Cargando…

Structural Features of Antiviral APOBEC3 Proteins are Linked to Their Functional Activities

Human APOBEC3 (A3) proteins are cellular cytidine deaminases that potently restrict the replication of retroviruses by hypermutating viral cDNA and/or inhibiting reverse transcription. There are seven members of this family including A3A, B, C, DE, F, G, and H, all encoded in a tandem array on human...

Descripción completa

Detalles Bibliográficos
Autores principales: Kitamura, Shingo, Ode, Hirotaka, Iwatani, Yasumasa
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Research Foundation 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3243911/
https://www.ncbi.nlm.nih.gov/pubmed/22203821
http://dx.doi.org/10.3389/fmicb.2011.00258
_version_ 1782219704618713088
author Kitamura, Shingo
Ode, Hirotaka
Iwatani, Yasumasa
author_facet Kitamura, Shingo
Ode, Hirotaka
Iwatani, Yasumasa
author_sort Kitamura, Shingo
collection PubMed
description Human APOBEC3 (A3) proteins are cellular cytidine deaminases that potently restrict the replication of retroviruses by hypermutating viral cDNA and/or inhibiting reverse transcription. There are seven members of this family including A3A, B, C, DE, F, G, and H, all encoded in a tandem array on human chromosome 22. A3F and A3G are the most potent inhibitors of HIV-1, but only in the absence of the virus-encoded protein, Vif. HIV-1 utilizes Vif to abrogate A3 functions in the producer cells. More specifically, Vif, serving as a substrate receptor, facilitates ubiquitination of A3 proteins by forming a Cullin5 (Cul5)-based E3 ubiquitin ligase complex, which targets A3 proteins for rapid proteasomal degradation. The specificity of A3 degradation is determined by the ability of Vif to bind to the target. Several lines of evidence have suggested that three distinct regions of A3 proteins are involved in the interaction with Vif. Here, we review the biological functions of A3 family members with special focus on A3G and base our analysis on the available structural information.
format Online
Article
Text
id pubmed-3243911
institution National Center for Biotechnology Information
language English
publishDate 2011
publisher Frontiers Research Foundation
record_format MEDLINE/PubMed
spelling pubmed-32439112011-12-27 Structural Features of Antiviral APOBEC3 Proteins are Linked to Their Functional Activities Kitamura, Shingo Ode, Hirotaka Iwatani, Yasumasa Front Microbiol Microbiology Human APOBEC3 (A3) proteins are cellular cytidine deaminases that potently restrict the replication of retroviruses by hypermutating viral cDNA and/or inhibiting reverse transcription. There are seven members of this family including A3A, B, C, DE, F, G, and H, all encoded in a tandem array on human chromosome 22. A3F and A3G are the most potent inhibitors of HIV-1, but only in the absence of the virus-encoded protein, Vif. HIV-1 utilizes Vif to abrogate A3 functions in the producer cells. More specifically, Vif, serving as a substrate receptor, facilitates ubiquitination of A3 proteins by forming a Cullin5 (Cul5)-based E3 ubiquitin ligase complex, which targets A3 proteins for rapid proteasomal degradation. The specificity of A3 degradation is determined by the ability of Vif to bind to the target. Several lines of evidence have suggested that three distinct regions of A3 proteins are involved in the interaction with Vif. Here, we review the biological functions of A3 family members with special focus on A3G and base our analysis on the available structural information. Frontiers Research Foundation 2011-12-21 /pmc/articles/PMC3243911/ /pubmed/22203821 http://dx.doi.org/10.3389/fmicb.2011.00258 Text en Copyright © 2011 Kitamura, Ode and Iwatani. http://www.frontiersin.org/licenseagreement This is an open-access article distributed under the terms of the Creative Commons Attribution Non Commercial License, which permits non-commercial use, distribution, and reproduction in other forums, provided the original authors and source are credited.
spellingShingle Microbiology
Kitamura, Shingo
Ode, Hirotaka
Iwatani, Yasumasa
Structural Features of Antiviral APOBEC3 Proteins are Linked to Their Functional Activities
title Structural Features of Antiviral APOBEC3 Proteins are Linked to Their Functional Activities
title_full Structural Features of Antiviral APOBEC3 Proteins are Linked to Their Functional Activities
title_fullStr Structural Features of Antiviral APOBEC3 Proteins are Linked to Their Functional Activities
title_full_unstemmed Structural Features of Antiviral APOBEC3 Proteins are Linked to Their Functional Activities
title_short Structural Features of Antiviral APOBEC3 Proteins are Linked to Their Functional Activities
title_sort structural features of antiviral apobec3 proteins are linked to their functional activities
topic Microbiology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3243911/
https://www.ncbi.nlm.nih.gov/pubmed/22203821
http://dx.doi.org/10.3389/fmicb.2011.00258
work_keys_str_mv AT kitamurashingo structuralfeaturesofantiviralapobec3proteinsarelinkedtotheirfunctionalactivities
AT odehirotaka structuralfeaturesofantiviralapobec3proteinsarelinkedtotheirfunctionalactivities
AT iwataniyasumasa structuralfeaturesofantiviralapobec3proteinsarelinkedtotheirfunctionalactivities