Genetic Analysis of the Localization of APOBEC3F to Human Immunodeficiency Virus Type 1 Virion Cores

Donahue, John P.; Levinson, Rebecca T.; Sheehan, Jonathan H.; Sutton, Lorraine; Taylor, Harry E.; Meiler, Jens; D’Aquila, Richard T.; Cao, Song

doi:10.1128/jvi.01981-14

Cited by 5 publications

(6 citation statements)

References 55 publications

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“…This step of the restriction mechanism is evidenced by chimeric A3 enzymes and amino acid substitution mutants that package, but somehow fail to breach the core and inhibit viral infectivity (Donahue et al, 2015; Haché et al, 2005; Song et al, 2012). Upon receptor binding and fusion, the conical capsid is deposited in the cytosol of a target cells, reverse transcription occurs concomitant with RNase H activity to degrade template viral genomic RNA, and single-stranded viral cDNA becomes susceptible to the mutagenic activity of an encapsidated A3 enzyme.…”

Section: Human Apobec3 Enzymes and Hiv Restrictionmentioning

confidence: 99%

APOBECs and virus restriction

2015

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The APOBEC family of single-stranded DNA cytosine deaminases comprises a formidable arm of the vertebrate innate immune system. Pre-vertebrates express a single APOBEC, whereas some mammals produce as many as eleven enzymes. The APOBEC3 subfamily displays both copy number variation and polymorphisms, consistent with ongoing pathogenic pressures. These enzymes restrict the replication of many DNA-based parasites, such as exogenous viruses and endogenous transposable elements. APOBEC1 and activation-induced cytosine deaminase (AID) have specialized functions in RNA editing and antibody gene diversification, respectively, whereas APOBEC2 and APOBEC4 appear to have different functions. Nevertheless, the APOBEC family protects against both periodic viral zoonoses as well as exogenous and endogenous parasite replication. This review highlights viral pathogens that are restricted by APOBEC enzymes, but manage to escape through unique mechanisms. The sensitivity of viruses that lack counterdefense measures highlights the need to develop APOBEC-enabling small molecules as a new class of anti-viral drugs.

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Section: Human Apobec3 Enzymes and Hiv Restrictionmentioning

confidence: 99%

APOBECs and virus restriction

2015

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“…Studies have proven that cytoplasmic A3D, A3F, A3G, and A3H can be encapsidated in virions budding from HIV-producing cells and that this decreases infectivity of those virions. [7][8][9][10][11][12][13][14][15] Levels of those A3s in the cytoplasm that enable this incorporation into virions are higher in some T lymphocyte and myeloid cell differentiation states. 16,17 HIV infectivity is decreased more if virions are produced from specific types of T lymphocytes with relatively up-regulated cytoplasmic A3s, in comparison to those produced from T lymphocytes with lower levels of cytoplasmic A3s.…”

Section: Introductionmentioning

confidence: 99%

The von Hippel–Lindau Cullin-RING E3 ubiquitin ligase regulates APOBEC3 cytidine deaminases

Scholtés

Sawyer

Vaca

et al. 2021

Translational Research

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This is a PDF file of an article that has undergone enhancements after acceptance, such as the addition of a cover page and metadata, and formatting for readability, but it is not yet the definitive version of record. This version will undergo additional copyediting, typesetting and review before it is published in its final form, but we are providing this version to give early visibility of the article. Please note that, during the production process, errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain.

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“…The incorporation/encapsidation into HIV virions, which is mainly mediated through RNA binding by the A3 proteins, requires both CD1 and CD2 domains of A3F, whereas only CD1 of A3G is needed 32; 34; 35; 36; 37; 38; 39 . On the other hand, while HIV Vif targets A3G for E3 ubiquitin ligase mediated degradation through binding to the CD1 of A3G, Vif targets A3F by binding to its CD2 domain 25; 26; 40; 41; 42; 43.…”

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confidence: 99%

The in vitro Biochemical Characterization of an HIV-1 Restriction Factor APOBEC3F: Importance of Loop 7 on Both CD1 and CD2 for DNA Binding and Deamination

Chen

Xiao

Wolfe

et al. 2016

Journal of Molecular Biology

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APOBEC3F (A3F) is a member of the apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like (APOBEC) family of proteins that can deaminate cytosine (C) to uracil (U) on nucleic acids. A3F is one of the four APOBEC members with two Zn-coordinated homologous cytosine deaminase domains (CD), with the others being A3G, A3D, and A3B. Here we report the in vitro characterization of DNA binding and deaminase activities using purified wild type (wt) and various mutant proteins of A3F from an E. coli expression system. We show that, even though CD1 is catalytically inactive and CD2 is the active deaminase domain, presence of CD1 on the N-terminus of CD2 enhances the deaminase activity by over an order of magnitude. This enhancement of CD2 catalytic activity is mainly through the increase of substrate ssDNA binding by the N-terminal CD1 domain. We further show that the loop 7 of both CD1 and CD2 of A3F plays an important role for ssDNA binding for each individual domain, as well as for the deaminase activity of CD2 domain in the full length A3F.

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Genetic Analysis of the Localization of APOBEC3F to Human Immunodeficiency Virus Type 1 Virion Cores

Cited by 5 publications

References 55 publications

APOBECs and virus restriction

APOBECs and virus restriction

The von Hippel–Lindau Cullin-RING E3 ubiquitin ligase regulates APOBEC3 cytidine deaminases

The in vitro Biochemical Characterization of an HIV-1 Restriction Factor APOBEC3F: Importance of Loop 7 on Both CD1 and CD2 for DNA Binding and Deamination

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