HIV protease cleaves poly(A)-binding protein

Álvarez, E., Castello, A. , Menéndez-Arias, L. and Carrasco, L. (2006) HIV protease cleaves poly(A)-binding protein. Biochemical Journal, 396(2), pp. 219-226. (doi: 10.1042/BJ20060108) (PMID:16594896) (PMCID:PMC1462710)

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The PABP [poly(A)-binding protein] is able to interact with the 3′ poly(A) tail of eukaryotic mRNA, promoting its translation. Cleavage of PABP by viral proteases encoded by several picornaviruses and caliciviruses plays a role in the abrogation of cellular protein synthesis. We report that infection of MT-2 cells with HIV-1 leads to efficient proteolysis of PABP. Analysis of PABP integrity was carried out in BHK-21 (baby-hamster kidney) and COS-7 cells upon individual expression of the protease from several members of the Retroviridae family, e.g. MoMLV (Moloney murine leukaemia virus), MMTV (mouse mammary tumour virus), HTLV-I (human T-cell leukaemia virus type I), SIV (simian immunodeficiency virus), HIV-1 and HIV-2. Moreover, protease activity against PABP was tested in a HeLa-cell-free system. Only MMTV, HIV-1 and HIV-2 proteases were able to cleave PABP in the absence of other viral proteins. Purified HIV-1 and HIV-2 proteases cleave PABP1 directly at positions 237 and 477, separating the two first RNA-recognition motifs from the C-terminal domain of PABP. An additional cleavage site located at position 410 was detected for HIV-2 protease. These findings indicate that some retroviruses may share with picornaviruses and caliciviruses the capacity to proteolyse PABP.

Item Type:Articles
Glasgow Author(s) Enlighten ID:Castello, Professor Alfredo
Authors: Álvarez, E., Castello, A., Menéndez-Arias, L., and Carrasco, L.
College/School:College of Medical Veterinary and Life Sciences > School of Infection & Immunity
College of Medical Veterinary and Life Sciences > School of Infection & Immunity > Centre for Virus Research
Journal Name:Biochemical Journal
Publisher:Portland Press
ISSN (Online):1470-8728
Published Online:02 March 2006

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