Selected article for: "acid receptor and low pathogenic"

Author: Braun, Elisabeth; Sauter, Daniel
Title: Furin-mediated protein processing in infectious diseases and cancer
  • Document date: 2019_8_5
  • ID: k3m72uxw_22
    Snippet: 53 Both subunits remain linked via disulphide bonds and form trimeric structures. While HA 1 binds to the sialic acid receptor on viral target cells, HA 2 harbours the fusion peptide that mediates fusion of viral and cellular endosomal membranes. HA cleavage can occur within producer cells, upon release of virions from infected cells or directly prior to entry into new target cells. 54 As a general rule, hemagglutinins of mammalian and low pathog.....
    Document: 53 Both subunits remain linked via disulphide bonds and form trimeric structures. While HA 1 binds to the sialic acid receptor on viral target cells, HA 2 harbours the fusion peptide that mediates fusion of viral and cellular endosomal membranes. HA cleavage can occur within producer cells, upon release of virions from infected cells or directly prior to entry into new target cells. 54 As a general rule, hemagglutinins of mammalian and low pathogenic avian influenza A viruses cannot be cleaved by furin as they usually only harbour a mono-or dibasic cleavage site. Instead, they depend on trypsin-like proteases such as transmembrane protease serine S1 member 2 (TMPRSS2) or human airway trypsin-like protease (HAT). 55 Expression of such trypsin-like proteases is largely restricted to the respiratory and gastrointestinal tract.

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