Introduction of H2C2-type zinc-binding residues into HIV-2 Vpr increases its expression level

Ryoko Koga; Minami Yamamoto; Halil Ibrahim Ciftci; Masami Otsuka; Mikako Fujita

doi:10.1002/2211-5463.12358

Introduction of H2C2-type zinc-binding residues into HIV-2 Vpr increases its expression level

FEBS Open Bio. 2017 Dec 19;8(1):146-153. doi: 10.1002/2211-5463.12358. eCollection 2018 Jan.

Authors

Ryoko Koga¹, Minami Yamamoto¹, Halil Ibrahim Ciftci¹, Masami Otsuka¹, Mikako Fujita²

Affiliations

¹ Department of Bioorganic Medicinal Chemistry Faculty of Life Sciences Kumamoto University Japan.
² Research Institute for Drug Discovery School of Pharmacy Kumamoto University Japan.

Abstract

Human immunodeficiency virus type 2 has two structurally similar proteins, Vpx and Vpr. Vpx degrades the host anti-viral protein SAMHD1 and is expressed at high levels, while Vpr is responsible for cell cycle arrest and is expressed at much lower levels. We constructed a Vpr mutant with a high level of expression by replacing the amino acids HHCR/HHCH with a putative H2C2-type zinc-binding site that is carried by Vpx. Our finding suggests that during the evolution of Vpr and Vpx, zinc-binding likely became a mechanism for regulating their expression levels.

Keywords: HIV‐2; Vpr; Vpx; cysteine; protein expression; zinc.