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

Caroline Goujon; Rebecca A Greenbury; Stelios Papaioannou; Tomas Doyle; Michael H Malim

doi:10.1128/JVI.00169-15

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

Caroline Goujon, Rebecca A Greenbury, Stelios Papaioannou, Tomas Doyle, Michael H Malim

Infectious Diseases

Research output: Contribution to journal › Article › peer-review

52 Citations (Scopus)

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 language	English
Pages (from-to)	4676-4680
Number of pages	5
Journal	Journal of Virology
Volume	89
Issue number	8
DOIs	https://doi.org/10.1128/JVI.00169-15
Publication status	Published - 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

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1128/JVI.00169-15

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

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.",

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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doi = "10.1128/JVI.00169-15",

language = "English",

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T1 - A triple-arginine motif in the amino-terminal domain and oligomerization are required for HIV-1 inhibition by human MX2

AU - Goujon, Caroline

AU - Greenbury, Rebecca A

AU - Papaioannou, Stelios

AU - Doyle, Tomas

AU - Malim, Michael H

PY - 2015/4/1

Y1 - 2015/4/1

N2 - 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.

AB - 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.

KW - Amino Acid Motifs

KW - Arginine

KW - Flow Cytometry

KW - Fluorescent Antibody Technique, Indirect

KW - HIV-1

KW - Humans

KW - Immunoblotting

KW - Molecular Sequence Data

KW - Myxovirus Resistance Proteins

KW - Polymerization

U2 - 10.1128/JVI.00169-15

DO - 10.1128/JVI.00169-15

M3 - Article

C2 - 25673704

SN - 0022-538X

VL - 89

SP - 4676

EP - 4680

JO - Journal of Virology

JF - Journal of Virology

IS - 8

ER -

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

Abstract

Keywords

UN SDGs

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