anti-Apolipoprotein B mRNA Editing Enzyme, Catalytic Polypeptide-Like 3H (APOBEC3H) Antibodies

Human Apolipoprotein B mRNA Editing Enzyme, Catalytic Polypeptide-Like 3H (APOBEC3H) interaction partners

1. Data demonstrate that the cellular RNA bound by APOBEC3H does not completely inhibit enzyme activity, in contrast to other APOBEC family members. Despite degradation of the cellular RNA, an approximately 12-nt RNA remains bound to the enzyme, even in the presence of ssDNA. The RNA-mediated dimer is disrupted by mutating W115 on loop 7 or R175 and R176 on helix 6, but this also disrupts protein stability.

2. Structure, Multimerization, Subcellular Localization and mC Selectivity of a Genomic Mutator and Anti-HIV Factor APOBEC3H

3. we reveal the 2.20-A crystal structure of the chimpanzee A3H (cpzA3H) dimer bound to a short double-stranded RNA (dsRNA), which appears to be similar to two recently reported structures of pig-tailed macaque A3H and human A3H

4. APOBEC3H has a structural zipcode for subcellular localization and selecting viral substrates for restriction.

5. Data show that splice variants SV200 is at least fourfold more HIV-1 restrictive than other apolipoprotein B mRNA editing enzyme catalytic polypeptide-like 3H APOBEC3H (A3H) splice variants.

6. the results support a model in which structured RNA negatively regulates the potentially harmful DNA deamination activity of APOBEC3H while, at the same time, positively regulating its antiviral activity.

7. These studies combine to suggest that A3B and A3H-I haplotypes, together, explain the bulk of 'APOBEC signature' mutations in cancer.

8. APOBEC3H role in the spontaneous control of HIV infection.

9. we speculate that stably expressed human A3H protects humans against the cross-species transmission of zoonotic infection of SIV of chimpanzee

10. Stable variants of APOBEC3H impose selective pressure on HIV-1.

11. The deamination activity of these APOBEC3H variants correlates well with their reported anti-HIV activity for the different haplotypes, suggesting that deaminase activity may be an important factor in determining their respective anti-HIV activities.

12. These results indicate that APOBEC3 proteins can be copackaged and can comutate the same genomes, and can cooperate to inhibit HIV replication.

13. There are 10 APOBEC3H residues required for the HIV-1 Vif susceptibility and Vif binding.

14. Haplotype analysis showed that the frequencies of 15del-105R was high (0.475 vs 0.400, OR=1.36, permutation P=0.037) in the HIV-1-infected subjects, confirming the association of A3H polymorphisms with the susceptibility to HIV-1 infection

15. The eQTL-missense polymorphisms of APOBEC3H are associated with lung cancer risk in a Han Chinese population

16. APOBEC3H haplotype II was able to processively deaminate multiple cytosines in a single enzyme-substrate encounter by using sliding, jumping, and intersegmental transfer movements.

17. The existence and persistence of both types of HIV-1 Vif variant suggests the importance of APOBEC3H suppression and cell cycle regulation for HIV-1's survival in vivo.

18. Importantly, APOBEC3H appears to use both deaminase-dependent and -independent mechanisms to target reverse transcription and restrict HIV-1 replication.

19. stable APOBEC3H haplotypes present as in vivo barriers to HIV-1 replication, that Vif is capable of adapting to these restrictive pressures, and that an evolutionary equilibrium has yet to be reached.

20. A3H with low anti-HIV-1 activity, APOBEC3H-hapC, is associated with the susceptibility to HIV-1 infection, whereas the A3H producing a stable protein, A3H-hapB, may confer a low risk of disease progression to AIDS.

Rhesus Monkey Apolipoprotein B mRNA Editing Enzyme, Catalytic Polypeptide-Like 3H (APOBEC3H) interaction partners

1. The arginine at position 14 of the SIV Vif is a critical residue for virus restriction by rhA3D, rhA3G and rhA3H.