Critical Role of the Human T-Cell Leukemia Virus Type 1 Capsid N-Terminal Domain for Gag-Gag Interactions and Virus Particle Assembly

Author:

Martin Jessica L.12,Mendonça Luiza M.13,Marusinec Rachel1,Zuczek Jennifer4,Angert Isaac15,Blower Ruth J.13,Mueller Joachim D.15,Perilla Juan R.4,Zhang Wei136,Mansky Louis M.1237ORCID

Affiliation:

1. Institute for Molecular Virology, University of Minnesota, Minneapolis, Minnesota, USA

2. Pharmacology Graduate Program, University of Minnesota, Minneapolis, Minnesota, USA

3. Division of Basic Sciences, School of Dentistry, University of Minnesota, Minneapolis, Minnesota, USA

4. Department of Chemistry & Biochemistry, University of Delaware, Newark, Delaware, USA

5. School of Physics & Astronomy, University of Minnesota, Minneapolis, Minnesota, USA

6. Characterization Facility, University of Minnesota, Minneapolis, Minnesota, USA

7. Masonic Cancer Center, University of Minnesota, Minneapolis, Minnesota, USA

Abstract

Retrovirus particle assembly and release from infected cells is driven by the Gag structural protein. Gag-Gag interactions, which form an oligomeric lattice structure at a particle budding site, are essential to the biogenesis of an infectious virus particle. The CA domain of Gag is generally thought to possess the key determinants for Gag-Gag interactions, and the present study has discovered several critical amino acid residues in the CA domain of HTLV-1 Gag, an important cancer-causing human retrovirus, which are distinct from that of HIV-1 as well as other retroviruses studied to date. Altogether, our results provide important new insights into a poorly understood aspect of HTLV-1 replication that significantly enhances our understanding of the molecular nature of Gag-Gag interaction determinants crucial for virus particle assembly.

Funder

HHS | National Institutes of Health

Publisher

American Society for Microbiology

Subject

Virology,Insect Science,Immunology,Microbiology

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