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Related Experiment Video

Updated: May 16, 2025

A Phenotyping Regimen for Genetically Modified Mice Used to Study Genes Implicated in Human Diseases of Aging

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DHX15 inhibits mouse APOBEC3 deamination.

Wenming Zhao¹, Ayan Modak¹, Susan R Ross¹

¹Department of Microbiology and Immunology, University of Illinois Chicago College of Medicine, Chicago, Illinois, United States of America.

|April 1, 2025

Summary

Mouse APOBEC3 (A3) protein

Area of Science:

Virology
Molecular Biology
Immunology

Background:

APOBEC3 proteins are crucial for innate immunity against viral infections.
Human APOBEC3 inactivates HIV-1 via cytidine deamination, but mouse APOBEC3 (mA3) does not effectively target murine retroviruses.
The mechanism behind mA3's limited antiviral activity remains unclear.

Purpose of the Study:

To investigate the interaction partners of mA3.
To elucidate the mechanism by which mA3's antiviral activity is regulated.
To understand the role of mA3 in host defense against murine retroviruses.

Main Methods:

Co-immunoprecipitation assays to identify mA3 interacting proteins.
In vitro cytidine deaminase activity assays.

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Murine leukemia virus (MLV) replication assays.

Western blotting and quantitative PCR for gene knockdown analysis.

Analysis of proviral DNA mutations and cellular DNA damage.

Main Results:

The dead box helicase DHX15 was identified as an interactor of mA3, inhibiting its deamination activity.
DHX15 is incorporated into MLV virions independently of mA3.
Knockdown of DHX15 enhanced MLV replication and increased G-to-A mutations in proviral DNA.
DHX15 knockdown led to DNA damage in murine cells.

Conclusions:

DHX15 negatively regulates mA3's antiviral cytidine deaminase activity.
DHX15 plays a role in MLV replication and potentially in maintaining genome integrity in cells expressing mA3.
Understanding the DHX15-mA3 interaction provides insights into host-pathogen interactions and retroviral restriction mechanisms.