Assay and functional analysis of dynamin-like Mx proteins

Georg Kochs; Mike Reichelt; Dganit Danino; Jenny E. Hinshaw; Otto Haller

doi:10.1016/S0076-6879(05)04055-3

Assay and functional analysis of dynamin-like Mx proteins

Georg Kochs^*, Mike Reichelt, Dganit Danino, Jenny E. Hinshaw, Otto Haller

^*Corresponding author for this work

Research output: Contribution to journal › Review article › peer-review

35 Scopus citations

Abstract

Mx proteins are interferon-induced large guanosin triphosphatases (GTPases) that share structural and functional properties with dynamin and dynamin-like proteins, such as self-assembly and association with intracellular membranes. A unique property of some Mx proteins is their antiviral activity against a range of RNA viruses, including influenza viruses and members of the bunyavirus family. These viruses are inhibited at an early stage in their life cycle, soon after host cell entry and before genome amplification. The association of the human MxA GTPase with membranes of the endoplasmic reticulum seems to support its antiviral function by providing an interaction platform that facilitates viral target recognition, MxA oligomerization, and missorting of the resulting multiprotein complex into large intracellular aggregates.

Original language	English
Article number	55
Pages (from-to)	632-643
Number of pages	12
Journal	Methods in Enzymology
Volume	404
DOIs	https://doi.org/10.1016/S0076-6879(05)04055-3
State	Published - 2005
Externally published	Yes

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10.1016/S0076-6879(05)04055-3

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title = "Assay and functional analysis of dynamin-like Mx proteins",

abstract = "Mx proteins are interferon-induced large guanosin triphosphatases (GTPases) that share structural and functional properties with dynamin and dynamin-like proteins, such as self-assembly and association with intracellular membranes. A unique property of some Mx proteins is their antiviral activity against a range of RNA viruses, including influenza viruses and members of the bunyavirus family. These viruses are inhibited at an early stage in their life cycle, soon after host cell entry and before genome amplification. The association of the human MxA GTPase with membranes of the endoplasmic reticulum seems to support its antiviral function by providing an interaction platform that facilitates viral target recognition, MxA oligomerization, and missorting of the resulting multiprotein complex into large intracellular aggregates.",

author = "Georg Kochs and Mike Reichelt and Dganit Danino and Hinshaw, {Jenny E.} and Otto Haller",

year = "2005",

doi = "10.1016/S0076-6879(05)04055-3",

language = "英语",

volume = "404",

pages = "632--643",

journal = "Methods in Enzymology",

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T1 - Assay and functional analysis of dynamin-like Mx proteins

AU - Kochs, Georg

AU - Reichelt, Mike

AU - Danino, Dganit

AU - Hinshaw, Jenny E.

AU - Haller, Otto

PY - 2005

Y1 - 2005

N2 - Mx proteins are interferon-induced large guanosin triphosphatases (GTPases) that share structural and functional properties with dynamin and dynamin-like proteins, such as self-assembly and association with intracellular membranes. A unique property of some Mx proteins is their antiviral activity against a range of RNA viruses, including influenza viruses and members of the bunyavirus family. These viruses are inhibited at an early stage in their life cycle, soon after host cell entry and before genome amplification. The association of the human MxA GTPase with membranes of the endoplasmic reticulum seems to support its antiviral function by providing an interaction platform that facilitates viral target recognition, MxA oligomerization, and missorting of the resulting multiprotein complex into large intracellular aggregates.

AB - Mx proteins are interferon-induced large guanosin triphosphatases (GTPases) that share structural and functional properties with dynamin and dynamin-like proteins, such as self-assembly and association with intracellular membranes. A unique property of some Mx proteins is their antiviral activity against a range of RNA viruses, including influenza viruses and members of the bunyavirus family. These viruses are inhibited at an early stage in their life cycle, soon after host cell entry and before genome amplification. The association of the human MxA GTPase with membranes of the endoplasmic reticulum seems to support its antiviral function by providing an interaction platform that facilitates viral target recognition, MxA oligomerization, and missorting of the resulting multiprotein complex into large intracellular aggregates.

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U2 - 10.1016/S0076-6879(05)04055-3

DO - 10.1016/S0076-6879(05)04055-3

M3 - 文献综述

C2 - 16413306

AN - SCOPUS:30544451047

SN - 0076-6879

VL - 404

SP - 632

EP - 643

JO - Methods in Enzymology

JF - Methods in Enzymology

M1 - 55

ER -

Assay and functional analysis of dynamin-like Mx proteins

Abstract

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