compounds thus represent a novel class of agents that can block HBV RT functions through a mechanism and target that are completely distinct from those of existing anti-HBV drugs.

* Corresponding author. Mailing address: Department of Microbiology and Immunology-H107, Penn State University College of Medicine, 500 University Dr., Hershey, PA 17033. Phone: (717) 531-6523. Fax: (717) 531-6522. E-mail: juh13{at}psu.edu

{triangledown} Published ahead of print on 19 December 2007.

Journal of Virology, March 2008, p. 2305-2312, Vol. 82, No. 5
0022-538X/08/$08.00+0     doi:10.1128/JVI.02147-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



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