Human APOBEC3 induced mutation of human immunodeficiency virus type-1 contributes to adaptation and evolution in natural infection.

Human APOBEC3 proteins are cytidine deaminases that contribute broadly to innate immunity through the control of exogenous retrovirus replication and endogenous retroelement retrotransposition. As an intrinsic antiretroviral defense mechanism, APOBEC3 proteins induce extensive guanosine-to-adenosine...

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Autores principales:	Eun-Young Kim, Ramon Lorenzo-Redondo, Susan J Little, Yoon-Seok Chung, Prabhjeet K Phalora, Irina Maljkovic Berry, John Archer, Sudhir Penugonda, Will Fischer, Douglas D Richman, Tanmoy Bhattacharya, Michael H Malim, Steven M Wolinsky
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2014
Materias:	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/370d1a339d744cdda8e3f55d1c1c4c79
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spelling	oai:doaj.org-article:370d1a339d744cdda8e3f55d1c1c4c792021-11-25T05:46:13ZHuman APOBEC3 induced mutation of human immunodeficiency virus type-1 contributes to adaptation and evolution in natural infection.1553-73661553-737410.1371/journal.ppat.1004281https://doaj.org/article/370d1a339d744cdda8e3f55d1c1c4c792014-07-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/25080100/pdf/?tool=EBIhttps://doaj.org/toc/1553-7366https://doaj.org/toc/1553-7374Human APOBEC3 proteins are cytidine deaminases that contribute broadly to innate immunity through the control of exogenous retrovirus replication and endogenous retroelement retrotransposition. As an intrinsic antiretroviral defense mechanism, APOBEC3 proteins induce extensive guanosine-to-adenosine (G-to-A) mutagenesis and inhibit synthesis of nascent human immunodeficiency virus-type 1 (HIV-1) cDNA. Human APOBEC3 proteins have additionally been proposed to induce infrequent, potentially non-lethal G-to-A mutations that make subtle contributions to sequence diversification of the viral genome and adaptation though acquisition of beneficial mutations. Using single-cycle HIV-1 infections in culture and highly parallel DNA sequencing, we defined trinucleotide contexts of the edited sites for APOBEC3D, APOBEC3F, APOBEC3G, and APOBEC3H. We then compared these APOBEC3 editing contexts with the patterns of G-to-A mutations in HIV-1 DNA in cells obtained sequentially from ten patients with primary HIV-1 infection. Viral substitutions were highest in the preferred trinucleotide contexts of the edited sites for the APOBEC3 deaminases. Consistent with the effects of immune selection, amino acid changes accumulated at the APOBEC3 editing contexts located within human leukocyte antigen (HLA)-appropriate epitopes that are known or predicted to enable peptide binding. Thus, APOBEC3 activity may induce mutations that influence the genetic diversity and adaptation of the HIV-1 population in natural infection.Eun-Young KimRamon Lorenzo-RedondoSusan J LittleYoon-Seok ChungPrabhjeet K PhaloraIrina Maljkovic BerryJohn ArcherSudhir PenugondaWill FischerDouglas D RichmanTanmoy BhattacharyaMichael H MalimSteven M WolinskyPublic Library of Science (PLoS)articleImmunologic diseases. AllergyRC581-607Biology (General)QH301-705.5ENPLoS Pathogens, Vol 10, Iss 7, p e1004281 (2014)
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 Eun-Young Kim Ramon Lorenzo-Redondo Susan J Little Yoon-Seok Chung Prabhjeet K Phalora Irina Maljkovic Berry John Archer Sudhir Penugonda Will Fischer Douglas D Richman Tanmoy Bhattacharya Michael H Malim Steven M Wolinsky Human APOBEC3 induced mutation of human immunodeficiency virus type-1 contributes to adaptation and evolution in natural infection.
description	Human APOBEC3 proteins are cytidine deaminases that contribute broadly to innate immunity through the control of exogenous retrovirus replication and endogenous retroelement retrotransposition. As an intrinsic antiretroviral defense mechanism, APOBEC3 proteins induce extensive guanosine-to-adenosine (G-to-A) mutagenesis and inhibit synthesis of nascent human immunodeficiency virus-type 1 (HIV-1) cDNA. Human APOBEC3 proteins have additionally been proposed to induce infrequent, potentially non-lethal G-to-A mutations that make subtle contributions to sequence diversification of the viral genome and adaptation though acquisition of beneficial mutations. Using single-cycle HIV-1 infections in culture and highly parallel DNA sequencing, we defined trinucleotide contexts of the edited sites for APOBEC3D, APOBEC3F, APOBEC3G, and APOBEC3H. We then compared these APOBEC3 editing contexts with the patterns of G-to-A mutations in HIV-1 DNA in cells obtained sequentially from ten patients with primary HIV-1 infection. Viral substitutions were highest in the preferred trinucleotide contexts of the edited sites for the APOBEC3 deaminases. Consistent with the effects of immune selection, amino acid changes accumulated at the APOBEC3 editing contexts located within human leukocyte antigen (HLA)-appropriate epitopes that are known or predicted to enable peptide binding. Thus, APOBEC3 activity may induce mutations that influence the genetic diversity and adaptation of the HIV-1 population in natural infection.
format	article
author	Eun-Young Kim Ramon Lorenzo-Redondo Susan J Little Yoon-Seok Chung Prabhjeet K Phalora Irina Maljkovic Berry John Archer Sudhir Penugonda Will Fischer Douglas D Richman Tanmoy Bhattacharya Michael H Malim Steven M Wolinsky
author_facet	Eun-Young Kim Ramon Lorenzo-Redondo Susan J Little Yoon-Seok Chung Prabhjeet K Phalora Irina Maljkovic Berry John Archer Sudhir Penugonda Will Fischer Douglas D Richman Tanmoy Bhattacharya Michael H Malim Steven M Wolinsky
author_sort	Eun-Young Kim
title	Human APOBEC3 induced mutation of human immunodeficiency virus type-1 contributes to adaptation and evolution in natural infection.
title_short	Human APOBEC3 induced mutation of human immunodeficiency virus type-1 contributes to adaptation and evolution in natural infection.
title_full	Human APOBEC3 induced mutation of human immunodeficiency virus type-1 contributes to adaptation and evolution in natural infection.
title_fullStr	Human APOBEC3 induced mutation of human immunodeficiency virus type-1 contributes to adaptation and evolution in natural infection.
title_full_unstemmed	Human APOBEC3 induced mutation of human immunodeficiency virus type-1 contributes to adaptation and evolution in natural infection.
title_sort	human apobec3 induced mutation of human immunodeficiency virus type-1 contributes to adaptation and evolution in natural infection.
publisher	Public Library of Science (PLoS)
publishDate	2014
url	https://doaj.org/article/370d1a339d744cdda8e3f55d1c1c4c79
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Human APOBEC3 induced mutation of human immunodeficiency virus type-1 contributes to adaptation and evolution in natural infection.

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