Selected article for: "cleavage site and precise site"

Author: Aleksandra Milewska; Katherine Falkowski; Magdalena Kalinska; Ewa Bielecka; Antonina Naskalska; Pawel Mak; Adam Lesner; Marek Ochman; Maciej Urlik; Jan Potempa; Tomasz Kantyka; Krzysztof Pyrc
Title: Kallikrein 13: a new player in coronaviral infections
  • Document date: 2020_3_2
  • ID: 6om1y33o_16
    Snippet: Most coronaviral S proteins are processed into S1 and S2 subunits by host proteases, The copyright holder for this preprint (which was not peer-reviewed) is the . https://doi.org/10.1101/2020.03.01.971499 doi: bioRxiv preprint HCoV-HKU1 S protein has two regions that are prone to proteolytic activation: the S1/S2 furin 330 cleavage site and a secondary cleavage site termed S2', which is adjacent to a potential fusion 331 peptide (38). While the S.....
    Document: Most coronaviral S proteins are processed into S1 and S2 subunits by host proteases, The copyright holder for this preprint (which was not peer-reviewed) is the . https://doi.org/10.1101/2020.03.01.971499 doi: bioRxiv preprint HCoV-HKU1 S protein has two regions that are prone to proteolytic activation: the S1/S2 furin 330 cleavage site and a secondary cleavage site termed S2', which is adjacent to a potential fusion 331 peptide (38). While the S1/S2 site is believed to be processed by furin during protein 332 biosynthesis, the S2/S2' site is expected to be cleaved during virus entry. As we already knew being tested. We found that the S1/S2 site was efficiently cleaved by KLK13, whereas the 338 S2/S2' region remained intact. As CleavEx technique is a convenient surrogate system allowing 339 for precise mapping of the cleavage site, it has some limitations. To ensure the reliability of 340 results, purified full-length HCoV-HKU1 S protein was subjected to the proteolytic cleavage.

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