EC Number   |
Application |
Reference |
|---|
  3.4.21.122 | analysis |
development of a cell-based fusion assay for the S protein in a TMPRSS2-dependent manner using cell lines expressing Renilla luciferase-based split reporter proteins. S-protein is stably expressed in the effector cells, and the corresponding receptor for S, CD26, is stably coexpressed with TMPRSS2 in the target cells. Membrane fusion between the effector and target cells is quantitatively measured by determining the Renilla luciferase activity. The assay is optimized for a 384-well format |
752507 |
| 3.4.21.122 | analysis |
use of TMPRSS2 to produce high titre influenza hemagglutixadnin lentiviral pseudotypes from Group 2 influenza viruses. These lentiviral pseudotypes transduce HEK293T/17 cells with high efficiency. The Group 2 influenza pseudotype particles can be used as surrogate antigens in neutralization assays and are efficiently neutralized by corresponding influenza virus reference sera |
754448 |
| 3.4.21.122 | medicine |
clinical isolates of coronaviruses HCoV-OC43 and -HKU1 prefer the cell-surface protease TMRRSS2 over endosomal cathepsins for host cell entry. Virus adaptation in cultured cells after isolation alters the route of cell entry and such modified isolates might not reflect the HCoVs of the natural world |
755649 |
| 3.4.21.122 | medicine |
clinical isolates of human coronavirus HCoV-229E are less likely to utilize cathepsin L for host cell entry. rather, they show a preference for TMPRSS2. Amino acid substitutions R642M and N714K in the S protein of HCoV-229E clinical isolates alter their sensitivity to a cathepsin L inhibitor. After 20 passages in HeLa cells, the ability of the isolate to use cathepsin increases, caused by amino acid substitution I577S in the S protein |
754555 |
| 3.4.21.122 | medicine |
cotransfection of mammalian cells with plasmids encoding hemagglutinin of influenza viruses and protease TMPRSS2 or human airway trypsin-like protease HAT results in hemagglutinin cleavage in situ. Transient expression of either protease in MDCK cells enables multicycle replication of influenza viruses in these cells in the absence of exogenous trypsin |
754527 |
| 3.4.21.122 | medicine |
in Vero cells expressing TMPRSS2, large syncytia are induced by SARS-CoV infection. Lysosome-tropic reagents fail to inhibit, whereas the heptad repeat peptide efficiently inhibits viral entry into cells. Production of virus in TMPRSS2-expressing cells does not result in S-protein cleavage or increased infectivity of the resulting virus. TMPRSS2 needs to be expressed in the opposing (target) cell membrane to activate S protein rather than in the producer cell |
754528 |
| 3.4.21.122 | medicine |
MDCK cells with inducible expression of either TMPRSS2 or protease HAT cells support growth of human and avian influenza viruses of different subtypes in the absence of exogenous trypsin. Multicycle viral replication in both cell lines is markedly suppressed in the presence of serine protease inhibitors |
755631 |
| 3.4.21.122 | medicine |
primary prostate cancer and prostate cancer metastases. TMPRSS2 expression is significantly higher in both neoplastic prostate and in the epithelium of prostatic hyperplasia compared to normal epithelium. TMPRSS2 expression is further elevated in higher Gleason grade cancers (patterns 4 and 5) compared to pattern 3. In most high-grade cancers, TMPRSS2 is mislocalized, being expressed in the cytoplasm as well as in the cell membrane |
753135 |
| 3.4.21.122 | medicine |
SARS spike (S) protein cleavage by TMPRSS2 decreases viral sensitivity to inhibition by neutralizing antibodies, and TMPRSS2-dependent SARS S shedding confers resistance against antibody-mediated neutralization. TMPRSS2 cleaves and activates SARS S in trans. TMPRSS2 on target cells allows efficient SARS S-driven virus-cell fusion in the presence of a lysosomotropic agent and a cathepsin inhibitor |
754532 |
| 3.4.21.122 | medicine |
the ability of TMPRSS2 to promote prostate cancer tumor growth and metastasis is associated with increased matriptase activation and enhanced degradation of extracellular matrix nidogen-1 and laminin beta1 in tumor xenografts |
753143 |
