anti-Apolipoprotein B mRNA Editing Enzyme, Catalytic Polypeptide-Like 3A (APOBEC3A) Antibodies

Human Apolipoprotein B mRNA Editing Enzyme, Catalytic Polypeptide-Like 3A (APOBEC3A) interaction partners

1. Study identified the APOBEC3A (A3A) preferred ssDNA binding motif, (T/C)TC(A/G) and found binding correlated with enzymatic activity. Also, A3A can bind RNA in a sequence specific manner. Surprisingly, A3A's signature sequence was necessary but not sufficient to account for A3A's high affinity for ssDNA. Significantly, A3A bound more tightly to the motif in longer oligonucleotides, and in the context of a hairpin loop.

2. This study supports the model that different APOBEC3 proteins have evolved to inhibit LINE-1 retrotransposition through distinct mechanisms and shows that APOBEC3A is a potent deamination-dependent inhibitor of LINE-1 retrotransposition.

3. It is the major target for C-to-T substitutions in the HPV genomes.

4. We show that knockdown of A3A in latently infected human primary CD4 T cells enhanced HIV-1 reactivation. Collectively, we provide evidence and a mechanism by which A3A reinforces HIV-1 latency in infected CD4 T cells.

5. Data show the crystal structure of a complex of a cytidine deaminase (APOBEC3A) with single-stranded DNA (ssDNA) bound in the active site at 2.2 A.

6. The results suggest that APOBEC3A expression is downregulated during progression towards invasiveness in human papillomaviruse (HPV)-negative penile squamous cell carcinoma (SCC), but maintained in HPV-positive penile SCC.

7. Enhanced apolipoprotein APOBEC3A repressed human papillomavirus HPV11 E6 expression through gene hypermutation, and recombinant human interferon-omega rhIFN-omega might be an effective agent against HPV11 infection by up-regulation of APOBEC3A.

8. APOBEC3A is the most likely gene to be active in HPV+ HNSCC. APOBEC activity correlates with upregulation of immune signaling pathways, supporting the hypothesis that APOBEC activity could be activated as part of the innate immune response

9. direct evidence that both A3A and HPV16 E7 interact with CUL2, suggesting that the E7-CUL2 complex formed during HPV infection may regulate A3A protein levels in the cell.

10. review of current understanding of APOBEC3A and APOBEC3B biology in human papillomavirus Infection restriction, evolution, and associated cancer mutagenesis

11. p53 activation alters APOBECA3 gene regulation.Activated p53 binds transcriptional regulatory regions of APOBECA3 gene.

12. These results highlight the fundamental impact of APOBEC3A overexpression on human transcriptome by widespread RNA editing.

13. High-level APOBEC3A expression is associated with better overall survival, especially among patients carrying APOBEC3B-deletion alleles in Taiwanese oral squamous cell carcinoma patients.

14. Our study demonstrates that 20% of C-->T and C-->G mutations in the TpCpW context-where W denotes A or T, segregating as polymorphisms in human population-or 1.4% of all heritable mutations are attributable to APOBEC3A/B activity.

15. findings reveal the role of A3A as a potent anti-Human cytomegalovirus (HCMV) innate barrier, activated by HCMV infection in the authentic tissues of the maternal-fetal interface. These findings pave the way to new insights into the potential impact of APOBEC proteins on HCMV pathogenesis.

16. APOBEC3A/B and HLA-DQA1 are powerful biomarkers for systemic sclerosis risk evaluation and contribute to the susceptibility to systemic sclerosis.

17. High APOBEC3A expression is associated with acute myelogenous leukemia.

18. Steady-state kinetic analysis reveals that APOBEC3A (A3A) discriminates against all ox-mCs by 3700-fold, arguing that ox-mC deamination does not contribute substantially to demethylation. A3A is, by contrast, highly proficient at C/mC deamination.

19. a solution-state model of APOBEC3A interaction with its single-stranded DNA substrate obtained with the 'method of small changes', is reported.

20. exposures to relevant environmental factors might induce APOBEC3A or APOBEC3B expression above genotoxic levels and initiate tumorigenesis in a tissue-specific manner in the right cellular environment where ssDNA is available