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Literature summary for 3.4.21.122 extracted from

  • Heurich, A.; Hofmann-Winkler, H.; Gierer, S.; Liepold, T.; Jahn, O.; Poehlmann, S.
    TMPRSS2 and ADAM17 cleave ACE2 differentially and only proteolysis by TMPRSS2 augments entry driven by the severe acute respiratory syndrome coronavirus spike protein (2014), J. Virol., 88, 1293-1307 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in HEK-293T and Cos-7 cell Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens O15393
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
angiotensin-converting enzyme 2 + H2O
-
Homo sapiens ?
-
?

General Information

General Information Comment Organism
physiological function ACE2 processing by TMPRSS2 or HAT is required for augmentation of SARS-S-driven entry. In contrast, ACE2 cleavage is dispensable for activation of the viral S protein. Expression of TMPRSS2 increases cellular uptake of soluble SARS-S. TMPRSS2 competes with the metalloprotease ADAM17 for ACE2 processing, but only cleavage by TMPRSS2 results in augmented SARS-S-driven entry Homo sapiens