Selected article for: "disulfide bond and receptor binding"
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_4
    Snippet: Precursor GP is cleaved by the host enzyme furin in the Golgi apparatus, resulting in the formation of two GP subunits, GP 1 and GP 2 . GP 1 contains the receptor binding domain (RBD) and is responsible for interacting with one or more cellular receptors. This interaction is believed to mediate virus entry into the endosomal compartment. GP 2 contains a fusion loop, heptad repeat regions, the transmembrane domain and a short cytoplasmic tail. Whi.....
    Document: Precursor GP is cleaved by the host enzyme furin in the Golgi apparatus, resulting in the formation of two GP subunits, GP 1 and GP 2 . GP 1 contains the receptor binding domain (RBD) and is responsible for interacting with one or more cellular receptors. This interaction is believed to mediate virus entry into the endosomal compartment. GP 2 contains a fusion loop, heptad repeat regions, the transmembrane domain and a short cytoplasmic tail. While furin processing of the filovirus GP routinely occurs within the Golgi apparatus before the glycoprotein is expressed on the plasma membrane, proteolytic clipping is not required for virion infectivity [4] . The cleaved subunits are linked by a disulfide bond to generate a GP 1,2 heterodimer that is located on the surface of virions and is approximately 150 kDa in size [5] .

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