APOBEC3G Antibody
- Known as:
- APOBEC3G Antibody
- Catalog number:
- AF1080a
- Product Quantity:
- 0.1mg
- Category:
- -
- Supplier:
- Abgen
- Gene target:
- APOBEC3G Antibody
Related genes to: APOBEC3G Antibody
- Gene:
- APOBEC3G NIH gene
- Name:
- apolipoprotein B mRNA editing enzyme catalytic subunit 3G
- Previous symbol:
- -
- Synonyms:
- CEM15, MDS019, dJ494G10.1, FLJ12740, bK150C2.7
- Chromosome:
- 22q13.1
- Locus Type:
- gene with protein product
- Date approved:
- 2001-12-12
- Date modifiied:
- 2016-10-05
Related products to: APOBEC3G Antibody
Related articles to: APOBEC3G Antibody
- Despite the widespread success of combination antiretroviral therapy (cART) in suppressing plasma viremia to undetectable levels, people living with HIV-1 (PLWH) continue to face a significantly elevated risk of chronic inflammation and Serious Non-AIDS Events (SNAEs). In this narrative review, we bridge the critical gap between molecular virology, immunometabolism, and clinical pathology by examining the complex interface of intrinsic immunity and viral persistence. We analyzed the evolutionary "arms race" between conserved host restriction factors, including TRIM5α, APOBEC3G, SAMHD1, BST-2, MX2, and SERINC, and the sophisticated viral evasion mechanisms that facilitate reservoir establishment. We further examined the role of bacterial translocation and gut barrier dysfunction in perpetuating systemic inflammation, emphasizing how HIV-1-mediated depletion of mucosal Th17 cells and disruption of tight junction proteins create a "leaky gut" that permits microbial product translocation despite suppressive therapy. Among viral proteins that may contribute to residual pathology during suppressive cART, we focused on the HIV-1 matrix protein p17, which has been proposed to function as a secreted "viral cytokine" from latent reservoirs, acting through CXCR1/CXCR2 receptors and the RACK1-JAK1-STAT1 pathway. Although primarily characterized in in vitro and ex vivo models, emerging data suggested that p17 may sustain systemic immune activation and metabolic reprogramming; however, its relative contribution compared with other viral proteins (Tat, Nef, gp120) in virologically suppressed patients remains to be fully delineated in human studies. Furthermore, we examined how HIV-1 hijacks cellular bioenergetics by shifting host cells from oxidative phosphorylation to aerobic glycolysis. We present an integrative model that connects restriction factor biology, p17-mediated chronic inflammation, immunometabolic dysregulation, and gut barrier dysfunction into a unified pathogenic framework, distinguishing established mechanisms from working hypotheses. Last, we assessed emerging therapeutic strategies, including CRISPR/Cas9-mediated enhancement of restriction factors, modulation of the mTOR pathway, and novel "Shock and Kill" approaches, stratified by development stage and demonstrated endpoints, offering potential pathways toward a functional cure. - Source: PubMed
Publication date: 2026/03/10
Nitsotolis ThomasAssimakopoulos Stelios FKouriannidi ElliLagadinou MariaPapalexandrou AlexiaIoannou PetrosMarangos MarkosMilionis HaralamposChristaki Eirini - Current animal models of HIV-1 infection are either immunocompromised or rely on proxy viruses instead of HIV-1. Here, we establish an immunocompetent animal model for CXCR4-tropic HIV-1 in owl monkeys (Aotus nancymaae). Through analysis of 191 owl monkeys, genetic characterization and functional testing demonstrate that CD4 and Tetherin in this species support HIV-1 replication. Although owl monkeys do carry restrictive TRIMCyp and APOBEC3G alleles, small changes to the HIV-1 genome allow the virus to overcome these barriers. The resulting virus remains 93% wildtype HIV-1 in sequence. Fully immunocompetent owl monkeys can be infected with this virus, recapitulating key aspects of HIV-1 infection in humans: an initial surge of virus replication, subsequent establishment of a durable set point viremia, seroconversion, and the formation of a viral reservoir. The owl monkey model broadens the experimental options for HIV-1 research, and future studies will explore its utility for CCR5-tropic virus strains. - Source: PubMed
Publication date: 2026/03/09
Meyerson Nicholas RBauer Vanessa LFattor Will TWarren Cody JBarbachano-Guerrero ArturoWeiss Melisa JDirasantha ObaiahBurris Bridget LAdesina Adetunji STimpona Joseph LFeldman Emily RFahy Ryan TGendler PaulFainberg AvaNehete Pramod NShelton Kathryn AGalvan AnalyTustin George WKoehle Paul JSalinas Maria DDavila OmarLindemann Elizabeth IClark Sean EGarnett Mackenzie LDeMarco C ToddScianna Salvatore RDenny Thomas NKuhn Jens HAye Pyone PVeazey Ron SKezar Sarah MWilkerson Gregory KSawyer Sara L - Vif and Vpr are HIV-1 accessory proteins that create optimal conditions for viral replication. They are considered as potential targets for the development of therapeutic agents. Natural amino acid substitutions in these proteins have previously been associated with disease progression. The aim of this study was to analyze the genetic diversity of Vif and Vpr in HIV-1 group M clades. A total of 5286 sequences were downloaded and analyzed. For 37 clades in group M, the consensus sequences, amino acid natural variation, and clade-specific amino acid residue substitutions (CSSs) were evaluated. Structural analysis and modeling of consensus sequences were performed for subtypes A1, B, C, and D. The average conservation degree in the HIV-1 group M was 86.4% for Vif and 91.3% for Vpr. In both proteins, the lowest amino acid diversity was observed in sub-subtype A6, and the highest in subtype B. In consensus sequences, the substitutions, which might influence pathogenesis, have been determined: in Vif-22H (11_cpx, 91_cpx) and 136P (A6, 01_AE, 15_01B, 59_01B, 89_BF1, 103_01B, 111_01C, 133_A6B), in Vpr-41N (06_cpx) and 55A (B, 07_BC, 35_01D, 56_cpx, 66_cpx, 66_BF1, 71_BF1, 85_BC, 137_0107). In functional motifs, CSSs associated with changes in the chemical properties of amino acid residues were noted. These findings could be taken into account for the development of therapeutic drugs in the future. No correlation was observed between the subtypes and the spatial organization of the oligomeric structures of Vif and Vpr. Using the structural analysis and modeling, it has been shown for the first time that Vif can interact with APOBEC3G as an oligomer. - Source: PubMed
Publication date: 2026/01/15
Galzitskaya OxanaLebedev AlekseyAntonova AnastasiiaMezhenskaya EkaterinaGlyakina AnnaDeryusheva EvgeniyaLikhachev IlyaKuznetsova Anna - Cytosine base editors (CBEs) enable efficient cytosine-to-thymine substitutions at targeted genomic loci without introducing double-stranded breaks. Among CBEs, APOBEC3G BEs (A3G-BEs) preferentially edit the second cytosine within a 5'-CC-3' motif in human cells, reducing potential bystander editing. However, A3G-BEs often unintentionally edit multiple CC motifs within their editing window and are limited by protospacer adjacent motif (PAM) constraints imposed by SpCas9, which restricts their applicability. Here, we engineered A3G-BE variants through linker optimization, rational mutagenesis, and the integration of SpG and SpRY Cas9 effectors with relaxed PAM constraints. These improvements enhanced the precision of single-cytosine editing within CC motifs and broadened the targeting scope to previously inaccessible genomic sites. We then validated the engineered A3G-BE variants by precisely installing and correcting cystic fibrosis-causing mutations in HEK293T cells. When applied to 16HBE14o-human bronchial epithelial cells, precise editing modulated cystic fibrosis transmembrane conductance regulator mRNA levels, protein expression, and channel function, establishing precision A3G-BE variants as powerful tools for modeling and treating cystic fibrosis and other human diseases. - Source: PubMed
Publication date: 2026/01/14
Zeng HongzhiLiu AidiDaniel Tyler CGolla Devin ALu ZhenyuSerodio RebeccaMillette Brigid ALingineni AnanyaGilberd PeretzChee KellyTalloo KomalPeddi AdvaithPark So HyunBao GangGao Xue - Type I interferons (IFNs), particularly IFN-α, occupy a central paradox in HIV-1 infection: they provide an essential early antiviral barrier that limits initial dissemination, yet their sustained activation contributes to chronic immune activation, CD4 T-cell dysfunction, and incomplete viral control. This duality-protective in acute infection but pathogenic during chronic disease-remains a major unresolved challenge for interferon-based therapeutic strategies in HIV-1. Recent advances in ISG functional profiling, IFN-α subtype-specific antiviral potency, and the development of targeted innate-pathway modulators (e.g., STING-selective agonists, ncRNA regulators, TLR7 activators) have renewed interest in reevaluating interferon-centered approaches. These developments make it timely to reassess whether IFN-α can be safely and effectively integrated into modern HIV-1 therapeutic concepts, particularly in early-infection windows or in rationally designed combination regimens. In this review, we synthesize current knowledge of interferon-mediated restriction mechanisms, the hierarchy of key antiviral ISGs (e.g., APOBEC3G, MX2, BST2), and HIV-1 evasion of the JAK-STAT and cGAS-STING pathways. We further analyze how dose, timing, and IFN-α subtype contribute to divergent antiviral versus inflammatory outcomes across different stages of infection. Emerging precision strategies that modulate interferon signaling without triggering systemic inflammation offer promising translational directions. Balancing antiviral efficacy with immune homeostasis will be essential for developing next-generation interferon-based interventions aimed at durable control or functional cure of HIV-1 infection. - Source: PubMed
Publication date: 2025/12/18
Zhu LuyingJi JiahaoXiao JingWang FuchunYu JiaqiLiu YanminZhang YangWu HaoSu BinLu XiaofanZhang Tong