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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Paireder, Melanie Biniossek, Martin L. Porodko, Andreas Mayer, Bettina Mach, Lukas Novinec, Marko Schilling, Oliver Tholen, Stefan |
| Description | Author Affiliation: Paireder M ( Department of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Vienna, Austria.); Tholen S ( Institute for Molecular Medicine and Cell Research, University of Freiburg, Germany.); Porodko A ( Department of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Vienna, Austria.); Biniossek ML ( Institute for Molecular Medicine and Cell Research, University of Freiburg, Germany.); Mayer B ( Institute for Molecular Medicine and Cell Research, University of Freiburg, Germany.); Novinec M ( Department of Chemistry and Biochemistry, Faculty of Chemistry and Chemical Technology, University of Ljubljana, Slovenia.); Schilling O ( Institute for Molecular Medicine and Cell Research, University of Freiburg, Germany); Mach L ( Department of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Vienna, Austria. Electronic address: lukas.mach@boku.ac.at.) |
| Abstract | The tobacco-related plant Nicotiana benthamiana is gaining interest as a versatile host for the production of monoclonal antibodies and other protein therapeutics. However, the susceptibility of plant-derived recombinant proteins to endogenous proteolytic enzymes limits their use as biopharmaceuticals. We have now identified two previously uncharacterized N. benthamiana proteases with high antibody-degrading activity, the papain-like cysteine proteinases NbCysP6 and NbCysP7. Both enzymes are capable of hydrolysing a wide range of synthetic substrates, although only NbCysP6 tolerates basic amino acids in its specificity-determining S2 subsite. The overlapping substrate specificities of NbCysP6 and NbCysP7 are also documented by the closely related properties of their other subsites as deduced from the action of the enzymes on proteome-derived peptide libraries. Notable differences were observed to the substrate preferences of N. benthamiana cathepsin B, another antibody-degrading papain-like cysteine proteinase. The complementary activities of NbCysP6, NbCysP7 and N. benthamiana cathepsin B indicate synergistic roles of these proteases in the turnover of recombinant and endogenous proteins in planta, thus representing a paradigm for the shaping of plant proteomes by the combined action of papain-like cysteine proteinases. |
| ISSN | 00063002 |
| Journal | Biochimica et Biophysica Acta (BBA) - Reviews on Cancer |
| Issue Number | 4 |
| Volume Number | 1865 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2017-04-01 |
| Publisher Place | Netherlands |
| Access Restriction | Open |
| Subject Keyword | Biochemistry |
| Content Type | Text |
| Resource Type | Article |
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