Human retroviral host restriction factors APOBEC3G and APOBEC3F localize to mRNA processing bodies.

APOBEC3G is an antiviral host factor capable of inhibiting the replication of both exogenous and endogenous retroviruses as well as hepatitis B, a DNA virus that replicates through an RNA intermediate. To gain insight into the mechanism whereby APOBEC3G restricts retroviral replication, we investiga...

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Autores principales:	Michael J Wichroski, G Brett Robb, Tariq M Rana
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2006
Materias:	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/b1b30e356e6b4e8abff026e1079e54d3
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spelling	oai:doaj.org-article:b1b30e356e6b4e8abff026e1079e54d32021-11-25T05:46:24ZHuman retroviral host restriction factors APOBEC3G and APOBEC3F localize to mRNA processing bodies.1553-73661553-737410.1371/journal.ppat.0020041https://doaj.org/article/b1b30e356e6b4e8abff026e1079e54d32006-05-01T00:00:00Zhttps://doi.org/10.1371/journal.ppat.0020041https://doaj.org/toc/1553-7366https://doaj.org/toc/1553-7374APOBEC3G is an antiviral host factor capable of inhibiting the replication of both exogenous and endogenous retroviruses as well as hepatitis B, a DNA virus that replicates through an RNA intermediate. To gain insight into the mechanism whereby APOBEC3G restricts retroviral replication, we investigated the subcellular localization of the protein. Herein, we report that APOBEC3G localizes to mRNA processing (P) bodies, cytoplasmic compartments involved in the degradation and storage of nontranslating mRNAs. Biochemical analysis revealed that APOBEC3G localizes to a ribonucleoprotein complex with other P-body proteins which have established roles in cap-dependent translation (eIF4E and eIF4E-T), translation suppression (RCK/p54), RNA interference-mediated post-transcriptional gene silencing (AGO2), and decapping of mRNA (DCP2). Similar analysis with other APOBEC3 family members revealed a potential link between the localization of APOBEC3G and APOBEC3F to a common ribonucleoprotein complex and P-bodies with potent anti-HIV-1 activity. In addition, we present evidence suggesting that an important role for HIV-1 Vif, which subverts both APOBEC3G and APOBEC3F antiviral function by inducing their degradation, could be to selectively remove these proteins from and/or restrict their localization to P-bodies. Taken together, the results of this study reveal a novel link between innate immunity against retroviruses and P-bodies suggesting that APOBEC3G and APOBEC3F could function in the context of P-bodies to restrict HIV-1 replication.Michael J WichroskiG Brett RobbTariq M RanaPublic Library of Science (PLoS)articleImmunologic diseases. AllergyRC581-607Biology (General)QH301-705.5ENPLoS Pathogens, Vol 2, Iss 5, p e41 (2006)
institution	DOAJ
collection	DOAJ
language	EN
topic	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
spellingShingle	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5 Michael J Wichroski G Brett Robb Tariq M Rana Human retroviral host restriction factors APOBEC3G and APOBEC3F localize to mRNA processing bodies.
description	APOBEC3G is an antiviral host factor capable of inhibiting the replication of both exogenous and endogenous retroviruses as well as hepatitis B, a DNA virus that replicates through an RNA intermediate. To gain insight into the mechanism whereby APOBEC3G restricts retroviral replication, we investigated the subcellular localization of the protein. Herein, we report that APOBEC3G localizes to mRNA processing (P) bodies, cytoplasmic compartments involved in the degradation and storage of nontranslating mRNAs. Biochemical analysis revealed that APOBEC3G localizes to a ribonucleoprotein complex with other P-body proteins which have established roles in cap-dependent translation (eIF4E and eIF4E-T), translation suppression (RCK/p54), RNA interference-mediated post-transcriptional gene silencing (AGO2), and decapping of mRNA (DCP2). Similar analysis with other APOBEC3 family members revealed a potential link between the localization of APOBEC3G and APOBEC3F to a common ribonucleoprotein complex and P-bodies with potent anti-HIV-1 activity. In addition, we present evidence suggesting that an important role for HIV-1 Vif, which subverts both APOBEC3G and APOBEC3F antiviral function by inducing their degradation, could be to selectively remove these proteins from and/or restrict their localization to P-bodies. Taken together, the results of this study reveal a novel link between innate immunity against retroviruses and P-bodies suggesting that APOBEC3G and APOBEC3F could function in the context of P-bodies to restrict HIV-1 replication.
format	article
author	Michael J Wichroski G Brett Robb Tariq M Rana
author_facet	Michael J Wichroski G Brett Robb Tariq M Rana
author_sort	Michael J Wichroski
title	Human retroviral host restriction factors APOBEC3G and APOBEC3F localize to mRNA processing bodies.
title_short	Human retroviral host restriction factors APOBEC3G and APOBEC3F localize to mRNA processing bodies.
title_full	Human retroviral host restriction factors APOBEC3G and APOBEC3F localize to mRNA processing bodies.
title_fullStr	Human retroviral host restriction factors APOBEC3G and APOBEC3F localize to mRNA processing bodies.
title_full_unstemmed	Human retroviral host restriction factors APOBEC3G and APOBEC3F localize to mRNA processing bodies.
title_sort	human retroviral host restriction factors apobec3g and apobec3f localize to mrna processing bodies.
publisher	Public Library of Science (PLoS)
publishDate	2006
url	https://doaj.org/article/b1b30e356e6b4e8abff026e1079e54d3
work_keys_str_mv	AT michaeljwichroski humanretroviralhostrestrictionfactorsapobec3gandapobec3flocalizetomrnaprocessingbodies AT gbrettrobb humanretroviralhostrestrictionfactorsapobec3gandapobec3flocalizetomrnaprocessingbodies AT tariqmrana humanretroviralhostrestrictionfactorsapobec3gandapobec3flocalizetomrnaprocessingbodies
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Human retroviral host restriction factors APOBEC3G and APOBEC3F localize to mRNA processing bodies.

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