| APOBEC3F Is a Mutational Driver of the Human Monkeypox Virus Identified in the 2022 Outbreak. | APOBEC3F Is a Mutational Driver of the Human Monkeypox Virus Identified in the 2022 Outbreak.
Suspène R, Raymond KA, Boutin L, Guillier S, Lemoine F, Ferraris O, Tournier JN, Iseni F, Simon-Lorière E, Vartanian JP., Free PMC Article | 11/16/2023 |
| Stability of APOBEC3F in the Presence of the APOBEC3 Antagonist HIV-1 Vif Increases at the Expense of Co-Expressed APOBEC3H Haplotype I. | Stability of APOBEC3F in the Presence of the APOBEC3 Antagonist HIV-1 Vif Increases at the Expense of Co-Expressed APOBEC3H Haplotype I.
Yousefi M, Annan Sudarsan AK, Gaba A, Chelico L., Free PMC Article | 03/7/2023 |
| Differential Activity of APOBEC3F, APOBEC3G, and APOBEC3H in the Restriction of HIV-2. | Differential Activity of APOBEC3F, APOBEC3G, and APOBEC3H in the Restriction of HIV-2.
Meissner ME, Willkomm NA, Lucas J, Arndt WG, Aitken SF, Julik EJ, Baliga S, Mansky LM., Free PMC Article | 02/5/2022 |
| analysis of the dependence of the deamination rate of human APOBEC3F on the length of single-stranded DNA, which is affected by the concentrations of APOBEC3F and single-stranded DNA | An insight into the dependence of the deamination rate of human APOBEC3F on the length of single-stranded DNA, which is affected by the concentrations of APOBEC3F and single-stranded DNA.
Wan L, Kamba K, Nagata T, Katahira M. | 07/18/2020 |
| The cryo-EM structure of the Vif-targeted C-terminal domain of human A3F in complex with HIV-1 Vif and the cellular cofactor core-binding factor beta (CBFbeta) at 3.9-A resolution shows that Vif and CBFbeta form a platform to recruit A3F, revealing a direct A3F-recruiting role of CBFbeta beyond Vif stabilization, and it captures multiple independent A3F-Vif interfaces. | Structural basis of antagonism of human APOBEC3F by HIV-1 Vif.
Hu Y, Desimmie BA, Nguyen HC, Ziegler SJ, Cheng TC, Chen J, Wang J, Wang H, Zhang K, Pathak VK, Xiong Y., Free PMC Article | 02/15/2020 |
| Apolipoprotein B mRNA editing enzyme catalytic subunit 3F (A3F) polymorphism A3F 231V restrict HIV-1 infection more efficiently than A3F 231 and is partially protected from Vif-mediated degradation. A3F 231V induces more mutations than A3F 231I in HIV-1 proviral DNA. A3F genotypes are commonly heterozygous. Hetero-oligomerization with A3F 231V results in partial stabilization of A3F 231I and A3G in the presence of Vif. | Polymorphisms of the cytidine deaminase APOBEC3F have different HIV-1 restriction efficiencies.
Mohammadzadeh N, Follack TB, Love RP, Stewart K, Sanche S, Chelico L. | 03/9/2019 |
| APOBEC3DE binds to itself, APOBEC3F, and APOBEC3G and antagonizes APOBEC3F and, to a lesser extent, APOBEC3G restriction of hepatitis B virus replication. | APOBEC3DE Antagonizes Hepatitis B Virus Restriction Factors APOBEC3F and APOBEC3G.
Bouzidi MS, Caval V, Suspène R, Hallez C, Pineau P, Wain-Hobson S, Vartanian JP. | 06/24/2017 |
| These results indicate that APOBEC3 proteins can be copackaged and can comutate the same genomes, and can cooperate to inhibit HIV replication. | APOBEC3 proteins can copackage and comutate HIV-1 genomes.
Desimmie BA, Burdick RC, Izumi T, Doi H, Shao W, Alvord WG, Sato K, Koyanagi Y, Jones S, Wilson E, Hill S, Maldarelli F, Hu WS, Pathak VK., Free PMC Article | 06/24/2017 |
| an APOBEC3F/APOBEC3G hetero-oligomer can form that has unique properties compared to each APOBEC3 alone. This hetero-oligomer has increased efficiency of virus hypermutation, raising the idea that we still may not fully realize the antiviral mechanisms of endogenous APOBEC3 enzymes. Hetero-oligomerization may be a mechanism to increase their antiviral activity in the presence of Vif. | Mechanism of Enhanced HIV Restriction by Virion Coencapsidated Cytidine Deaminases APOBEC3F and APOBEC3G.
Ara A, Love RP, Follack TB, Ahmed KA, Adolph MB, Chelico L., Free PMC Article | 05/20/2017 |
| virus adaptation and computational studies to interrogate the APOBEC3F-Vif interface and build a robust structural model; taken together with mutagenesis results, propose a wobble model to explain how HIV-1 Vif has evolved to bind different APOBEC3 enzymes | The Binding Interface between Human APOBEC3F and HIV-1 Vif Elucidated by Genetic and Computational Approaches.
Richards C, Albin JS, Demir Ö, Shaban NM, Luengas EM, Land AM, Anderson BD, Holten JR, Anderson JS, Harki DA, Amaro RE, Harris RS., Free PMC Article | 01/28/2017 |
| Findings support a role for APOBEC3G/F proteins in the generation of plasma drug-resistant minority human immunodeficiency virus type 1 variants (DRMVs). However, this role seems to be limited to a small subset of mutations and does not explain most of the DRMVs evaluated. | Contribution of APOBEC3G/F activity to the development of low-abundance drug-resistant human immunodeficiency virus type 1 variants.
Noguera-Julian M, Cozzi-Lepri A, Di Giallonardo F, Schuurman R, Däumer M, Aitken S, Ceccherini-Silberstein F, D'Arminio Monforte A, Geretti AM, Booth CL, Kaiser R, Michalik C, Jansen K, Masquelier B, Bellecave P, Kouyos RD, Castro E, Furrer H, Schultze A, Günthard HF, Brun-Vezinet F, Metzner KJ, Paredes R, CHAIN Minority HIV-1 Variants Working group. | 11/5/2016 |
| Overexpression of APOBEC3F in tumor tissues is potentially predictive for poor recurrence-free survival from hepatitis b virus-hepatocellular carcinoma patients. | Overexpression of APOBEC3F in tumor tissues is potentially predictive for poor recurrence-free survival from HBV-related hepatocellular carcinoma.
Yang Z, Zhuang L, Yu Y, Zhou W, Lu Y, Xu Q, Tang B, Chen X. | 10/22/2016 |
| Our results provide genetic epidemiological evidence that A3F(APOBEC3F ) modulates HIV-1/AIDS disease progression | Role of APOBEC3F Gene Variation in HIV-1 Disease Progression and Pneumocystis Pneumonia.
An P, Penugonda S, Thorball CW, Bartha I, Goedert JJ, Donfield S, Buchbinder S, Binns-Roemer E, Kirk GD, Zhang W, Fellay J, Yu XF, Winkler CA., Free PMC Article | 08/6/2016 |
| Six residues located within the conserved HIV-1 Vif F1-, F2-, and F3-box motifs are essential for both APOBEC3C and APOBEC3F degradation, and an additional four residues are uniquely required for APOBEC3F degradation. | Structural Insights into HIV-1 Vif-APOBEC3F Interaction.
Nakashima M, Ode H, Kawamura T, Kitamura S, Naganawa Y, Awazu H, Tsuzuki S, Matsuoka K, Nemoto M, Hachiya A, Sugiura W, Yokomaku Y, Watanabe N, Iwatani Y., Free PMC Article | 05/14/2016 |
| This study showed for the first time a high level of APOBEC3F/3G editing in HIV-2 sequences from antiretroviral-naive patients. | High level of APOBEC3F/3G editing in HIV-2 DNA vif and pol sequences from antiretroviral-naive patients.
Bertine M, Charpentier C, Visseaux B, Storto A, Collin G, Larrouy L, Damond F, Matheron S, Brun-Vézinet F, Descamps D, ANRS CO5 HIV-2 Cohort. | 02/6/2016 |
| APOBEC3D/F and APOBEC3G fundamentally work as restriction factors against HIV-1 in vivo | APOBEC3D and APOBEC3F potently promote HIV-1 diversification and evolution in humanized mouse model.
Sato K, Takeuchi JS, Misawa N, Izumi T, Kobayashi T, Kimura Y, Iwami S, Takaori-Kondo A, Hu WS, Aihara K, Ito M, An DS, Pathak VK, Koyanagi Y., Free PMC Article | 12/19/2015 |
| APOBEC3G is more efficient at mutating retroviral DNA than APOBEC3F. | Comparative analysis of the gene-inactivating potential of retroviral restriction factors APOBEC3F and APOBEC3G.
Bélanger K, Langlois MA. | 12/19/2015 |
| A3G and A3F inhibit porcine endogenous retrovirus replication. | Differential sensitivity of porcine endogenous retrovirus to APOBEC3-mediated inhibition.
Park SH, Kim JH, Jung YT. | 10/31/2015 |
| The rather indiscriminate RNA binding characteristics of A3G and A3F promote functionality by enabling recruitment into a wide range of retroviral particles whose packaged RNA genomes comprise divergent sequences. | Promiscuous RNA binding ensures effective encapsidation of APOBEC3 proteins by HIV-1.
Apolonia L, Schulz R, Curk T, Rocha P, Swanson CM, Schaller T, Ule J, Malim MH., Free PMC Article | 10/10/2015 |
| The nucleocapsid domain of HIV-1 Gag and a linker sequence between the two cytidine deaminase domains are required for viral packaging of APOBEC3F. | Human APOBEC3F incorporation into human immunodeficiency virus type 1 particles.
Wang X, Li X, Ma J, Zhang L, Ma L, Mi Z, Zhou J, Guo F, Kleiman L, Cen S. | 06/6/2015 |
| Authors found that one pair of leucines in each of APOBEC3F's C-terminal and N-terminal cytidine deaminase domains jointly determined the degree of localization of APOBEC3F into HIV-1 virion cores. | Genetic analysis of the localization of APOBEC3F to human immunodeficiency virus type 1 virion cores.
Donahue JP, Levinson RT, Sheehan JH, Sutton L, Taylor HE, Meiler J, D'Aquila RT, Song C., Free PMC Article | 04/11/2015 |
| This approach identified the alpha3 and alpha4 helices of human APOBEC3F as important determinants of the interaction with HIV-1 Vif. | APOBEC3F determinants of HIV-1 Vif sensitivity.
Land AM, Shaban NM, Evans L, Hultquist JF, Albin JS, Harris RS., Free PMC Article | 02/21/2015 |
| APOBEC3G/F mutational hotspots in the human immunodeficiency virus genome have roles in reducing recognition by CD8+ T cells | Positioning of APOBEC3G/F mutational hotspots in the human immunodeficiency virus genome favors reduced recognition by CD8+ T cells.
Monajemi M, Woodworth CF, Zipperlen K, Gallant M, Grant MD, Larijani M., Free PMC Article | 01/17/2015 |
| Authors found that APOBEA3G, APOBEA3F, and APOBEA3H-hapII, but not APOBEA3D, were susceptible to HIV-2 Vif-induced degradation. | HIV-1 and HIV-2 Vif interact with human APOBEC3 proteins using completely different determinants.
Smith JL, Izumi T, Borbet TC, Hagedorn AN, Pathak VK., Free PMC Article | 12/20/2014 |
| we demonstrate key differences in the impact of APOBEC3F- and APOBEC3G-induced mutagenesis on HIV-1 | Different mutagenic potential of HIV-1 restriction factors APOBEC3G and APOBEC3F is determined by distinct single-stranded DNA scanning mechanisms.
Ara A, Love RP, Chelico L., Free PMC Article | 11/8/2014 |