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Mimosine inhibits viral DNA synthesis through ribonucleotide reductase

Y Dai1, B Gold, J K Vishwanatha

  • 1Eppley Institute, Omaha, Nebraska.

Virology
|November 15, 1994
PubMed

Insights

Mimosine, a plant amino acid, inhibits viral DNA synthesis by chelating iron, essential for ribonucleotide reductase. This effect is reversible with iron, impacting viral replication.

Area of Science:

  • Biochemistry
  • Virology
  • Molecular Biology

Background:

  • Mimosine is a plant amino acid known for its toxicity to animals and its ability to inhibit animal cell replication.
  • Mimosine's effects on viral replication were not fully understood, prompting further investigation into its mechanism of action.

Purpose of the Study:

  • To investigate the effect of mimosine on the DNA synthesis of various DNA viruses.
  • To elucidate the mechanism by which mimosine inhibits viral DNA synthesis and replication.

Main Methods:

  • Assessing mimosine's impact on the replication of adenovirus, parvovirus, papovavirus, vaccinia virus, and herpes simplex virus 1 in cell cultures.
  • Evaluating mimosine's effect on SV40 DNA replication in a cell-free system.
  • Measuring the levels of deoxynucleotide triphosphates (dGTP and dATP) in mimosine-treated cells.
  • Testing mimosine's inhibitory activity on purified ribonucleotide reductase in vitro.

Main Results:

  • Mimosine inhibited the DNA synthesis of multiple DNA viruses and the replication of vaccinia and herpes simplex virus 1 in cultured cells.
  • Mimosine did not inhibit SV40 DNA replication in a cell-free system.
  • The inhibitory effect of mimosine on viral DNA synthesis was reversed by the addition of iron.
  • Mimosine treatment led to reduced intracellular pools of dGTP and dATP.
  • Mimosine demonstrated iron-dependent inhibition of ribonucleotide reductase activity in vitro.

Conclusions:

  • Mimosine inhibits viral DNA synthesis by targeting the enzyme ribonucleotide reductase.
  • The mechanism involves mimosine's iron-chelating properties, which interfere with the iron cofactor in the R2 subunit of ribonucleotide reductase.
  • This inhibition affects the availability of essential deoxynucleotides for viral DNA replication.

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