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APOBEC3 multimerization correlates with HIV-1 packaging and restriction activity in living cells
Jinhui Li1, Yan Chen1, Ming Li2
1School of Physics and Astronomy, University of Minnesota, 116 Church Street Southeast, Minneapolis, MN 55455, USA; Institute for Molecular Virology, University of Minnesota, 515 Delaware Street Southeast, Minneapolis, MN 55455, USA.
Journal of Molecular Biology
|December 24, 2013
Summary
APOBEC3G protein multimerization, not just enzymatic activity, is key for restricting human immunodeficiency virus type 1 (HIV-1) infectivity. This oligomerization influences packaging into viral particles, a crucial step for effective virus restriction.
Area of Science:
- Biochemistry
- Virology
- Molecular Biology
Background:
- APOBEC3G is a DNA cytosine deaminase critical for restricting retroviruses like HIV-1.
- HIV-1 restriction involves virion packaging and viral cDNA deamination.
- APOBEC3G's oligomerization relevance to restriction was previously unclear.
Purpose of the Study:
- To investigate the role of APOBEC3 protein oligomerization in HIV-1 restriction.
- To determine if APOBEC3 oligomerization correlates with virion packaging and antiviral activity.
Main Methods:
- Molecular brightness analysis in living cells to assess APOBEC3 oligomerization.
- Testing various APOBEC3 family members (APOBEC3A, 3B, 3C, 3D, 3F, 3G, 3H) and APOBEC2.
- Utilizing APOBEC3G mutants deficient in multimerization.
Main Results:
- APOBEC3G forms high-order multimers dependent on protein concentration.
- APOBEC3A, 3C, and 2 exist as monomers; 3B, 3D, 3F, and 3H (haplotype II) resemble APOBEC3G's multimerization.
- Multimerizing APOBEC3 proteins, unlike monomers, package into HIV-1 particles and restrict infectivity.
- APOBEC3G mutants compromised in multimerization also showed defects in packaging and restriction.
Conclusions:
- APOBEC3 protein oligomerization is strongly correlated with HIV-1 packaging and restriction.
- Multimerization may be a prerequisite for packaging into HIV-1 virions.
- The findings suggest a mechanism where APOBEC3 oligomerization facilitates viral restriction.
