Key result
HIV-1 and HIV-2 proteases directly cleave poly(A)-binding protein (PABP) at specific positions, indicating a shared capacity with other viruses to proteolyse PABP.
Population
MT-2 cells, BHK-21 (baby-hamster kidney) cells, COS-7 cells, and a HeLa-cell-free system
Design
Preclinical
Authors
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Extends PABP cleavage to HIV proteases in vitro; hypothesis-generating for retroviral host shutoff and requires human validation.
HIV-1, HIV-2, and MMTV proteases can directly cleave poly(A)-binding protein, suggesting retroviruses share mechanisms with picornaviruses and caliciviruses to abrogate cellular protein synthesis.
Álvarez et al. (2006) studied HIV infection. HIV-1 and HIV-2 proteases vs. Other retroviral proteases was evaluated on Cleavage of PABP. HIV-1 and HIV-2 proteases directly cleave poly(A)-binding protein (PABP) at specific positions, indicating a shared capacity with other viruses to proteolyse PABP.
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