Publications by authors named "Linda Bittel"
Article Synopsis
- The study investigates the priming process of the Ebola virus (EBOV) glycoprotein GP involving furin and endosomal cathepsins but finds that furin cleavage isn't essential for the virus's ability to infect.
- It demonstrates that different cell lines utilize various proteases for the processing of EBOV GP, highlighting inconsistencies in how the virus enters different types of cells.
- The research reveals that an EBOV mutant lacking a furin cleavage site can still be activated by other proteases like TMPRSS2 and CatL, indicating the virus's adaptability and its dependency on proteolytic activation for entry into host cells.
Cleavage of influenza virus hemagglutinin (HA) by host proteases is essential for virus infectivity. HA of most influenza A and B (IAV/IBV) viruses is cleaved at a monobasic motif by trypsin-like proteases. Previous studies have reported that transmembrane serine protease 2 (TMPRSS2) is essential for activation of H7N9 and H1N1pdm IAV in mice but that H3N2 IAV and IBV activation is independent of TMPRSS2 and carried out by as-yet-undetermined protease(s).
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