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Related Experiment Videos

HIV protease cleaves poly(A)-binding protein.

Enrique Alvarez1, Alfredo Castelló, Luis Menéndez-Arias

  • 1Centro de Biología Molecular Severo Ochoa (CSIC-UAM), Facultad de Ciencias, Universidad Autónoma, Cantoblanco, 28049 Madrid, Spain. ealvarez@cnb.uam.es

The Biochemical Journal
|April 6, 2006
PubMed
Summary
This summary is machine-generated.

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Human immunodeficiency virus (HIV) proteases cleave poly(A)-binding protein (PABP), inhibiting cellular protein synthesis. This retroviral activity mirrors that seen with picornaviruses and caliciviruses.

Area of Science:

  • Virology
  • Molecular Biology
  • Biochemistry

Background:

  • Poly(A)-binding protein (PABP) is crucial for eukaryotic mRNA translation.
  • Viral proteases from picornaviruses and caliciviruses cleave PABP, inhibiting host protein synthesis.
  • Retroviruses, including HIV, were investigated for similar PABP cleavage activity.

Purpose of the Study:

  • To determine if HIV-1 and other retroviral proteases can cleave PABP.
  • To identify specific retroviral proteases responsible for PABP cleavage.
  • To characterize the cleavage sites on PABP by HIV proteases.

Main Methods:

  • Infection of cell lines (MT-2, BHK-21, COS-7) with HIV-1 and other Retroviridae members.
  • Expression of individual viral proteases in mammalian cells.

Related Experiment Videos

  • Cell-free protease activity assays using purified viral proteases.
  • Analysis of PABP integrity and identification of cleavage sites.

    • Main Results:

    • HIV-1 infection efficiently proteolyzed PABP in MT-2 cells.
    • Proteases from MMTV, HIV-1, and HIV-2 directly cleaved PABP in vitro.
    • HIV-1 and HIV-2 proteases cleaved PABP at specific positions (237, 477 for HIV-1; 237, 410, 477 for HIV-2).
    • Cleavage separated key RNA-recognition motifs from the PABP C-terminal domain.

    Conclusions:

    • Certain retroviruses, including HIV-1 and HIV-2, possess the capacity to proteolyze PABP.
    • This PABP cleavage mechanism is shared between retroviruses and other viral families like picornaviruses.
    • Viral PABP cleavage contributes to the abrogation of cellular protein synthesis during retroviral infection.