Evidence map›Paper›PMID 25355867›Full record

ArticlePlant physiology2014

Proteolytic and N-glycan processing of human α1-antitrypsin expressed in Nicotiana benthamiana.

Alexandra Castilho, Markus Windwarder, Pia Gattinger, Lukas Mach, Richard Strasser, Friedrich Altmann, Herta Steinkellner

Open access · hybridAbstract read
In one paragraph

Article in Plant physiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
6.4field-weighted citation impact, top 4% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

39 citing papers in PubMed, 61 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. The Major Peanut Allergen Ara h 2 Produced inFrontiers in plant science · 2021
    Article
  18. Article
  19. β-Hexosaminidases Along the Secretory Pathway ofFrontiers in plant science · 2021
    Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 1 institution in 1 country.

Alexandra CastilhoDepartments of Applied Genetics and Cell Biology (A.C., P.G., L.M., R.S., H.S.) andChemistry (M.W., F.A.), University of Natural Resources and Life Sciences, 1190 Vienna, Austria.
Markus WindwarderDepartments of Applied Genetics and Cell Biology (A.C., P.G., L.M., R.S., H.S.) andChemistry (M.W., F.A.), University of Natural Resources and Life Sciences, 1190 Vienna, Austria.
Pia GattingerDepartments of Applied Genetics and Cell Biology (A.C., P.G., L.M., R.S., H.S.) andChemistry (M.W., F.A.), University of Natural Resources and Life Sciences, 1190 Vienna, Austria.
Lukas MachDepartments of Applied Genetics and Cell Biology (A.C., P.G., L.M., R.S., H.S.) andChemistry (M.W., F.A.), University of Natural Resources and Life Sciences, 1190 Vienna, Austria.
Richard StrasserDepartments of Applied Genetics and Cell Biology (A.C., P.G., L.M., R.S., H.S.) andChemistry (M.W., F.A.), University of Natural Resources and Life Sciences, 1190 Vienna, Austria.
Friedrich AltmannDepartments of Applied Genetics and Cell Biology (A.C., P.G., L.M., R.S., H.S.) andChemistry (M.W., F.A.), University of Natural Resources and Life Sciences, 1190 Vienna, Austria.
Herta SteinkellnerDepartments of Applied Genetics and Cell Biology (A.C., P.G., L.M., R.S., H.S.) andChemistry (M.W., F.A.), University of Natural Resources and Life Sciences, 1190 Vienna, Austria herta.steinkellner@boku.ac.at.
BOKU University · AT

Funding

Austrian Science Fund FWF L 575
6 · The paper itself

Abstract

Plants are increasingly being used as an expression system for complex recombinant proteins. However, our limited knowledge of the intrinsic factors that act along the secretory pathway, which may compromise product integrity, renders process design difficult in some cases. Here, we pursued the recombinant expression of the human protease inhibitor α1-antitrypsin (A1AT) in Nicotiana benthamiana. This serum protein undergoes intensive posttranslational modifications. Unusually high levels of recombinant A1AT were expressed in leaves (up to 6 mg g(-1) of leaf material) in two forms: full-length A1AT located in the endoplasmic reticulum displaying inhibitory activity, and secreted A1AT processed in the reactive center loop, thus rendering it unable to interact with target proteinases. We found that the terminal protein processing is most likely a consequence of the intrinsic function of A1AT (i.e. its interaction with proteases [most likely serine proteases] along the secretory pathway). Secreted A1AT carried vacuolar-type paucimannosidic N-glycans generated by the activity of hexosaminidases located in the apoplast/plasma membrane. Notwithstanding, an intensive glycoengineering approach led to secreted A1AT carrying sialylated N-glycan structures largely resembling its serum-derived counterpart. In summary, we elucidate unique insights in plant glycosylation processes and show important aspects of postendoplasmic reticulum protein processing in plants.

Indexed as

Protein Processing, Post-Translationalalpha 1-AntitrypsinBiological TransportCell MembraneEndoplasmic ReticulumGene ExpressionGlycosylationHumansNicotianaPlant LeavesPolysaccharidesProteolysisRecombinant ProteinsSecretory PathwaySerine ProteasesSerine Proteinase Inhibitorsalpha 1-AntitrypsinPolysaccharidesRecombinant ProteinsSerine ProteasesSerine Proteinase Inhibitors

Identifiers

PMID25355867
PMCPMC4256845
OpenAlexW1992961087

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.