APOBEC3G Complexes Decrease Human Immunodeficiency Virus Type 1 Production

Martin, Kenneth L.; Johnson, Megan E.; D’Aquila, Richard T.

doi:10.1128/jvi.00273-11

Cited by 17 publications

(9 citation statements)

References 60 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In contrast to this study, it was previously reported that A3G-C97A packages efficiently into virions 10,84 . It is conceivable that this incongruence is associated with different expression levels.…”

Section: Discussioncontrasting

confidence: 97%

APOBEC3 Multimerization Correlates with HIV-1 Packaging and Restriction Activity in Living Cells

Chen

et al. 2014

Journal of Molecular Biology

View full text Add to dashboard Cite

APOBEC3G belongs to a family of DNA cytosine deaminases that are involved in the restriction of a broad number of retroviruses including HIV-1. Prior studies have identified two distinct mechanistic steps in Vif-deficient HIV-1 restriction: packaging into virions and deaminating viral cDNA. APOBEC3A, for example, although highly active, is not packaged and is therefore not restrictive. APOBEC3G, on the other hand, although having weaker enzymatic activity, is packaged into virions and is strongly restrictive. Although a number of studies have described the propensity for APOBEC3 oligomerization, its relevance to HIV-1 restriction remains unclear. Here, we address this problem by examining APOBEC3 oligomerization in living cells using molecular brightness analysis. We find that APOBEC3G forms high-order multimers as a function of protein concentration. In contrast, APOBEC3A, APOBEC3C and APOBEC2 are monomers at all tested concentrations. Among other members of the APOBEC3 family, we show that the multimerization propensities of APOBEC3B, APOBEC3D, APOBEC3F, and APOBEC3H (haplotype II) bear more resemblance to APOBEC3G than to APOBEC3A/3C/2. Prior studies have shown that all of these multimerizing APOBEC3 proteins, but not the monomeric family members, have the capacity to package into HIV-1 particles and restrict viral infectivity. This correlation between oligomerization and restriction is further evidenced by two different APOBEC3G mutants, which are each compromised for multimerization, packaging, and HIV-1 restriction. Overall, our results imply that multimerization of APOBEC3 proteins may be related to the packaging mechanism and ultimately to virus restriction.

show abstract

Section: Discussioncontrasting

confidence: 97%

APOBEC3 Multimerization Correlates with HIV-1 Packaging and Restriction Activity in Living Cells

Chen

et al. 2014

Journal of Molecular Biology

View full text Add to dashboard Cite

show abstract

“…Moreover, an intact zinc-coordination motif of A3G-NTD is required for inhibiting Alu and HIV-1 retroelements33. Mutation in the C97 residue of the NTD cause defects in forming A3G cytoplasmic complexes resulting in decreased HIV-1 virus production38. Evolutionary analyses of primate sequences indicate that A3G has undergone a strong positive selection throughout its gene sequence, as evidenced by an excess of non-synonymous over synonymous nucleotide substitutions3940.…”

Section: Discussionmentioning

confidence: 99%

The double-domain cytidine deaminase APOBEC3G is a cellular site-specific RNA editing enzyme

Sharma

Patnaik

Taggart

et al. 2016

Sci Rep

113

View full text Add to dashboard Cite

APOBEC3G is a cytidine deaminase with two homologous domains and restricts retroelements and HIV-1. APOBEC3G deaminates single-stranded DNAs via its C-terminal domain, whereas the N-terminal domain is considered non-catalytic. Although APOBEC3G is known to bind RNAs, APOBEC3G-mediated RNA editing has not been observed. We recently discovered RNA editing by the single-domain enzyme APOBEC3A in innate immune cells. To determine if APOBEC3G is capable of RNA editing, we transiently expressed APOBEC3G in the HEK293T cell line and performed transcriptome-wide RNA sequencing. We show that APOBEC3G causes site-specific C-to-U editing of mRNAs from over 600 genes. The edited cytidines are often flanked by inverted repeats, but are largely distinct from those deaminated by APOBEC3A. We verified protein-recoding RNA editing of selected genes including several that are known to be involved in HIV-1 infectivity. APOBEC3G co-purifies with highly edited mRNA substrates. We find that conserved catalytic residues in both cytidine deaminase domains are required for RNA editing. Our findings demonstrate the novel RNA editing function of APOBEC3G and suggest a role for the N-terminal domain in RNA editing.

show abstract

“…However, the viral infectivity factor Vif protein induces APOBEC3 degradation, preventing its incorporation into virions [ 47 ], affecting its subcellular localization, degradation rates and antiviral properties [ 250 ]. Several groups have reported that depletion of PB components or RISC components (including DDX6, LSM-1, GW182, XRN1, DGCR8, Dicer and Drosha) increases the viral production and that gRNA and Gag protein localize to PBs [ 251 , 252 , 253 ]. Nevertheless, gRNA localization in PBs has not been detected by others [ 228 , 254 ], and the depletion of Ago2 or DDX6 resulted in the inhibition of HIV-1 replication [ 255 , 256 ].…”

Section: Viral Infections and Processing Bodiesmentioning

confidence: 99%

Who Regulates Whom? An Overview of RNA Granules and Viral Infections

Poblete-Durán

Prades-Pérez

Vera-Otárola

et al. 2016

Viruses

100

View full text Add to dashboard Cite

After viral infection, host cells respond by mounting an anti-viral stress response in order to create a hostile atmosphere for viral replication, leading to the shut-off of mRNA translation (protein synthesis) and the assembly of RNA granules. Two of these RNA granules have been well characterized in yeast and mammalian cells, stress granules (SGs), which are translationally silent sites of RNA triage and processing bodies (PBs), which are involved in mRNA degradation. This review discusses the role of these RNA granules in the evasion of anti-viral stress responses through virus-induced remodeling of cellular ribonucleoproteins (RNPs).

show abstract

APOBEC3G Complexes Decrease Human Immunodeficiency Virus Type 1 Production

Abstract: APOBEC3G (A3G) is packaged into human immunodeficiency virus type 1 (HIV-1

Cited by 17 publications

References 60 publications

APOBEC3 Multimerization Correlates with HIV-1 Packaging and Restriction Activity in Living Cells

APOBEC3 Multimerization Correlates with HIV-1 Packaging and Restriction Activity in Living Cells

The double-domain cytidine deaminase APOBEC3G is a cellular site-specific RNA editing enzyme

Who Regulates Whom? An Overview of RNA Granules and Viral Infections

Contact Info

Product

Resources

About