Moloney leukemia virus 10 (MOV10) inhibits the degradation of APOBEC3G through interference with the Vif-mediated ubiquitin–proteasome pathway
Abstract Background MOV10 protein has ATP-dependent 5′–3′ RNA helicase activity and belongs to the UPF1p superfamily. It can inhibit human immunodeficiency virus type 1 (HIV-1) replication at multiple stages and interact with apolipoprotein-B-mRNA-editing enzyme catalytic polypeptide-like 3G (APOBEC...
Main Authors: | , , , , , , , , , |
---|---|
Format: | Article |
Language: | English |
Published: |
BMC
2017-12-01
|
Series: | Retrovirology |
Subjects: | |
Online Access: | http://link.springer.com/article/10.1186/s12977-017-0382-1 |
id |
doaj-07d3a58695794bae93a4037d03132780 |
---|---|
record_format |
Article |
spelling |
doaj-07d3a58695794bae93a4037d031327802020-11-24T23:24:43ZengBMCRetrovirology1742-46902017-12-0114111910.1186/s12977-017-0382-1Moloney leukemia virus 10 (MOV10) inhibits the degradation of APOBEC3G through interference with the Vif-mediated ubiquitin–proteasome pathwayCancan Chen0Xiaocao Ma1Qifei Hu2Xinghua Li3Feng Huang4Junsong Zhang5Ting Pan6Jinyu Xia7Chao Liu8Hui Zhang9Institute of Human Virology, Zhongshan School of Medicine, Sun Yat-sen UniversityInstitute of Human Virology, Zhongshan School of Medicine, Sun Yat-sen UniversityInstitute of Human Virology, Zhongshan School of Medicine, Sun Yat-sen UniversityDepartment of Infectious Diseases, The Fifth Affiliated Hospital, Sun Yat-sen UniversityInstitute of Human Virology, Zhongshan School of Medicine, Sun Yat-sen UniversityInstitute of Human Virology, Zhongshan School of Medicine, Sun Yat-sen UniversityInstitute of Human Virology, Zhongshan School of Medicine, Sun Yat-sen UniversityDepartment of Infectious Diseases, The Fifth Affiliated Hospital, Sun Yat-sen UniversityInstitute of Human Virology, Zhongshan School of Medicine, Sun Yat-sen UniversityInstitute of Human Virology, Zhongshan School of Medicine, Sun Yat-sen UniversityAbstract Background MOV10 protein has ATP-dependent 5′–3′ RNA helicase activity and belongs to the UPF1p superfamily. It can inhibit human immunodeficiency virus type 1 (HIV-1) replication at multiple stages and interact with apolipoprotein-B-mRNA-editing enzyme catalytic polypeptide-like 3G (APOBEC3G or A3G), a member of the cytidine deaminase family that exerts potent inhibitory effects against HIV-1 infection. However, HIV-1-encoded virion infectivity factor (Vif) protein specifically mediates the degradation of A3G via the ubiquitin–proteasome system (UPS). Results We demonstrate that MOV10 counteracts Vif-mediated degradation of A3G by inhibiting the assembly of the Vif-CBF-β-Cullin 5-ElonginB-ElonginC complex. Through interference with UPS, MOV10 enhances the level of A3G in HIV-1-infected cells and virions, and synergistically inhibits the replication and infectivity of HIV-1. In addition, the DEAG-box of MOV10 is required for inhibition of Vif-mediated A3G degradation as the DEAG-box mutant significantly loses this ability. Conclusions Our results demonstrate a novel mechanism involved in the anti-HIV-1 function of MOV10. Given that both MOV10 and A3G belong to the interferon antiviral system, their synergistic inhibition of HIV-1 suggests that these proteins may play complicated roles in antiviral functions.http://link.springer.com/article/10.1186/s12977-017-0382-1MOV10A3GVifHIV-1Ubiquitin–proteasome system (UPS) |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Cancan Chen Xiaocao Ma Qifei Hu Xinghua Li Feng Huang Junsong Zhang Ting Pan Jinyu Xia Chao Liu Hui Zhang |
spellingShingle |
Cancan Chen Xiaocao Ma Qifei Hu Xinghua Li Feng Huang Junsong Zhang Ting Pan Jinyu Xia Chao Liu Hui Zhang Moloney leukemia virus 10 (MOV10) inhibits the degradation of APOBEC3G through interference with the Vif-mediated ubiquitin–proteasome pathway Retrovirology MOV10 A3G Vif HIV-1 Ubiquitin–proteasome system (UPS) |
author_facet |
Cancan Chen Xiaocao Ma Qifei Hu Xinghua Li Feng Huang Junsong Zhang Ting Pan Jinyu Xia Chao Liu Hui Zhang |
author_sort |
Cancan Chen |
title |
Moloney leukemia virus 10 (MOV10) inhibits the degradation of APOBEC3G through interference with the Vif-mediated ubiquitin–proteasome pathway |
title_short |
Moloney leukemia virus 10 (MOV10) inhibits the degradation of APOBEC3G through interference with the Vif-mediated ubiquitin–proteasome pathway |
title_full |
Moloney leukemia virus 10 (MOV10) inhibits the degradation of APOBEC3G through interference with the Vif-mediated ubiquitin–proteasome pathway |
title_fullStr |
Moloney leukemia virus 10 (MOV10) inhibits the degradation of APOBEC3G through interference with the Vif-mediated ubiquitin–proteasome pathway |
title_full_unstemmed |
Moloney leukemia virus 10 (MOV10) inhibits the degradation of APOBEC3G through interference with the Vif-mediated ubiquitin–proteasome pathway |
title_sort |
moloney leukemia virus 10 (mov10) inhibits the degradation of apobec3g through interference with the vif-mediated ubiquitin–proteasome pathway |
publisher |
BMC |
series |
Retrovirology |
issn |
1742-4690 |
publishDate |
2017-12-01 |
description |
Abstract Background MOV10 protein has ATP-dependent 5′–3′ RNA helicase activity and belongs to the UPF1p superfamily. It can inhibit human immunodeficiency virus type 1 (HIV-1) replication at multiple stages and interact with apolipoprotein-B-mRNA-editing enzyme catalytic polypeptide-like 3G (APOBEC3G or A3G), a member of the cytidine deaminase family that exerts potent inhibitory effects against HIV-1 infection. However, HIV-1-encoded virion infectivity factor (Vif) protein specifically mediates the degradation of A3G via the ubiquitin–proteasome system (UPS). Results We demonstrate that MOV10 counteracts Vif-mediated degradation of A3G by inhibiting the assembly of the Vif-CBF-β-Cullin 5-ElonginB-ElonginC complex. Through interference with UPS, MOV10 enhances the level of A3G in HIV-1-infected cells and virions, and synergistically inhibits the replication and infectivity of HIV-1. In addition, the DEAG-box of MOV10 is required for inhibition of Vif-mediated A3G degradation as the DEAG-box mutant significantly loses this ability. Conclusions Our results demonstrate a novel mechanism involved in the anti-HIV-1 function of MOV10. Given that both MOV10 and A3G belong to the interferon antiviral system, their synergistic inhibition of HIV-1 suggests that these proteins may play complicated roles in antiviral functions. |
topic |
MOV10 A3G Vif HIV-1 Ubiquitin–proteasome system (UPS) |
url |
http://link.springer.com/article/10.1186/s12977-017-0382-1 |
work_keys_str_mv |
AT cancanchen moloneyleukemiavirus10mov10inhibitsthedegradationofapobec3gthroughinterferencewiththevifmediatedubiquitinproteasomepathway AT xiaocaoma moloneyleukemiavirus10mov10inhibitsthedegradationofapobec3gthroughinterferencewiththevifmediatedubiquitinproteasomepathway AT qifeihu moloneyleukemiavirus10mov10inhibitsthedegradationofapobec3gthroughinterferencewiththevifmediatedubiquitinproteasomepathway AT xinghuali moloneyleukemiavirus10mov10inhibitsthedegradationofapobec3gthroughinterferencewiththevifmediatedubiquitinproteasomepathway AT fenghuang moloneyleukemiavirus10mov10inhibitsthedegradationofapobec3gthroughinterferencewiththevifmediatedubiquitinproteasomepathway AT junsongzhang moloneyleukemiavirus10mov10inhibitsthedegradationofapobec3gthroughinterferencewiththevifmediatedubiquitinproteasomepathway AT tingpan moloneyleukemiavirus10mov10inhibitsthedegradationofapobec3gthroughinterferencewiththevifmediatedubiquitinproteasomepathway AT jinyuxia moloneyleukemiavirus10mov10inhibitsthedegradationofapobec3gthroughinterferencewiththevifmediatedubiquitinproteasomepathway AT chaoliu moloneyleukemiavirus10mov10inhibitsthedegradationofapobec3gthroughinterferencewiththevifmediatedubiquitinproteasomepathway AT huizhang moloneyleukemiavirus10mov10inhibitsthedegradationofapobec3gthroughinterferencewiththevifmediatedubiquitinproteasomepathway |
_version_ |
1725559184243556352 |