Counteraction of the multifunctional restriction factor tetherin
The interferon-inducible restriction factor tetherin (also known as CD317, BST-2 or HM1.24) has emerged as a key component of the antiviral immune response. Initially, tetherin was shown to restrict replication of various enveloped viruses by inhibiting the release of budding virions from infected c...
| Main Author: | |
|---|---|
| Format: | Online |
| Language: | English |
| Published: |
Frontiers Media S.A.
2014
|
| Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3989765/ |
| id |
pubmed-3989765 |
|---|---|
| recordtype |
oai_dc |
| spelling |
pubmed-39897652014-04-29 Counteraction of the multifunctional restriction factor tetherin Sauter, Daniel Microbiology The interferon-inducible restriction factor tetherin (also known as CD317, BST-2 or HM1.24) has emerged as a key component of the antiviral immune response. Initially, tetherin was shown to restrict replication of various enveloped viruses by inhibiting the release of budding virions from infected cells. More recently, it has become clear that tetherin also acts as a pattern recognition receptor inducing NF-κB-dependent proinflammatory gene expression in virus infected cells. Whereas the ability to restrict virion release is highly conserved among mammalian tetherin orthologs and thus probably an ancient function of this protein, innate sensing seems to be an evolutionarily recent activity. The potent and broad antiviral activity of tetherin is reflected by the fact that many viruses evolved means to counteract this restriction factor. A continuous arms race with viruses has apparently driven the evolution of different isoforms of tetherin with different functional properties. Interestingly, tetherin has also been implicated in cellular processes that are unrelated to immunity, such as the organization of the apical actin network and membrane microdomains or stabilization of the Golgi apparatus. In this review, I summarize our current knowledge of the different functions of tetherin and describe the molecular strategies that viruses have evolved to antagonize or evade this multifunctional host restriction factor. Frontiers Media S.A. 2014-04-10 /pmc/articles/PMC3989765/ /pubmed/24782851 http://dx.doi.org/10.3389/fmicb.2014.00163 Text en Copyright © 2014 Sauter. http://creativecommons.org/licenses/by/3.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
| repository_type |
Open Access Journal |
| institution_category |
Foreign Institution |
| institution |
US National Center for Biotechnology Information |
| building |
NCBI PubMed |
| collection |
Online Access |
| language |
English |
| format |
Online |
| author |
Sauter, Daniel |
| spellingShingle |
Sauter, Daniel Counteraction of the multifunctional restriction factor tetherin |
| author_facet |
Sauter, Daniel |
| author_sort |
Sauter, Daniel |
| title |
Counteraction of the multifunctional restriction factor tetherin |
| title_short |
Counteraction of the multifunctional restriction factor tetherin |
| title_full |
Counteraction of the multifunctional restriction factor tetherin |
| title_fullStr |
Counteraction of the multifunctional restriction factor tetherin |
| title_full_unstemmed |
Counteraction of the multifunctional restriction factor tetherin |
| title_sort |
counteraction of the multifunctional restriction factor tetherin |
| description |
The interferon-inducible restriction factor tetherin (also known as CD317, BST-2 or HM1.24) has emerged as a key component of the antiviral immune response. Initially, tetherin was shown to restrict replication of various enveloped viruses by inhibiting the release of budding virions from infected cells. More recently, it has become clear that tetherin also acts as a pattern recognition receptor inducing NF-κB-dependent proinflammatory gene expression in virus infected cells. Whereas the ability to restrict virion release is highly conserved among mammalian tetherin orthologs and thus probably an ancient function of this protein, innate sensing seems to be an evolutionarily recent activity. The potent and broad antiviral activity of tetherin is reflected by the fact that many viruses evolved means to counteract this restriction factor. A continuous arms race with viruses has apparently driven the evolution of different isoforms of tetherin with different functional properties. Interestingly, tetherin has also been implicated in cellular processes that are unrelated to immunity, such as the organization of the apical actin network and membrane microdomains or stabilization of the Golgi apparatus. In this review, I summarize our current knowledge of the different functions of tetherin and describe the molecular strategies that viruses have evolved to antagonize or evade this multifunctional host restriction factor. |
| publisher |
Frontiers Media S.A. |
| publishDate |
2014 |
| url |
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3989765/ |
| _version_ |
1612079114773069824 |