Inhibition of hepadnavirus reverse transcriptase-ε RNA interaction by porphyrin compounds

Li Lin, Jianming Hu

Research output: Contribution to journalArticlepeer-review

39 Scopus citations

Abstract

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 ε. As RT-ε 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.

Original languageEnglish (US)
Pages (from-to)2305-2312
Number of pages8
JournalJournal of virology
Volume82
Issue number5
DOIs
StatePublished - Mar 2008

All Science Journal Classification (ASJC) codes

  • Microbiology
  • Immunology
  • Insect Science
  • Virology

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