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TMPRSS2 Isoform 1 Activates Respiratory Viruses and Is Expressed in Viral Target Cells

Pawel Zmora1, Anna-Sophie Moldenhauer1, Heike Hofmann-Winkler1

  • 1Infection Biology Unit, German Primate Center, Göttingen, Germany.

Plos One
|September 18, 2015
PubMed

Insights

A newly identified TMPRSS2 isoform (isoform 1) activates influenza and SARS-CoV viruses. This protease is expressed in lung cells and plays a role in viral activation within hosts.

Area of Science:

  • Biochemistry
  • Virology
  • Molecular Biology

Background:

  • The cellular protease TMPRSS2 activates influenza virus hemagglutinin (HA) and is crucial for viral spread.
  • TMPRSS2 also activates other respiratory viruses like SARS-CoV.
  • Previous research focused on TMPRSS2 isoform 2, neglecting other isoforms generated by alternative splicing.

Purpose of the Study:

  • To characterize novel TMPRSS2 isoforms involved in viral activation.
  • To investigate the role of TMPRSS2 isoform 1 in activating influenza and SARS-CoV.

Main Methods:

  • Expression analysis of TMPRSS2 isoforms in lung cells and tissues.
  • Colocalization studies of TMPRSS2 isoform 1 with viral proteins.
  • Functional assays to assess the cleavage and activation of viral proteins by TMPRSS2 isoform 1.

Main Results:

  • TMPRSS2 isoform 1, featuring an extended N-terminal cytoplasmic domain, is expressed in lung-derived cells and tissues.
  • TMPRSS2 isoform 1 colocalizes with influenza HA and effectively cleaves and activates it.
  • TMPRSS2 isoform 1 facilitates cathepsin L-independent entry of SARS-CoV into target cells.

Conclusions:

  • TMPRSS2 isoform 1 is present in cells targeted by respiratory viruses.
  • This isoform contributes to the activation of influenza and SARS-CoV, impacting viral pathogenesis.
  • Further research into TMPRSS2 isoforms is warranted for understanding viral activation mechanisms.

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