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Validated All-in-One™ qPCR Primer for APOBEC3G(NM_021822.3) Search again
Product ID:
HQP016317
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
A3G, ARCD, ARP-9, ARP9, CEM-15, CEM15, MDS019, bK150C2.7, dJ494G10.1
Gene Description:
apolipoprotein B mRNA editing enzyme catalytic subunit 3G
Target Gene Accession:
NM_021822.3(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
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| A | B |
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Each All-in-One™ qPCR Primer is experimentally validated to yield a single dissociation curve peak and to generate a single amplification of the correct size for the targeted gene. A cDNA Pool, containing reverse transcript products of 8 different human tissue total RNA(Liver, Testis,Muscle,Thyroid,Brain,Spleen,Stomach,Small Intestine)),was used as the qPCR validation template. qPCR was performed using 0.2 µM primer with 2XAll-in-One™ qPCR Mix (Catalog#: QP001,QP002,QP004,QP005). Reactions were incubated for 10min. at 95°C, followed by 40 cycles of 95°C for 10 sec.; 60°C, 20 sec. and 72°C, 15sec. using Bio-Rad iQ5™ Instrument. At the end of the last cycle, temperature was increased from 72 to 95°C to produce a melting curve. Panel A: Validated Result for Amplification Curve; Panel B: Validated Result for Melting Curve. |
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Summary
This gene is a member of the cytidine deaminase gene family. It is one of seven related genes or pseudogenes found in a cluster, thought to result from gene duplication, on chromosome 22.
Gene References into function
- Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein.
- APOBEC3G is incorporated into HIV-1 particles and acts to restrict HIV-1 replication in infected cells by deaminating dC to dU in the first (minus)-strand cDNA replication intermediate during the viral reverse transcription process
- a cytidine deaminase that is able to induce G to A hypermutation in newly synthesized HIV-1 DNA
- APOBEC3G exerts its antiviral effect during reverse transcription to trigger G-to-A hypermutation in the nascent HIV DNA
- mutagenesis analysis on two cytidine deaminase motifs in CEM15/Apobec-3G indicates that the enzymatic activity of this protein is essential but not a sole determinant of the HIV-1 antiviral activity
- Viral infectivity factor prevents virion incorporation of endogenous APOBEC3G by effectively depleting the intracellular levels of this enzyme in HIV-1-infected T cells.
- Vif inhibits packaging of APOBEC3G into virus particles in a dose-dependent manner and reduces its intracellular expression level.
- ability of HIV-1 Vif to suppress antiviral activity of APOBEC3G was specifically dependent on Cul5-SCF function, allowing Vif to interact with APOBEC3G and induce its ubiquitination and degradation
- results suggest that Vif functions by targeting APOBEC3G for degradation via the ubiquitin-proteasome pathway and implicate the proteasome as a site of dynamic interplay between microbial and cellular defenses.
- HIV-1 Vif could induce rapid degradation of human APOBEC3G that was blocked by the proteasome inhibitor MG132. The efficiency of Vif-induced downregulation of APOBEC3G expression depended on the level of Vif expression.
- inhibits hepatitis B virus replication; block of HBV DNA accumulation by APOBEC3G seems to result from an inhibition of viral pregenomic RNA packaging
- A single amino acid substitution mutant of human APOBEC3G (D128K) can interact with HIV-1 Vif but is not depleted from cells; thus, it inhibits HIV-1 replication in an HIV-1 Vif-resistant manner.
- APOBEC3G inhibits HIV-1 infection through interference with reverse transcription.
- cytoplasmic apolipoprotein B mRNA editing enzyme(APOBEC3G) becomes membrane-bound in cells expressing HIV-1 Gag, and its incorporation into Gag viral-like particles (VLPs) is proportional to the amount of APOBEC3G expressed in the cell
- APOBEC3G interactions with HIV-1 and nonviral RNAs that are packaged into viral particles are sufficient for APOBEC3G virion incorporation
- APOBEC3G gene has been subject to strong positive selection throughout the history of primate evolution
- observations allow speculation (i) that APOBEC-mediated C-to-U editing may contribute to the sequence variation of viruses that replicate entirely through RNA, and (ii) that additional cellular RNA substrates might exist for the APOBEC enzymes
- expression of the antiviral APOBEC3G editing enzyme is dynamically controlled by the PKCalpha/betaI/MEK/ERK protein kinase cascade in human T lymphocytes
- Results demonstrate that the expression of HIV-1 Gag is sufficient to induce the packaging of human APOBEC3G into Gag particles.
- Depletion of APOBEC3G from Vif expressing cells is not a universal property of Vif and thus is not imperative for the production of infectious virions.
- Depletion of APOBEC3G is not the sole protective mechanism of Vif and additional mechanisms exerted by this protein can be envisioned which counteract APOBEC3G and enhance HIV infectivity.
- cytoplasmic Vif-APOBEC3G interactions are required but are not sufficient for Vif to modulate APOBEC3G and can be monitored by co-localization in vivo
- Vif targets APOBEC3G for degradation by forming an SCF-like E3 ubiquitin ligase containing Cullin 5 and Elongins B and C (Cul5-EloB-EloC) through a novel SOCS-box
- ubiquitination of APOBEC3G by Nedd4-1 favors its targeting to the virus assembly site where APOBEC3G interacts with Gag and is packaged into HIV-1 particles in the absence of Vif
- Induces degradation of APOBEC3G by bringing to relevance that deaminase inhibition can also result from a direct interaction with Vif protein.
- Functional analysis of Vif protein shows less restriction of human immunodeficiency virus type 2 by APOBEC3G.
- only the C-terminal domain of APOBEC3F and -3G dictates the retroviral minus strand 5'-TC and 5'-CC dinucleotide hypermutation preferences.
- APOBEC3G, by editing viral genetic material, provides an ancestral wide cellular defence against endogenous and exogenous invaders
- Using APOBEC3G deletion and point mutants, we mapped the encapsidation determinant to the Zn(2+) coordination residues of the N-terminal catalytic domain (CD1).
- the E3 ubiquitin ligase activity of the Vif-BC-Cul5 complex is essential for Vif function against APOBEC3G
- APOBEC3G potently inhibits replication of the Ty1 LTR retrotransposon in yeast.
- APOBEC3G-restricts HIV-1 infection in resting CD4+ T cells, which may not be strictly dependent on deoxycytidine deamination
- APOBEC3G is incorporated into HTLV-1 virions and inhibits the infection of HTLV-1 through different mechanisms from that on HIV-1
- APOBEC3G hypermutates genomic DNA and inhibits Ty1 retrotransposition in yeast.
- APOBEC3G is induced by IFN stimulation in human hepatocytes and thus could be involved in host defense mechanisms directed against hepatitis viruses
- APOBEC3F was less potent than APOBEC3G in inhibitinhg HIV-1; Vif proteins appeared more potent & specific when APOBEC3G is the target rather than APOBEC3F
- Most of the highly conserved tryptophan residues were required for efficient suppression of both APOBEC3G (A3G) and APOBEC3F (A3F), but some of these residues were selectively required for the suppression of A3F but not A3G.
- G --> A mutational gradient generated in viral genomic DNA in vivo could result from an intrinsic processive directional attack by APOBEC3G on single-stranded cDNA
- Mutation of a conserved cysteine residue (C97) that is part of an N-terminal zinc-finger motif in APOBEC3G abolishes multimerization of APOBEC3G; however this C97 mutant is both catalytically active and has antiviral activity
- results provide novel insights into the catalytic function and antiviral property of APOBEC3G
- novel link between innate immunity against retroviruses and P-bodies suggesting that APOBEC3G and APOBEC3F could function in the context of P-bodies to restrict HIV-1 replication.
- molecular analysis of the deaminase and nucleic acid binding activities of human APOBEC3G
- These findings indicate that APOBEC3G could suppress HBV replication and antigen expression both in vivo and in vitro, promising an advance in treatment of HBV infection.
- APOBEC3G binds HIV-1 RNA and messenger RNAs that shuttle between polysomes and stress granules
- APOBEC3G-induced HIV-1 hypermutation represents a potent host antiviral factor in vivo
- might be a role for APOBEC3G in susceptibility to HIV-1 infection
- Data identify nonautonomous Alu and hY retroelements as cellular targets of APOBEC3G (A3G) and suggest how different forms of A3G protect cells from exogenous retroviruses (LMM A3G) and endogenous retroelements (HMM A3G).
- We demonstrated an increased expression of APOBEC3G in both hepatocytes and lymphocytes of chronic hepatitis patients infected with HCV.
- These findings support APOBEC3G degradation as a requirement for HIV-1 Vif function.
- data indicate that APOBEC3G is not a restriction factor for vaccinia virus replication nor is vaccinia virus able to degrade APOBEC3G
- APOBEC3G selectively inhibits Alu retrotransposition in an ORF1p-independent manner. An active cytidine deaminase site is not required for the inhibition of Alu retrotransposition and the resultant integration events lack G to A or C to T hypermutation.
- presents low resolution structures of hA3G in HMM and LMM forms determined by small angle x-ray scattering and advanced shape reconstruction methods
- it is concluded that approximately 7 (+/-4) molecules of A3G are incorporated into Deltavif HIV-1 virions produced from PBMCs; results indicate that virion incorporation of only a few molecules of A3G is sufficient to inhibit HIV-1 replication
- APOBEC3F and APOBEC3G complexes undergo dynamic conversion during HIV-1 infection
- Findings highlight a role for APOBEC3G/3F in explaining the resistance of most dendritic cells to HIV-1 infection, as well as the susceptibility of a fraction of immature dendritic cells.
- Small interfering RNA-mediated depletion of APOBEC3G, but not TRIM5alpha, enhances HIV-1 infection of immature dendritic cells (iDCs), indicating that APOBEC3G controls the sensitivity of iDCs to HIV-1 infection
- cytoplasmically expressed DNA deaminase APOBEC3G acts in a processive manner, possibly suggesting that evolutionary pressure has altered the ability of DNA deaminases to act in a processive or distributive manner, depending on the physiological need
- APOBEC3G associates with RNPs that are found throughout the cytosol as well as in discrete microdomains.
- Expression upregulated by inflammatory cytokines, such as interferon, interleukin-6, and tumor necrosis factor.
- Ligation of cell surface CCR5 receptors by CCL3 or CD40 by CD40L activated the ERK1/2 and p38 MAPK signaling pathways that induced APOBEC3G mRNA expression and production of the APOBEC3G protein
- Our results suggest that APOBEC3G, upregulated by IFNs, has a dual effect on HBV: induction of hypermutation and reduction of virus synthesis.
- mouse A3-containing and human A3G-containing virions showed a marked decrease in titre
- we confirm the central role played by the aspartic acid at position 128 and identify proline 129 and aspartic acid 130 as important contributory residues for interaction with HIV-1 Vif.
- the degradation of APOBEC3G-edited viral DNA mediated by virion-associated UNG2 and APE during or after reverse transcription could be partially responsible for the potent anti-HIV-1 effect by APOBEC3G in the absence of vif
- The inhibitory effect of APOBEC3 proteins on Hepatits B virus replication is mainly at the DNA level at very early stages during viral reverse transcription, with only a minor effect on viral RNA packaging.
- our results indicate that APOBEC3G multimerizes in an RNA-dependent fashion and that RNA-APOBEC3G multimers are recruited to the plasma membrane and subsequently into virion particles by Gag.
- investigation of possible anti-HIV activity of hA3G (APOBEC3G); hA3G mRNA levels follow a hierarchical order of long-term nonprogressors>HIV-uninfected>Progressors; hA3G mRNA abundance correlates with surrogates of HIV disease progression
- A GC-box of the human APOBEC3G gene represents a binding site for the ubiquitous transcription factors specificity protein (Sp) 1 and Sp3.
- These results demonstrate that targeting of APO3G to proteasome degradation and interference with viral encapsidation are distinct functional properties of Vif.
- Results reveal two distinct Vif determinants, amino acids Y(40)RHHY(44) and D(14)RMR(17), which are essential for binding to APOBEC3G and APOBEC3F, respectively.
- Vif binding to RNA and DNA offers several non-exclusive ways to counteract APOBEC3G/3F factors, in addition to the well documented Vif-induced degradation by the proteasome and to the Vif-mediated repression of translation of these antiviral factors
- RNAs tested in this study were packaged into viruses or virus-like particles we failed to identify a correlation between APO3G encapsidation and the packaging of these cellular RNAs.
- interaction of APOBEC3G with HIV1gp2 nucleocapsid is required for the inhibition of reverse transcription initiation
- intracellular degradation of APO3G may not be the sole activity of Vif required for the production of infectious virions from APO3G-expressing cells
- the major cellular function of A3G, in addition to inhibiting the mobility of retrotransposons and replication of endogenous retroviruses, is most likely to prevent the decay of miRNA-targeted mRNA in processing bodies
- This report demonstrates that the reduction of late viral DNA synthesis is due to the inhibition by human APOBEC3G of the strand transfer steps that occur during reverse transcription.
- corroborated an APOBEC2-based structural model for the catalytic domain of APOBEC3G indicating that most non-essential residues are solvent accessible and most essential residues cluster within the protein core
- 7SL RNA that is encapsidated into diverse retroviruses is a key cofactor of the antiviral APOBEC3G.
- The localization of the expressed GFP-APOBEC3G was observed in the cytoplasm of CD4+ HeLa cells.
- T cells, unlike epithelial-derived cell lines, express an unidentified RNase-resistant factor that inhibits APOBEC3G (A3G) deaminase activity.
- Cell-based binding assays confirmed these results and demonstrated that residues 40 to 71 in the N terminus of Vif contain a nonlinear binding site for APOBEC3G.
- Inhibition of hA3G degradation by the C-terminal hA3G fragment 157-384 appears to be related to its ability to prevent the polyubiquitination of hA3G induced by Vif, a process that is required for Vif-mediated proteosomal degradation of hA3G.
- We conclude that efficient inhibition of vif-defective human immunodeficiency virus type 1 requires catalytically active APO3G.
- Our results expose a novel function of Vif that promotes the assembly of APO3G into presumably packaging-incompetent high moelcular mass complexes.
- enhanced APOBEC3 activity alone cannot explain the ability of elite suppressors to control viremia
- CRS enables hA3G to interact with cytoplasmic factors, and thereby enables hA3G to serve in host cell defense by restricting an antiviral sentinel to the cytoplasm.
- absolute requirement for the catalytic glutamate of APOBEC3G in Ty1, MusD, and HIV-1 restriction strongly indicates that DNA cytosine deamination is an essential part of the mechanism
- Our data indicate that plasmacytoid dendritic cells are protected by an IFN-alpha mediated upregulation of APOBEC3G type of innate immunity from HIV-1 infection.
- solution structure of the human APOBEC3G catalytic domain
- APOBEC3G has important restriction activity in the cytoplasm and progressively diminishes viral cytoplasmic and nuclear cDNA forms with increasing magnitude during restriction.
- polyubiquitylated Vif might serve as a vehicle to transport APOBEC3G into proteasomes for degradation
- diverse A3G oligomerization modes contribute to the human immunodeficiency virus, type 1, proviral DNA mutational bias
- Study presents recent advances detailing the mechanisms of the Vif-Apobec3G regulatory circuit.
- define a number of subtle differences between the ribonucleoprotein complexes associated with APOBEC3F and APOBEC3G and speculate
- Vpr14-88-Apobec3G fusion protein is efficiently incorporated into Vif-positive HIV-1 particles and inhibits viral infection
- These results indicate that APOBEC3G, APOBEC3C and APOBEC3H have the ability to edit HBV DNA and that each protein is likely to contribute to various degrees to the generation of modified genomes in human liver cells.
- RNA binding by APOBEC3G is key for initiation of APOBEC3G:nucleocapsid complex formation in vitro.
- The paper provides evidence that the N-terminal domain of APOBEC3G is required for packaging into HBV nucleocapsids.
- Vif binds APOBEC3G (A3G) and a Cullin5-ElonginBC E3 ubiquitin ligase complex which results in the proteasomal degradation of A3G. Failure of a Vif mutant to bind A3G resulted in A3G incorporation into assembling virions with loss of viral infectivity.
- APOBEC3G-expressing T cells were infected with Vif-deficient HIV-1. Resistance occurred by a novel tolerance mechanism.
- The binding of APOBEC3G to 7SL RNA through its Alu domain suggests a mechanism for APOBEC-mediated inhibition of Alu retrotransposition. However 7SL RNA is not essential for the HIV-1 virion recruitment of the antiviral cytidine deaminase.
- A VxIPLx(4-5)LxPhix(2)YWxL motif in HIV-1 Vif is identified, which is required for efficient interaction between Vif and APOBEC3G (A3G), Vif-mediated A3G degradation and virion exclusion, and functional suppression of the A3G antiviral activity.
- Here, the authors demonstrate that the ability to bind to Gag and package into HIV-1 virions is entirely contained within the amino-terminal half of A3G.
- No genetic H186R polymorphism in exon 4 of APOBEC3G gene is found and therefore neither neither associated with differential susceptibility to HIV-1 infection/progression among North Indians.
- two regions of APOBEC3G combine to mediate an intermolecular interaction that controls subcellular localization
- Results show that the prolyl isomerase Pin1 modulates APOBEC3G expression.
- These data indicate that NF-IL6 is a natural inhibitor of APOBEC3G that facilitates HIV-1 replication.
- These data imply that protein kinase A-mediated phosphorylation of APOBEC3G can regulate the interaction between APOBEC3G and Vif.
- N-terminal domains of hA3G were unable to multimerize but remained functional for Gag and viral infectivity factor (Vif) interactions when expressed apart from the C terminus.
- high-resolution crystal structure of the carboxy-terminal deaminase domain of APOBEC3G (APOBEC3G-CD2)
- Thus, hA3G might be restricting viral growth in infected individuals through a mechanism that is independent of the cytidine deaminase activities of hA3G.
- enzymatic activity of encapsidated APOBEC3G does not correlate with the observed limited cytidine deamination in HIV-1 DNA, suggesting that APOBEC3G-laden exosomes restrict HIV-1 through a nonenzymatic mechanism.
- The results suggest that HIV-1 Vif preferentially induces degradation of newly synthesized APOBEC3G but indiscriminately inhibits encapsidation of "old" and "new" APOBEC3G.
- The authors found that the APOBEC3G domain that interacts with the Vif YRHHY region is located between amino acids 126 and 132 of A3G, which is consistent with the conclusions reported in previous studies.
- study finds that although reverse transcription initiates in the presence of APOBEC3G (A3G), elongation of the cDNA product is impeded; data support the model that A3G reduces HIV-1 cDNA levels by inhibiting synthesis rather than by inducing degradation
- analysis of the enzymatic reaction of wild-type APOBEC3G