A single amino acid substitution within the transmembrane domain of the human immunodeficiency virus type 1 Vpu protein renders simian-human immunodeficiency virus (SHIV(KU-1bMC33)) susceptible to rimantadine

Virology. 2006 May 10;348(2):449-61. doi: 10.1016/j.virol.2005.12.025. Epub 2006 Feb 3.

Abstract

Previous studies from our laboratory have shown that the transmembrane domain (TM) of the Vpu protein of human immunodeficiency virus type 1 (HIV-1) contributes to the pathogenesis of SHIV(KU-1bMC33) in macaques and that the TM domain of Vpu could be replaced with the M2 protein viroporin from influenza A virus. Recently, we showed that the replacement of the TM domain of Vpu with that of the M2 protein of influenza A virus resulted in a virus (SHIV(M2)) that was sensitive to rimantadine [Hout, D.R., Gomez, M.L., Pacyniak, E., Gomez, L.M., Inbody, S.H., Mulcahy, E.R., Culley, N., Pinson, D.M., Powers, M.F., Wong, S.W., Stephens, E.B., 2006. Substitution of the transmembrane domain of Vpu in simian human immunodeficiency virus (SHIV(KU-1bMC33)) with that of M2 of influenza A results in a virus that is sensitive to inhibitors of the M2 ion channel and is pathogenic for pig-tailed macaques. Virology 344, 541-558]. Based on previous studies of the M2 protein which have shown that the His-X-X-X-Trp motif within the M2 is essential to the function of the M2 proton channel, we have constructed a novel SHIV in which the alanine at position 19 of the TM domain was replaced with a histidine residue resulting in the motif His-Ile-Leu-Val-Trp. The SHIV(VpuA19H) replicated with similar kinetics as the parental SHIV(KU-1bMC33) and pulse-chase analysis revealed that the processing of viral proteins was similar to SHIV(KU-1bMC33). This SHIV(VpuA19H) virus was found to be more sensitive to the M2 ion channel blocker rimantadine than SHIV(M2). Electron microscopic examination of SHIV(VpuA19H)-infected cells treated with rimantadine revealed an accumulation of viral particles at the cell surface and within intracellular vesicles, which was similar to that previously observed to SHIV(M2)-infected cells treated with rimantadine. These data indicate that the Vpu protein of HIV-1 can be converted into a rimantadine-sensitive ion channel with the alteration of one amino acid and provide additional evidence that drugs targeting the Vpu TM/ion channel can be effective anti-HIV-1 drugs.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Amino Acid Sequence
  • Amino Acid Substitution
  • Animals
  • Anti-HIV Agents / pharmacology*
  • Base Sequence
  • Biological Transport, Active
  • CD4 Antigens / metabolism
  • DNA, Viral / genetics
  • Drug Resistance, Viral / genetics
  • Genes, vpu
  • HIV-1 / chemistry
  • HIV-1 / drug effects*
  • HIV-1 / genetics*
  • HeLa Cells
  • Human Immunodeficiency Virus Proteins
  • Humans
  • Hybridization, Genetic
  • Ion Channels / chemistry
  • Ion Channels / genetics
  • Ion Channels / metabolism
  • Microscopy, Electron
  • Molecular Sequence Data
  • Protein Structure, Tertiary
  • Rimantadine / pharmacology*
  • Simian Immunodeficiency Virus / chemistry
  • Simian Immunodeficiency Virus / drug effects*
  • Simian Immunodeficiency Virus / genetics*
  • Viral Matrix Proteins / chemistry
  • Viral Matrix Proteins / genetics
  • Viral Regulatory and Accessory Proteins / chemistry*
  • Viral Regulatory and Accessory Proteins / genetics*
  • Viral Regulatory and Accessory Proteins / metabolism

Substances

  • Anti-HIV Agents
  • CD4 Antigens
  • DNA, Viral
  • Human Immunodeficiency Virus Proteins
  • Ion Channels
  • M2 protein, Influenza A virus
  • Viral Matrix Proteins
  • Viral Regulatory and Accessory Proteins
  • vpu protein, Human immunodeficiency virus 1
  • Rimantadine