A catalogue of putative HIV-1 protease host cell substrates
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Francis Impens
Abstract
Processing of human immunodeficiency virus (HIV) proteins by the HIV-1 protease is essential for HIV infectivity. In addition, several studies have revealed cleavage of human proteins by this viral protease during infection; however, no large-scale HIV-1 protease degradomics study has yet been performed. To identify putative host substrates in an unbiased manner and on a proteome-wide scale, we used positional proteomics to identify peptides reporting protein processing by the HIV-1 protease, and a catalogue of over 120 cellular HIV-1 protease substrates processed in vitro was generated. This catalogue includes previously reported substrates as well as recently described interaction partners of HIV-1 proteins. Cleavage site alignments revealed a specificity profile in good correlation with previous studies, even though the ELLE consensus motif was not cleaved efficiently when incorporated into peptide substrates due to subsite cooperativity. Our results are further discussed in the context of HIV-1 infection and the complex substrate recognition by the viral protease.
©2012 by Walter de Gruyter Berlin Boston
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Articles in the same Issue
- Masthead
- Masthead
- Guest Editorial
- Highlight: The universe of proteolytic networks and mechanisms
- Highlight: 7th General Meeting of the International Proteolysis Society
- Current and prospective applications of non-proteinogenic amino acids in profiling of proteases substrate specificity
- Understanding the substrate specificity of conventional calpains
- Protease-dependent mechanisms of complement evasion by bacterial pathogens
- An ensemble view of thrombin allostery
- Processive proteolysis by γ-secretase and the mechanism of Alzheimer’s disease
- TMPRSS4 is a type II transmembrane serine protease involved in cancer and viral infections
- A catalogue of putative HIV-1 protease host cell substrates
- Identifi cation of protease exosite-interacting peptides that enhance substrate cleavage kinetics
- A plant Kunitz-type inhibitor mimics bradykinin-induced cytosolic calcium increase and intestinal smooth muscle contraction
- Characterisation and metabolism of astroglia-rich primary cultures from cathepsin K-deficient mice
- Disruption of gingipain oligomerization into non-covalent cell-surface attached complexes
- Review
- Synthesis and biological actions of diphosphoinositol phosphates (inositol pyrophosphates), regulators of cell homeostasis
- Minireviews
- Redox Biology on the rise
- Adipose triglyceride lipase in immune response, inflammation, and atherosclerosis
- Research Articles/Short Communications
- Protein Structure and Function
- Insights into the modulation of optimum pH by a single histidine residue in arginine deiminase from Pseudomonas aeruginosa
