Selected article for: "cysteine cathepsin and glycan cap"

Author: Hunt, Catherine L.; Lennemann, Nicholas J.; Maury, Wendy
Title: Filovirus Entry: A Novelty in the Viral Fusion World
  • Document date: 2012_2_7
  • ID: 1j9zmuub_29
    Snippet: As endosomal vesicles mature into late endosomes and the vesicular pH drops, activation of endosomal cysteine proteases Cathepsin L and B occurs. These cathepsins sequentially process EBOV GP 1 into smaller forms [50, 51] . Cathepsin L proteolysis first removes a substantial portion of EBOV GP 1 , generating an approximate 50 kDa GP 1,2 species that lacks both the glycan cap and mucin domain of GP 1 [50, 51] . Subsequently, GP 1 is further trimme.....
    Document: As endosomal vesicles mature into late endosomes and the vesicular pH drops, activation of endosomal cysteine proteases Cathepsin L and B occurs. These cathepsins sequentially process EBOV GP 1 into smaller forms [50, 51] . Cathepsin L proteolysis first removes a substantial portion of EBOV GP 1 , generating an approximate 50 kDa GP 1,2 species that lacks both the glycan cap and mucin domain of GP 1 [50, 51] . Subsequently, GP 1 is further trimmed by both Cathepsin L and B to generate a much smaller form of GP 1 . The exact size of this smaller GP 1 remains controversial, but is between 17 and 19 kDa [50, 51] . Irrespective of the exact size of the processed form, prevention of endosomal acidification or inhibition of Cathepsin B activity abolishes EBOV infectivity [50] [51] [52] 70] .

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