Stefanie Gierer

TL;DR: It is shown that arginine and lysine residues within ACE2 amino acids 697 to 716 are essential for cleavage by TMPRSS2 and HAT and that ACE2 processing is required for augmentation of SARS-S-driven entry by these proteases.

TL;DR: The results show that TMPRSS2 and HAT are expressed by important influenza and SARS-coronavirus target cells and could thus support viral spread in the human host.

TL;DR: The proteolytic systems hijacked by SARS-CoV for S protein activation are reviewed, their contribution to viral spread in the host is discussed and antiviral strategies targeting these enzymes are outlined.

TL;DR: It is found that the spike protein of hCoV-EMC (EMC-S) is incorporated into lentiviral particles and mediates transduction of human cell lines derived from different organs, as well as primary human macrophages.

TL;DR: Results indicate that HCoV-229E can employ redundant proteolytic pathways to ensure its activation in host cells, and suggest that diverse human respiratory viruses are activated by TMPRSS2, which may constitute a target for antiviral intervention.