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Article
| Open AccessThe structural basis for HIV-1 Vif antagonism of human APOBEC3G
The authors report the cryo-EM structure of human A3G bound to HIV-1 Vif, and the hijacked cellular proteins that promote ubiquitin-mediated proteolysis, suggesting how Vif antagonizes A3G by intercepting it to prevent viral restriction.
- Yen-Li Li
- , Caroline A. Langley
- & John D. Gross
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Letter |
Receptor usage dictates HIV-1 restriction by human TRIM5α in dendritic cell subsets
Human TRIM5α restricts HIV-1 infection of Langerhans cells through Langerin-dependent autophagy pathway.
- Carla M. S. Ribeiro
- , Ramin Sarrami-Forooshani
- & Teunis B. H. Geijtenbeek
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Letter |
Hepatitis B virus X protein identifies the Smc5/6 complex as a host restriction factor
Hepatitis B virus X protein stimulates transcription from the viral DNA episome by hijacking the host ubiquitin machinery to target the Smc5/6 complex for degradation.
- Adrien Decorsière
- , Henrik Mueller
- & Michel Strubin
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Article |
SERINC3 and SERINC5 restrict HIV-1 infectivity and are counteracted by Nef
The transmembrane proteins SERINC3 and SERINC5 are identified as new restriction factors for HIV-1 replication; this restriction is counteracted by Nef and glycoGag, which prevent SERINC3 and SERINC5 from becoming incorporated into HIV-1 virions and from profoundly blocking HIV-1 infectivity, suggesting a potential new therapeutic strategy for immunodeficiency viruses.
- Yoshiko Usami
- , Yuanfei Wu
- & Heinrich G. Göttlinger
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Article |
HIV-1 Nef promotes infection by excluding SERINC5 from virion incorporation
The transmembrane protein SERINC5 is identified as a potent inhibitor of HIV-1 particle infectivity that is counteracted by Nef; Nef redirects SERINC5 from the plasma membrane to a Rab7-positive endosomal compartment, thus excluding it from HIV-1 particles, emphasizing the potential of SERINC5 as a potent anti-retroviral factor.
- Annachiara Rosa
- , Ajit Chande
- & Massimo Pizzato
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Letter |
MX2 is an interferon-induced inhibitor of HIV-1 infection
MX2 is shown to be an interferon-induced inhibitor of HIV-1 infection, and this antiviral activity may involve the inhibition of nuclear import of subviral complexes.
- Melissa Kane
- , Shalini S. Yadav
- & Paul D. Bieniasz