PNAS 1993-10-15

The site of antiviral action of 3-nitrosobenzamide on the infectivity process of human immunodeficiency virus in human lymphocytes.

W G Rice, C A Schaeffer, L Graham, M Bu, J S McDougal, S L Orloff, F Villinger, M Young, S Oroszlan, M R Fesen

Index: Proc. Natl. Acad. Sci. U. S. A. 90 , 9721, (1993)

Full Text: HTML

Abstract

The C-nitroso compound 3-nitrosobenzamide, which has been shown to remove zinc from the retroviral-type zinc finger of p7NC nucleocapsid proteins, inhibits acute infection of human immunodeficiency virus type 1 in cultured human lymphocytes. The attachment of the virus to lymphocytes and the activities of critical viral enzymes, such as reverse transcriptase, protease, and integrase, are not affected by 3-nitrosobenzamide. However, the process of reverse transcription to form proviral DNA is effectively abolished by the drug, identifying the mode of action of 3-nitrosobenzamide as interrupting the role of p7NC in accurate proviral DNA synthesis during the infectious phase of the virus life cycle.

Related Compounds

  • 3-nitrosobenzamide

Related Articles:

Inhibition of the replication of native and 3'-azido-2',3'-dideoxythymidine (AZT)-resistant simian immunodeficiency virus (SIV) by 3-nitrosobenzamide.

1993-07-12

[FEBS Lett. 326 , 140, (1993)]

Structure/function correlations among coupled binuclear copper proteins through spectroscopic and reactivity studies of NspF.

2012-07-03

[Proc. Natl. Acad. Sci. U. S. A. 109(27) , 10793-7, (2012)]

A copper-containing oxidase catalyzes C-nitrosation in nitrosobenzamide biosynthesis.

2010-09-01

[Nat. Chem. Biol. 6(9) , 641-3, (2010)]

Anti-HIV agents that selectively target retroviral nucleocapsid protein zinc fingers without affecting cellular zinc finger proteins.

1998-04-23

[J. Med. Chem. 41(9) , 1371-81, (1998)]

Inhibition of HIV-1 infectivity by zinc-ejecting aromatic C-nitroso compounds.

1993-02-04

[Nature 361 , 473, (1993)]

More Articles...