APOBEC3F

Summary

Gene Symbol: APOBEC3F
Description: apolipoprotein B mRNA editing enzyme catalytic subunit 3F
Alias: A3F, ARP8, BK150C2.4.MRNA, KA6, DNA dC->dU-editing enzyme APOBEC-3F, apolipoprotein B editing enzyme catalytic polypeptide-like 3F, apolipoprotein B mRNA editing enzyme cytidine deaminase, apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3F, induced upon T-cell activation
Species: human
Products:     APOBEC3F

Top Publications

  1. Malim M. APOBEC proteins and intrinsic resistance to HIV-1 infection. Philos Trans R Soc Lond B Biol Sci. 2009;364:675-87 pubmed publisher
    Members of the APOBEC family of cellular polynucleotide cytidine deaminases, most notably APOBEC3G and APOBEC3F, are potent inhibitors of HIV-1 infection...
  2. Wichroski M, Robb G, Rana T. Human retroviral host restriction factors APOBEC3G and APOBEC3F localize to mRNA processing bodies. PLoS Pathog. 2006;2:e41 pubmed
    ..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...
  3. Delebecque F, Susp ne R, Calattini S, Casartelli N, Sa b A, Froment A, et al. Restriction of foamy viruses by APOBEC cytidine deaminases. J Virol. 2006;80:605-14 pubmed publisher
    ..APOBEC3G, and viral infectivity was also inhibited by murine and simian APOBEC3G homologues, as well as by human APOBEC3F. Wild-type and bet-deleted viruses were similarly sensitive to this antiviral activity, suggesting that Bet does ..
  4. Zuo T, Liu D, Lv W, Wang X, Wang J, Lv M, et al. Small-molecule inhibition of human immunodeficiency virus type 1 replication by targeting the interaction between Vif and ElonginC. J Virol. 2012;86:5497-507 pubmed publisher
  5. Pace C, Keller J, Nolan D, James I, Gaudieri S, Moore C, et al. Population level analysis of human immunodeficiency virus type 1 hypermutation and its relationship with APOBEC3G and vif genetic variation. J Virol. 2006;80:9259-69 pubmed
    APOBEC3G and APOBEC3F restrict human immunodeficiency virus type 1 (HIV-1) replication in vitro through the induction of G-->A hypermutation; however, the relevance of this host antiviral strategy to clinical HIV-1 is currently not ..
  6. Khatua A, Taylor H, Hildreth J, Popik W. Inhibition of LINE-1 and Alu retrotransposition by exosomes encapsidating APOBEC3G and APOBEC3F. Virology. 2010;400:68-75 pubmed publisher
    Human cytidine deaminases, including APOBEC3G (A3G) and A3F, are part of a cellular defense system against retroviruses and retroelements including non-LTR retrotransposons LINE-1 (L1) and Alu...
  7. Zhou X, Han X, Zhao K, Du J, Evans S, Wang H, et al. Dispersed and conserved hydrophobic residues of HIV-1 Vif are essential for CBF? recruitment and A3G suppression. J Virol. 2014;88:2555-63 pubmed publisher
    ..Therefore, information from this study will help people to further understand how Vif acts against host antiviral mechanism, which is important for novel anti-HIV-1 drug development. ..
  8. Henriet S, Mercenne G, Bernacchi S, Paillart J, Marquet R. Tumultuous relationship between the human immunodeficiency virus type 1 viral infectivity factor (Vif) and the human APOBEC-3G and APOBEC-3F restriction factors. Microbiol Mol Biol Rev. 2009;73:211-32 pubmed publisher
  9. Bohn M, Shandilya S, Albin J, Kouno T, Anderson B, McDougle R, et al. Crystal structure of the DNA cytosine deaminase APOBEC3F: the catalytically active and HIV-1 Vif-binding domain. Structure. 2013;21:1042-50 pubmed publisher
    Human APOBEC3F is an antiretroviral single-strand DNA cytosine deaminase, susceptible to degradation by the HIV-1 protein Vif...

More Information

Publications83

  1. Zhang W, Chen G, Niewiadomska A, Xu R, Yu X. Distinct determinants in HIV-1 Vif and human APOBEC3 proteins are required for the suppression of diverse host anti-viral proteins. PLoS ONE. 2008;3:e3963 pubmed publisher
    ..In the present study, we have demonstrated that the regions of APOBEC3F (A3F) that are required for its HIV-1-mediated binding and degradation are distinct from those reported for A3G...
  2. Fourati S, Malet I, Lambert S, Soulie C, Wirden M, Flandre P, et al. E138K and M184I mutations in HIV-1 reverse transcriptase coemerge as a result of APOBEC3 editing in the absence of drug exposure. AIDS. 2012;26:1619-24 pubmed publisher
    ..Thus, incomplete neutralization of one or more APOBEC3 proteins may favor viral escape to rilpivirine-emtricitabine. ..
  3. Marin M, Golem S, Rose K, Kozak S, Kabat D. Human immunodeficiency virus type 1 Vif functionally interacts with diverse APOBEC3 cytidine deaminases and moves with them between cytoplasmic sites of mRNA metabolism. J Virol. 2008;82:987-98 pubmed
    ..Additionally, Vif(IIIB) less efficiently degrades A3F, another potent anti-HIV-1 cytidine deaminase...
  4. Aguiar R, Peterlin B. APOBEC3 proteins and reverse transcription. Virus Res. 2008;134:74-85 pubmed publisher
    ..Together, these proteins provide strong and immediate intracellular immunity against incoming pathogens and restrict the movement of mobile genetic elements protecting the genome. ..
  5. Matsui Y, Shindo K, Nagata K, Io K, Tada K, Iwai F, et al. Defining HIV-1 Vif residues that interact with CBF? by site-directed mutagenesis. Virology. 2014;449:82-7 pubmed publisher
    ..These results support a model in which HIV-1 Vif residues E88/W89 may participate in binding CBF?. ..
  6. Jónsson S, Haché G, Stenglein M, Fahrenkrug S, Andresdottir V, Harris R. Evolutionarily conserved and non-conserved retrovirus restriction activities of artiodactyl APOBEC3F proteins. Nucleic Acids Res. 2006;34:5683-94 pubmed
    ..Here, we report an APOBEC3F-like, double deaminase domain protein from three artiodactyls: cattle, pigs and sheep...
  7. Refsland E, Hultquist J, Harris R. Endogenous origins of HIV-1 G-to-A hypermutation and restriction in the nonpermissive T cell line CEM2n. PLoS Pathog. 2012;8:e1002800 pubmed publisher
    ..In contrast, APOBEC3F-null cells produced viruses with near-normal mutational patterns...
  8. Miyagi E, Brown C, Opi S, Khan M, Goila Gaur R, Kao S, et al. Stably expressed APOBEC3F has negligible antiviral activity. J Virol. 2010;84:11067-75 pubmed publisher
    b>APOBEC3F (A3F) is a member of the family of cytidine deaminases that is often coexpressed with APOBEC3G (A3G) in cells susceptible to HIV infection...
  9. He Z, Zhang W, Chen G, Xu R, Yu X. Characterization of conserved motifs in HIV-1 Vif required for APOBEC3G and APOBEC3F interaction. J Mol Biol. 2008;381:1000-11 pubmed publisher
    ..or A3G) and related cytidine deaminases such as apolipoprotein B mRNA-editing catalytic polypeptide-like 3F (APOBEC3F, or A3F) are potent inhibitors of retroviruses...
  10. Izumi T, Burdick R, Shigemi M, Plisov S, HU W, Pathak V. Mov10 and APOBEC3G localization to processing bodies is not required for virion incorporation and antiviral activity. J Virol. 2013;87:11047-62 pubmed publisher
  11. Sato K, Izumi T, Misawa N, Kobayashi T, Yamashita Y, Ohmichi M, et al. Remarkable lethal G-to-A mutations in vif-proficient HIV-1 provirus by individual APOBEC3 proteins in humanized mice. J Virol. 2010;84:9546-56 pubmed publisher
    ..Taken together, these results provide the evidence indicating that endogenous APOBEC3s are associated with G-to-A mutation of HIV-1 provirus in vivo, which can result in the abrogation of HIV-1 infection. ..
  12. Holmes R, Malim M, Bishop K. APOBEC-mediated viral restriction: not simply editing?. Trends Biochem Sci. 2007;32:118-28 pubmed
  13. Goila Gaur R, Strebel K. HIV-1 Vif, APOBEC, and intrinsic immunity. Retrovirology. 2008;5:51 pubmed publisher
    ..However, Vif is also able to prevent encapsidation of APOBEC3G and APOBEC3F through degradation-independent mechanism(s)...
  14. Smith J, Bu W, Burdick R, Pathak V. Multiple ways of targeting APOBEC3-virion infectivity factor interactions for anti-HIV-1 drug development. Trends Pharmacol Sci. 2009;30:638-46 pubmed publisher
    ..advances in our understanding of intracellular immunity conferred by host cytidine deaminases APOBEC3G (A3G) and APOBEC3F (A3F) and the mechanism by which the virally encoded virion infectivity factor (Vif) protein induces their ..
  15. Amoedo N, Afonso A, Cunha S, Oliveira R, Machado E, Soares M. Expression of APOBEC3G/3F and G-to-A hypermutation levels in HIV-1-infected children with different profiles of disease progression. PLoS ONE. 2011;6:e24118 pubmed publisher
    Increasing evidence has accumulated showing the role of APOBEC3G (A3G) and 3F (A3F) in the control of HIV-1 replication and disease progression in humans. However, very few studies have been conducted in HIV-infected children...
  16. Pillai S, Abdel Mohsen M, Guatelli J, Skasko M, Monto A, Fujimoto K, et al. Role of retroviral restriction factors in the interferon-?-mediated suppression of HIV-1 in vivo. Proc Natl Acad Sci U S A. 2012;109:3035-40 pubmed publisher
    ..APOBEC3G, APOBEC3F, and BST-2 expression levels were measured in HIV/hepatitis C virus (HCV)-coinfected, antiretroviral therapy-naï..
  17. Russell R, Pathak V. Identification of two distinct human immunodeficiency virus type 1 Vif determinants critical for interactions with human APOBEC3G and APOBEC3F. J Virol. 2007;81:8201-10 pubmed
    Human cytidine deaminases APOBEC3G (A3G) and APOBEC3F (A3F) inhibit replication of Vif-deficient human immunodeficiency virus type 1 (HIV-1)...
  18. Vartanian J, Sommer P, Wain Hobson S. Death and the retrovirus. Trends Mol Med. 2003;9:409-13 pubmed
    ..This death mechanism is circumvented by the HIV viral infectivity factor protein, which prevents APOBEC3G from entering the virion. ..
  19. Hultquist J, Lengyel J, Refsland E, LaRue R, Lackey L, Brown W, et al. Human and rhesus APOBEC3D, APOBEC3F, APOBEC3G, and APOBEC3H demonstrate a conserved capacity to restrict Vif-deficient HIV-1. J Virol. 2011;85:11220-34 pubmed publisher
    ..In addition to APOBEC3G, we find that three other human APOBEC3 proteins, APOBEC3D, APOBEC3F, and APOBEC3H, are all potent HIV-1 restriction factors...
  20. Albin J, LaRue R, Weaver J, Brown W, Shindo K, Harjes E, et al. A single amino acid in human APOBEC3F alters susceptibility to HIV-1 Vif. J Biol Chem. 2010;285:40785-92 pubmed publisher
    Human APOBEC3F (huA3F) potently restricts the infectivity of HIV-1 in the absence of the viral accessory protein virion infectivity factor (Vif)...
  21. Chen H, Lilley C, Yu Q, Lee D, Chou J, Narvaiza I, et al. APOBEC3A is a potent inhibitor of adeno-associated virus and retrotransposons. Curr Biol. 2006;16:480-5 pubmed
    ..They also highlight the functional differences between APOBEC3 proteins. The APOBEC3 family members have distinct functions and may have evolved to resist various classes of genetic elements. ..
  22. Liddament M, Brown W, Schumacher A, Harris R. APOBEC3F properties and hypermutation preferences indicate activity against HIV-1 in vivo. Curr Biol. 2004;14:1385-91 pubmed
    ..g., ). Here, we show that APOBEC3F is also a potent retroviral restrictor but that its activity, unlike that of APOBEC3G, is partially resistant to ..
  23. Dang Y, Wang X, York I, Zheng Y. Identification of a critical T(Q/D/E)x5ADx2(I/L) motif from primate lentivirus Vif proteins that regulate APOBEC3G and APOBEC3F neutralizing activity. J Virol. 2010;84:8561-70 pubmed publisher
    ..It functions as an adaptor that binds to the cytidine deaminases APOBEC3G (A3G) and APOBEC3F (A3F) and bridges them to a cullin 5 (Cul5) and elongin (Elo) B/C E3 ubiquitin ligase complex for proteasomal ..
  24. Wang T, Tian C, Zhang W, Sarkis P, Yu X. Interaction with 7SL RNA but not with HIV-1 genomic RNA or P bodies is required for APOBEC3F virion packaging. J Mol Biol. 2008;375:1098-112 pubmed
    Human cytidine deaminase apolipoprotein B mRNA-editing catalytic polypeptide-like 3F (APOBEC3F, or A3F), like APOBEC3G, has broad antiviral activity against diverse retroelements, including Vif-deficient human immunodeficiency virus (HIV)-..
  25. Zennou V, Bieniasz P. Comparative analysis of the antiretroviral activity of APOBEC3G and APOBEC3F from primates. Virology. 2006;349:31-40 pubmed
    APOBEC3G and APOBEC3F exhibit antiretroviral activity primarily as a consequence of their ability to deaminate cytidines in retroviral DNA...
  26. Nathans R, Cao H, Sharova N, Ali A, Sharkey M, Stranska R, et al. Small-molecule inhibition of HIV-1 Vif. Nat Biotechnol. 2008;26:1187-92 pubmed publisher
    ..These results demonstrate that the HIV-1 Vif-A3G axis is a valid target for developing small molecule-based new therapies for HIV infection or for enhancing innate immunity against viruses...
  27. Tian C, Yu X, Zhang W, Wang T, Xu R, Yu X. Differential requirement for conserved tryptophans in human immunodeficiency virus type 1 Vif for the selective suppression of APOBEC3G and APOBEC3F. J Virol. 2006;80:3112-5 pubmed
    APOBEC3G (A3G) and related cytidine deaminases, such as APOBEC3F (A3F), are potent inhibitors of retroviruses. Formation of infectious human immunodeficiency virus type 1 (HIV-1) requires suppression of multiple cytidine deaminases by Vif...
  28. Wiegand H, Doehle B, Bogerd H, Cullen B. A second human antiretroviral factor, APOBEC3F, is suppressed by the HIV-1 and HIV-2 Vif proteins. EMBO J. 2004;23:2451-8 pubmed
    ..Here, we show that a second human protein, APOBEC3F, is also specifically packaged into HIV-1 virions and inhibits their infectivity...
  29. Nagao T, Yamashita T, Miyake A, Uchiyama T, Nomaguchi M, Adachi A. Different interaction between HIV-1 Vif and its cellular target proteins APOBEC3G/APOBEC3F. J Med Invest. 2010;57:89-94 pubmed
    ..human immunodeficiency virus type 1 (HIV-1) Vif for their interaction with cellular anti-viral factors APOBEC3G/APOBEC3F. Mutant viruses that display growth-defect in H9 cells did not counteract effectively APOBEC3G and/or APOBEC3F ..
  30. Wissing S, Galloway N, Greene W. HIV-1 Vif versus the APOBEC3 cytidine deaminases: an intracellular duel between pathogen and host restriction factors. Mol Aspects Med. 2010;31:383-97 pubmed publisher
    ..Vif acts by preventing virion encapsidation of two potent antiviral factors, the APOBEC3G and APOBEC3F cytidine deaminases...
  31. Liu B, Sarkis P, Luo K, Yu Y, Yu X. Regulation of Apobec3F and human immunodeficiency virus type 1 Vif by Vif-Cul5-ElonB/C E3 ubiquitin ligase. J Virol. 2005;79:9579-87 pubmed
    The human cytidine deaminase Apobec3F (h-A3F), a protein related to the previously recognized antiviral factor Apobec3G (h-A3G), has antiviral activity against human immunodeficiency virus type 1 (HIV-1) that is suppressed by the viral ..
  32. Luo K, Wang T, Liu B, Tian C, Xiao Z, Kappes J, et al. Cytidine deaminases APOBEC3G and APOBEC3F interact with human immunodeficiency virus type 1 integrase and inhibit proviral DNA formation. J Virol. 2007;81:7238-48 pubmed
    ..However, the mechanisms of A3G antiviral functions are incompletely understood. Here we demonstrate that A3G, A3F, and, to a lesser extent, the noncatalytic A3GC291S block human immunodeficiency virus type 1 (HIV-1) replication ..
  33. Haché G, Liddament M, Harris R. The retroviral hypermutation specificity of APOBEC3F and APOBEC3G is governed by the C-terminal DNA cytosine deaminase domain. J Biol Chem. 2005;280:10920-4 pubmed
    The human proteins APOBEC3F and APOBEC3G restrict retroviral infection by deaminating cytosine residues in the first cDNA strand of a replicating virus...
  34. Yamashita T, Kamada K, Hatcho K, Adachi A, Nomaguchi M. Identification of amino acid residues in HIV-1 Vif critical for binding and exclusion of APOBEC3G/F. Microbes Infect. 2008;10:1142-9 pubmed publisher
    ..E76A and W79A acted normally to inactivate A3G, they were found to exhibit a Vif-defective phenotype against A3F. Another unique mutant designated Y69A incompetent against both of A3G/F was also identified...
  35. Knoepfel S, Salisch N, Huelsmann P, Rauch P, Walter H, Metzner K. Comparison of G-to-A mutation frequencies induced by APOBEC3 proteins in H9 cells and peripheral blood mononuclear cells in the context of impaired processivities of drug-resistant human immunodeficiency virus type 1 reverse transcriptase variants. J Virol. 2008;82:6536-45 pubmed publisher
  36. Heger E, Thielen A, Gilles R, Obermeier M, Lengauer T, Kaiser R, et al. APOBEC3G/F as one possible driving force for co-receptor switch of the human immunodeficiency virus-1. Med Microbiol Immunol. 2012;201:7-16 pubmed publisher
    ..Causative agents for G-to-A mutations are the deaminases APOBEC3F and APOBEC3G...
  37. Chaipan C, Smith J, HU W, Pathak V. APOBEC3G restricts HIV-1 to a greater extent than APOBEC3F and APOBEC3DE in human primary CD4+ T cells and macrophages. J Virol. 2013;87:444-53 pubmed publisher
    ..We observed significant inhibition of HIV-1?vif produced in 293T cells in the presence of APOBEC3DE (A3DE), APOBEC3F (A3F), APOBEC3G (A3G), and APOBEC3H haplotype II (A3H HapII) but not APOBEC3B (A3B), APOBEC3C (A3C), or APOBEC3H ..
  38. Wedekind J, Dance G, Sowden M, Smith H. Messenger RNA editing in mammals: new members of the APOBEC family seeking roles in the family business. Trends Genet. 2003;19:207-16 pubmed
    ..In light of the hypothesis that these proteins might represent novel mRNA editing systems that could affect proteome diversity, we consider their structure, expression and relevance to biomedically significant processes or pathologies. ..
  39. Yang Y, Guo F, Cen S, Kleiman L. Inhibition of initiation of reverse transcription in HIV-1 by human APOBEC3F. Virology. 2007;365:92-100 pubmed
    Vif-negative HIV-1 produced in non-permissive human cells incorporate both APOBEC3F (hA3F) AND APOBEC3G (hA3G), and have a severely reduced ability to produce viral DNA in newly infected cells...
  40. Wang X, Dolan P, Dang Y, Zheng Y. Biochemical differentiation of APOBEC3F and APOBEC3G proteins associated with HIV-1 life cycle. J Biol Chem. 2007;282:1585-94 pubmed
    APOBEC3G and APOBEC3F are cytidine deaminase with duplicative cytidine deaminase motifs that restrict HIV-1 replication by catalyzing C-to-U transitions on nascent viral cDNA...
  41. Kobayashi T, Koizumi Y, Takeuchi J, Misawa N, Kimura Y, Morita S, et al. Quantification of deaminase activity-dependent and -independent restriction of HIV-1 replication mediated by APOBEC3F and APOBEC3G through experimental-mathematical investigation. J Virol. 2014;88:5881-7 pubmed publisher
    b>APOBEC3F and APOBEC3G cytidine deaminases potently inhibit human immunodeficiency virus type 1 (HIV-1) replication by enzymatically inserting G-to-A mutations in viral DNA and/or impairing viral reverse transcription independently of ..
  42. Han Y, Wang X, Dang Y, Zheng Y. APOBEC3G and APOBEC3F require an endogenous cofactor to block HIV-1 replication. PLoS Pathog. 2008;4:e1000095 pubmed publisher
    APOBEC3G (A3G)/APOBEC3F (A3F) are two members of APOBEC3 cytidine deaminase subfamily. Although they potently inhibit the replication of vif-deficient HIV-1, this mechanism is still poorly understood...
  43. Henry M, Guetard D, Suspène R, Rusniok C, Wain Hobson S, Vartanian J. Genetic editing of HBV DNA by monodomain human APOBEC3 cytidine deaminases and the recombinant nature of APOBEC3G. PLoS ONE. 2009;4:e4277 pubmed publisher
    ..A phylogenic analysis of A3 exons revealed that A3G is in fact a chimera with the first two exons being derived from the A3F gene. This might allow co-expression of the two genes that are able to restrict HIV-1Deltavif efficiently.
  44. Hultquist J, Binka M, LaRue R, Simon V, Harris R. Vif proteins of human and simian immunodeficiency viruses require cellular CBF? to degrade APOBEC3 restriction factors. J Virol. 2012;86:2874-7 pubmed publisher
  45. Jarmuz A, Chester A, Bayliss J, Gisbourne J, Dunham I, Scott J, et al. An anthropoid-specific locus of orphan C to U RNA-editing enzymes on chromosome 22. Genomics. 2002;79:285-96 pubmed
    ..Tissue-specific expression of these genes in a variety of cell lines, along with other evidence, suggests a role for these enzymes in growth or cell cycle control. ..
  46. Pery E, Rajendran K, Brazier A, Gabuzda D. Regulation of APOBEC3 proteins by a novel YXXL motif in human immunodeficiency virus type 1 Vif and simian immunodeficiency virus SIVagm Vif. J Virol. 2009;83:2374-81 pubmed publisher
    ..In HIV-1-infected CD4+ T cells, the viral accessory protein Vif binds to APOBEC3G (A3G), APOBEC3F (A3F), and APOBEC3C (A3C) and targets these proteins for polyubiquitination by forming an E3 ubiquitin ligase ..
  47. Harris R, Hultquist J, Evans D. The restriction factors of human immunodeficiency virus. J Biol Chem. 2012;287:40875-83 pubmed publisher
    ..These HIV restriction and counter-restriction mechanisms suggest strategies for new therapeutic interventions...
  48. Phalora P, Sherer N, Wolinsky S, Swanson C, Malim M. HIV-1 replication and APOBEC3 antiviral activity are not regulated by P bodies. J Virol. 2012;86:11712-24 pubmed publisher
    ..APOBEC3G and APOBEC3F interact with numerous proteins that regulate cellular RNA metabolism, including components of the RNA-induced ..
  49. Chiu Y, Greene W. APOBEC3G: an intracellular centurion. Philos Trans R Soc Lond B Biol Sci. 2009;364:689-703 pubmed publisher
    ..LMM A3G opposes the external threat posed by exogenous retroviruses, while HMM A3G complexes oppose the internal threat posed by the retrotransposition of select types of retroelements. ..
  50. Song C, Sutton L, Johnson M, D Aquila R, Donahue J. Signals in APOBEC3F N-terminal and C-terminal deaminase domains each contribute to encapsidation in HIV-1 virions and are both required for HIV-1 restriction. J Biol Chem. 2012;287:16965-74 pubmed publisher
    Human cytidine deaminases APOBEC3F (A3F) and APOBEC3G (A3G) inhibit human immunodeficiency virus type-1 (HIV-1) replication...
  51. Chen G, He Z, Wang T, Xu R, Yu X. A patch of positively charged amino acids surrounding the human immunodeficiency virus type 1 Vif SLVx4Yx9Y motif influences its interaction with APOBEC3G. J Virol. 2009;83:8674-82 pubmed publisher
    ..However, mutation of these residues had little effect on the Vif-mediated suppression of A3F, A3C, or A3DE, suggesting that these four residues are not important for Vif assembly with the Cul5 E3 ubiquitin ..
  52. Mbisa J, Bu W, Pathak V. APOBEC3F and APOBEC3G inhibit HIV-1 DNA integration by different mechanisms. J Virol. 2010;84:5250-9 pubmed publisher
    b>APOBEC3F (A3F) and APBOBEC3G (A3G) both are host restriction factors that can potently inhibit human immunodeficiency virus type 1 (HIV-1) replication...
  53. Xu H, Svarovskaia E, Barr R, Zhang Y, Khan M, Strebel K, et al. A single amino acid substitution in human APOBEC3G antiretroviral enzyme confers resistance to HIV-1 virion infectivity factor-induced depletion. Proc Natl Acad Sci U S A. 2004;101:5652-7 pubmed
    ..The HIV-1 Vif-resistant mutant APOBEC3G could provide a gene therapy approach to combat HIV-1 infection. ..
  54. Stenglein M, Harris R. APOBEC3B and APOBEC3F inhibit L1 retrotransposition by a DNA deamination-independent mechanism. J Biol Chem. 2006;281:16837-41 pubmed
    ..We show that expression of human APOBEC3B or APOBEC3F decreased the rate of L1 retrotransposition by 5-10-fold...
  55. Huthoff H, Towers G. Restriction of retroviral replication by APOBEC3G/F and TRIM5alpha. Trends Microbiol. 2008;16:612-9 pubmed publisher
    ..Examples of such molecules are APOBEC3G, APOBEC3F and TRIM5alpha...
  56. Holmes R, Koning F, Bishop K, Malim M. APOBEC3F can inhibit the accumulation of HIV-1 reverse transcription products in the absence of hypermutation. Comparisons with APOBEC3G. J Biol Chem. 2007;282:2587-95 pubmed
    b>APOBEC3F (apolipoprotein B mRNA-editing enzyme catalytic polypeptide 1-like protein 3F) is a cytidine deaminase that, like APOBEC3G, is able to restrict the replication of HIV-1/delta vif...
  57. Smith J, Pathak V. Identification of specific determinants of human APOBEC3F, APOBEC3C, and APOBEC3DE and African green monkey APOBEC3F that interact with HIV-1 Vif. J Virol. 2010;84:12599-608 pubmed publisher
    Human APOBEC3F (hA3F) and human APOBEC3G (hA3G) are potent anti-human immunodeficiency virus (anti-HIV) host factors that suppress viral replication by hypermutating the viral genome, inhibiting reverse transcription, and hindering ..
  58. Chiu Y, Greene W. The APOBEC3 cytidine deaminases: an innate defensive network opposing exogenous retroviruses and endogenous retroelements. Annu Rev Immunol. 2008;26:317-53 pubmed publisher
  59. Dang Y, Wang X, Zhou T, York I, Zheng Y. Identification of a novel WxSLVK motif in the N terminus of human immunodeficiency virus and simian immunodeficiency virus Vif that is critical for APOBEC3G and APOBEC3F neutralization. J Virol. 2009;83:8544-52 pubmed publisher
    The function of lentiviral Vif proteins is to neutralize the host antiviral cytidine deaminases APOBEC3G (A3G) and APOBEC3F (A3F)...
  60. Koning F, Newman E, Kim E, Kunstman K, Wolinsky S, Malim M. Defining APOBEC3 expression patterns in human tissues and hematopoietic cell subsets. J Virol. 2009;83:9474-85 pubmed publisher
    ..Here, we report a detailed examination of human APOBEC3 gene expression, focusing on APOBEC3G (A3G) and APOBEC3F (A3F), which are potent inhibitors of human immunodeficiency virus type 1 (HIV-1) infection but are suppressed by ..
  61. Binka M, Ooms M, Steward M, Simon V. The activity spectrum of Vif from multiple HIV-1 subtypes against APOBEC3G, APOBEC3F, and APOBEC3H. J Virol. 2012;86:49-59 pubmed publisher
    ..Seventeen Vif alleles from seven HIV-1 subtypes were tested for their abilities to degrade and counteract A3G, A3F, and A3H haplotype II (hapII)...
  62. Mulder L, Ooms M, Majdak S, Smedresman J, Linscheid C, Harari A, et al. Moderate influence of human APOBEC3F on HIV-1 replication in primary lymphocytes. J Virol. 2010;84:9613-7 pubmed publisher
    ..We used an HIV NL4-3 mutant that selectively counteracts APOBEC3G (A3G) but not APOBEC3F (A3F) to dissect the relative contribution of A3F to the inhibition of HIV-1 replication in primary human ..
  63. Russell R, Smith J, Barr R, Bhattacharyya D, Pathak V. Distinct domains within APOBEC3G and APOBEC3F interact with separate regions of human immunodeficiency virus type 1 Vif. J Virol. 2009;83:1992-2003 pubmed publisher
    Human APOBEC3G (A3G) and APOBEC3F (A3F) inhibit the replication of Vif-deficient human immunodeficiency virus type 1 (HIV-1). HIV-1 Vif overcomes these host restriction factors by binding to them and inducing their degradation...
  64. Dang Y, Davis R, York I, Zheng Y. Identification of 81LGxGxxIxW89 and 171EDRW174 domains from human immunodeficiency virus type 1 Vif that regulate APOBEC3G and APOBEC3F neutralizing activity. J Virol. 2010;84:5741-50 pubmed publisher
    The human cytidine deaminases APOBEC3G (A3G) and APOBEC3F (A3F) potently restrict human immunodeficiency virus type 1 (HIV-1) replication, but they are neutralized by the viral protein Vif...
  65. Zhen A, Wang T, Zhao K, Xiong Y, Yu X. A single amino acid difference in human APOBEC3H variants determines HIV-1 Vif sensitivity. J Virol. 2010;84:1902-11 pubmed publisher
    ..we found that Vif hijacks the same E3 ligase to degrade A3H_HapII as it does to inactivate APOBEC3G (A3G) and APOBEC3F (A3F), more Vif motifs were involved in A3H_HapII inactivation than in either A3G or A3F suppression...
  66. Gallois Montbrun S, Holmes R, Swanson C, Fernández Ocaña M, Byers H, Ward M, et al. Comparison of cellular ribonucleoprotein complexes associated with the APOBEC3F and APOBEC3G antiviral proteins. J Virol. 2008;82:5636-42 pubmed publisher
    The human apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3F (APOBEC3F [A3F]) and A3G proteins are effective inhibitors of infection by various retroelements and share approximately 50% amino acid sequence identity...
  67. Zheng Y, Irwin D, Kurosu T, Tokunaga K, Sata T, Peterlin B. Human APOBEC3F is another host factor that blocks human immunodeficiency virus type 1 replication. J Virol. 2004;78:6073-6 pubmed
    ..Here, we identified the human APOBEC3F protein as another host factor that blocks human immunodeficiency virus type 1 (HIV-1) replication...
  68. Albin J, Harris R. Interactions of host APOBEC3 restriction factors with HIV-1 in vivo: implications for therapeutics. Expert Rev Mol Med. 2010;12:e4 pubmed publisher
    ..virion infectivity factor (Vif), which uses multiple mechanisms to prevent APOBEC3 proteins such as APOBEC3G and APOBEC3F from entering viral particles...
  69. Stenglein M, Burns M, Li M, Lengyel J, Harris R. APOBEC3 proteins mediate the clearance of foreign DNA from human cells. Nat Struct Mol Biol. 2010;17:222-9 pubmed publisher
    ..The efficiency and fidelity of genetic engineering, gene therapy, and DNA vaccination are likely to be influenced by this anti-DNA defense system. ..
  70. Malim M, Emerman M. HIV-1 accessory proteins--ensuring viral survival in a hostile environment. Cell Host Microbe. 2008;3:388-98 pubmed publisher
    ..Broadly speaking, the HIV-1 accessory proteins modify the local environment within infected cells to ensure viral persistence, replication, dissemination, and transmission. ..
  71. Albin J, Haché G, Hultquist J, Brown W, Harris R. Long-term restriction by APOBEC3F selects human immunodeficiency virus type 1 variants with restored Vif function. J Virol. 2010;84:10209-19 pubmed publisher
    ..immunodeficiency virus type 1 (HIV-1) vif compromise virus replication in human T-cell lines that stably express APOBEC3F (A3F) or APOBEC3G (A3G)...
  72. Hakata Y, Landau N. Reversed functional organization of mouse and human APOBEC3 cytidine deaminase domains. J Biol Chem. 2006;281:36624-31 pubmed
    ..The Vif protein of lentiviruses binds to specific APOBEC3 proteins, notably A3F and A3G, to induce their degradation by proteasomes...
  73. Pion M, Granelli Piperno A, Mangeat B, Stalder R, Correa R, Steinman R, et al. APOBEC3G/3F mediates intrinsic resistance of monocyte-derived dendritic cells to HIV-1 infection. J Exp Med. 2006;203:2887-93 pubmed
    ..An increase in the A3G/3F-mediated intrinsic resistance of iDCs could result in a block of HIV infection at its mucosal point of entry. ..
  74. Turelli P, Mangeat B, Jost S, Vianin S, Trono D. Inhibition of hepatitis B virus replication by APOBEC3G. Science. 2004;303:1829 pubmed