A triple-arginine motif in the amino-terminal domain and oligomerization are required for HIV-1 inhibition by human MX2

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Abstract

We have employed molecular genetic approaches to understand the domain organization of the HIV-1 resistance factor myxovirus resistance 2 (MX2). First, we describe an essential triple-arginine motif in the amino-terminal domain. Second, we demonstrate that this 91-residue domain mediates antiviral activity when appended to heterologous proteins, and we provide genetic evidence that protein oligomerization is required for MX2 function. These insights will facilitate future work aiming to elucidate MX2's mechanism of action.

Original languageEnglish
Pages (from-to)4676-4680
Number of pages5
JournalJournal of Virology
Volume89
Issue number8
DOIs
Publication statusPublished - 1 Apr 2015

Keywords

  • Amino Acid Motifs
  • Arginine
  • Flow Cytometry
  • Fluorescent Antibody Technique, Indirect
  • HIV-1
  • Humans
  • Immunoblotting
  • Molecular Sequence Data
  • Myxovirus Resistance Proteins
  • Polymerization

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