کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8304461 | 1538409 | 2016 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Nicotiana benthamiana cathepsin B displays distinct enzymatic features which differ from its human relative and aleurain-like protease
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کلمات کلیدی
MCAmAbCDRDTTpapain-like cysteine proteinase4-methylcoumaryl-7-amideCHN2PNGase FABZNicotiana benthamiana2-aminobenzoyl - 2-آمینوبن زیلALP - آلکالن فسفاتازMonoclonal antibody - آنتی بادی مونوکلونالEndo H - اندو هbenzyloxycarbonyl - بنزیلوسیکروبنیلdithiothreitol - دیتیوتریتولCysteine protease - سیستئین پروتئازComplementarity-determining region - منطقه تعریف کننده تکمیلیAntibody - پادتَن یا آنتیبادیProteolysis - پروتئولیزpeptide N-glycosidase F - پپتید N-گلیکوزیداز FCathepsin B - کاتئفسین BCathepsin - کاتپسینPlant - گیاه
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Nicotiana benthamiana cathepsin B displays distinct enzymatic features which differ from its human relative and aleurain-like protease Nicotiana benthamiana cathepsin B displays distinct enzymatic features which differ from its human relative and aleurain-like protease](/preview/png/8304461.png)
چکیده انگلیسی
The tobacco-related plant species Nicotiana benthamiana has recently emerged as a versatile expression platform for the rapid generation of recombinant biopharmaceuticals, but product yield and quality frequently suffer from unintended proteolysis. Previous studies have highlighted that recombinant protein fragmentation in plants involves papain-like cysteine proteinases (PLCPs). For this reason, we have now characterized two major N. benthamiana PLCPs in detail: aleurain-like protease (NbALP) and cathepsin B (NbCathB). As typical for PLCPs, the precursor of NbCathB readily undergoes autocatalytic activation when incubated at low pH. On the contrary, maturation of NbALP requires the presence of a cathepsin L-like PLCP as processing enzyme. While the catalytic features of NbALP closely resemble those of its mammalian homologue cathepsin H, NbCathB displays remarkable differences to human cathepsin B. In particular, NbCathB appears to be a far less efficient peptidyldipeptidase (removing C-terminal dipeptides) than its human counterpart, suggesting that it functions primarily as an endopeptidase. Importantly, NbCathB was far more efficient than NbALP in processing the human anti-HIV-1 antibody 2F5 into fragments observed during its production in N. benthamiana. This suggests that targeted down-regulation of NbCathB could improve the performance of this plant-based expression platform.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimie - Volume 122, March 2016, Pages 119-125
Journal: Biochimie - Volume 122, March 2016, Pages 119-125
نویسندگان
Melanie Niemer, Ulrich Mehofer, Maria Verdianz, Andreas Porodko, Philipp Schähs, Daniel Kracher, Brigita Lenarcic, Marko Novinec, Lukas Mach,