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TMPRSS2 Isoform 1 Activates Respiratory Viruses and Is Expressed in Viral Target Cells
by
Moldenhauer, Anna-Sophie
, Zmora, Pawel
, Hofmann-Winkler, Heike
, Pöhlmann, Stefan
in
Activation
/ Alternative splicing
/ Amino acids
/ Animals
/ Biology
/ Caco-2 Cells
/ Cathepsin L
/ Cathepsins - metabolism
/ Cell Line
/ Cell lines
/ Cercopithecus aethiops
/ Cloning
/ Coronaviridae
/ Coronaviruses
/ COS Cells
/ Genes
/ Health aspects
/ HEK293 Cells
/ Hemagglutinins
/ Hemagglutinins - metabolism
/ Hepatitis
/ Host-Pathogen Interactions - physiology
/ Humans
/ Infections
/ Influenza
/ Influenza viruses
/ Isoforms
/ Lectins
/ Lung - metabolism
/ Lung - virology
/ Lungs
/ mRNA
/ Orthomyxoviridae - metabolism
/ Pandemics
/ Pathogenesis
/ Plasmids
/ Proteases
/ Protein Isoforms - metabolism
/ Proteins
/ Respiratory diseases
/ RNA
/ RNA, Messenger - metabolism
/ SARS Virus - metabolism
/ Serine Endopeptidases - metabolism
/ Severe acute respiratory syndrome
/ Spike Glycoprotein, Coronavirus - metabolism
/ Spike protein
/ Viral infections
/ Virus Internalization
/ Viruses
2015
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TMPRSS2 Isoform 1 Activates Respiratory Viruses and Is Expressed in Viral Target Cells
by
Moldenhauer, Anna-Sophie
, Zmora, Pawel
, Hofmann-Winkler, Heike
, Pöhlmann, Stefan
in
Activation
/ Alternative splicing
/ Amino acids
/ Animals
/ Biology
/ Caco-2 Cells
/ Cathepsin L
/ Cathepsins - metabolism
/ Cell Line
/ Cell lines
/ Cercopithecus aethiops
/ Cloning
/ Coronaviridae
/ Coronaviruses
/ COS Cells
/ Genes
/ Health aspects
/ HEK293 Cells
/ Hemagglutinins
/ Hemagglutinins - metabolism
/ Hepatitis
/ Host-Pathogen Interactions - physiology
/ Humans
/ Infections
/ Influenza
/ Influenza viruses
/ Isoforms
/ Lectins
/ Lung - metabolism
/ Lung - virology
/ Lungs
/ mRNA
/ Orthomyxoviridae - metabolism
/ Pandemics
/ Pathogenesis
/ Plasmids
/ Proteases
/ Protein Isoforms - metabolism
/ Proteins
/ Respiratory diseases
/ RNA
/ RNA, Messenger - metabolism
/ SARS Virus - metabolism
/ Serine Endopeptidases - metabolism
/ Severe acute respiratory syndrome
/ Spike Glycoprotein, Coronavirus - metabolism
/ Spike protein
/ Viral infections
/ Virus Internalization
/ Viruses
2015
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TMPRSS2 Isoform 1 Activates Respiratory Viruses and Is Expressed in Viral Target Cells
by
Moldenhauer, Anna-Sophie
, Zmora, Pawel
, Hofmann-Winkler, Heike
, Pöhlmann, Stefan
in
Activation
/ Alternative splicing
/ Amino acids
/ Animals
/ Biology
/ Caco-2 Cells
/ Cathepsin L
/ Cathepsins - metabolism
/ Cell Line
/ Cell lines
/ Cercopithecus aethiops
/ Cloning
/ Coronaviridae
/ Coronaviruses
/ COS Cells
/ Genes
/ Health aspects
/ HEK293 Cells
/ Hemagglutinins
/ Hemagglutinins - metabolism
/ Hepatitis
/ Host-Pathogen Interactions - physiology
/ Humans
/ Infections
/ Influenza
/ Influenza viruses
/ Isoforms
/ Lectins
/ Lung - metabolism
/ Lung - virology
/ Lungs
/ mRNA
/ Orthomyxoviridae - metabolism
/ Pandemics
/ Pathogenesis
/ Plasmids
/ Proteases
/ Protein Isoforms - metabolism
/ Proteins
/ Respiratory diseases
/ RNA
/ RNA, Messenger - metabolism
/ SARS Virus - metabolism
/ Serine Endopeptidases - metabolism
/ Severe acute respiratory syndrome
/ Spike Glycoprotein, Coronavirus - metabolism
/ Spike protein
/ Viral infections
/ Virus Internalization
/ Viruses
2015
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TMPRSS2 Isoform 1 Activates Respiratory Viruses and Is Expressed in Viral Target Cells
Journal Article
TMPRSS2 Isoform 1 Activates Respiratory Viruses and Is Expressed in Viral Target Cells
2015
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Overview
The cellular protease TMPRSS2 cleaves and activates the influenza virus hemagglutinin (HA) and TMPRSS2 expression is essential for viral spread and pathogenesis in mice. Moreover, severe acute respiratory syndrome coronavirus (SARS-CoV) and other respiratory viruses are activated by TMPRSS2. However, previous studies on viral activation by TMPRSS2 focused on a 492 amino acids comprising form of the protein (isoform 2) while other TMPRSS2 isoforms, generated upon alternative splicing of the tmprss2 mRNA, have not been characterized. Here, we show that the mRNA encoding a TMPRSS2 isoform with an extended N-terminal cytoplasmic domain (isoform 1) is expressed in lung-derived cell lines and tissues. Moreover, we demonstrate that TMPRSS2 isoform 1 colocalizes with HA and cleaves and activates HA. Finally, we show that isoform 1 activates the SARS-CoV spike protein for cathepsin L-independent entry into target cells. Our results indicate that TMPRSS2 isoform 1 is expressed in viral target cells and might contribute to viral activation in the host.
Publisher
Public Library of Science,Public Library of Science (PLoS)
Subject
/ Animals
/ Biology
/ Cloning
/ Genes
/ Host-Pathogen Interactions - physiology
/ Humans
/ Isoforms
/ Lectins
/ Lungs
/ mRNA
/ Orthomyxoviridae - metabolism
/ Plasmids
/ Protein Isoforms - metabolism
/ Proteins
/ RNA
/ Serine Endopeptidases - metabolism
/ Severe acute respiratory syndrome
/ Spike Glycoprotein, Coronavirus - metabolism
/ Viruses
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