Caspase-3-mediated cleavage of p65/RelA results in a carboxy-terminal fragment that inhibits IκBα and enhances HIV-1 replication in human T lymphocytes
2008

Caspase-3 Cleavage of p65/RelA Enhances HIV-1 Replication

publication Evidence: moderate

Author Information

Author(s): Mayte Coiras, María Rosa López-Huertas, Elena Mateos, José Alcamí

Primary Institution: AIDS Immunopathology Unit, National Center of Microbiology, Instituto de Salud Carlos III, Madrid, Spain

Hypothesis

The study investigates how caspase-3-mediated cleavage of p65/RelA affects NF-κB activity and HIV-1 replication in human T lymphocytes.

Conclusion

Caspase-3 cleavage of p65/RelA produces a fragment that enhances NF-κB activity and promotes HIV-1 replication in T cells.

Supporting Evidence

  • The study found that the carboxy-terminal fragment of p65/RelA could translocate to the nucleus and associate with NF-κB1/p50.
  • Increased levels of ΔNH2p65 were observed in the nuclei of activated T cells.
  • The expression of ΔNH2p65 resulted in enhanced HIV-1 replication in peripheral blood lymphocytes.

Takeaway

When a specific part of a protein called p65/RelA is cut by another protein called caspase-3, it helps the virus HIV-1 to grow better in certain immune cells.

Methodology

The study involved analyzing the effects of caspase-3-mediated cleavage of p65/RelA on NF-κB activity and HIV-1 replication in activated human T lymphocytes.

Participant Demographics

The study used human peripheral blood lymphocytes (PBLs) from healthy donors.

Digital Object Identifier (DOI)

10.1186/1742-4690-5-109

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