Non-viral cellular substrates for human immunodeficiency virus type 1 protease

Shoeman, Robert L.; Kesselmeier, Cornelia; Mothes, Elfriede; Höner, Bernd; Traub, Peter

doi:10.1016/0014-5793(91)80116-K

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Non-viral cellular substrates for human immunodeficiency virus type 1 protease

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Shoeman, Robert L.
Coherent diffractive imaging, Max Planck Institute for Medical Research, Max Planck Society;
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;
Analytical Protein Biochemistry, Max Planck Institute for Medical Research, Max Planck Society;

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Shoeman, R. L., Kesselmeier, C., Mothes, E., Höner, B., & Traub, P. (1991). Non-viral cellular substrates for human immunodeficiency virus type 1 protease. FEBS Letters, 278(2), 199-203. doi:10.1016/0014-5793(91)80116-K.

Cite as: https://hdl.handle.net/21.11116/0000-0000-640F-0

Abstract

A computer search revealed 10 proteins with homology to the sequence we originally identified in vimentin as the site of cleavage by human immunodeficiency virus type 1 (HIV-1) protease. Of these 10 proteins (actin, alpha-actinin, spectrin, tropomyosins, vinculin, dystrophin, MAP-2, villin, TRK-1 and Ig mu-chain), we show that 4 of the first 5 were cleaved in vitro by this protease, as are MAP-1 and -2 [(1990) J. Gen. Virol. 71, 1985-1991]. In these proteins, cleavage is not restricted to a single motif, but occurs at many sites. However, cleavage is not random, since 9 other proteins including the cytoskeletal proteins filamin and band 4.1 are not cleaved in the in vitro assay. Thus, the ability of HIV-1 protease to cleave specific components of the cytoskeleton may be an important, although as yet unevaluated aspect of the life cycle of this retrovirus and/or may directly contribute to the pathogenesis observed during infection.