About: The Proteolytic Activation of (H3N2) Influenza A Virus Hemagglutinin Is Facilitated by Different Type II Transmembrane Serine Proteases

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About: The Proteolytic Activation of (H3N2) Influenza A Virus Hemagglutinin Is Facilitated by Different Type II Transmembrane Serine Proteases Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	The Proteolytic Activation of (H3N2) Influenza A Virus Hemagglutinin Is Facilitated by Different Type II Transmembrane Serine Proteases
Creator	Pöhlmann, Stefan Kühn, Nora Schughart, Klaus Hatesuer, Bastian Bergmann, Silke Hummler, Edith Keppner, Anna Kösterke, Nadine Weiß, Siegfried Lambertz, Ruth Van Den Brand, Judith
Source	PMC
abstract	Cleavage of influenza virus hemagglutinin (HA) by host cell proteases is necessary for viral activation and infectivity. In humans and mice, members of the type II transmembrane protease family (TTSP), e.g., TMPRSS2, TMPRSS4, and TMPRSS11d (HAT), have been shown to cleave influenza virus HA for viral activation and infectivity in vitro. Recently, we reported that inactivation of a single HA-activating protease gene, Tmprss2, in knockout mice inhibits the spread of H1N1 influenza viruses. However, after infection of Tmprss2 knockout mice with an H3N2 influenza virus, only a slight increase in survival was observed, and mice still lost body weight. In this study, we investigated an additional trypsin-like protease, TMPRSS4. Both TMPRSS2 and TMPRSS4 are expressed in the same cell types of the mouse lung. Deletion of Tmprss4 alone in knockout mice does not protect them from body weight loss and death upon infection with H3N2 influenza virus. In contrast, Tmprss2(−/−) Tmprss4(−/−) double-knockout mice showed a remarkably reduced virus spread and lung pathology, in addition to reduced body weight loss and mortality. Thus, our results identified TMPRSS4 as a second host cell protease that, in addition to TMPRSS2, is able to activate the HA of H3N2 influenza virus in vivo. IMPORTANCE Influenza epidemics and recurring pandemics are responsible for significant global morbidity and mortality. Due to high variability of the virus genome, resistance to available antiviral drugs is frequently observed, and new targets for treatment of influenza are needed. Host cell factors essential for processing of the virus hemagglutinin represent very suitable drug targets because the virus is dependent on these host factors for replication. We reported previously that Tmprss2-deficient mice are protected against H1N1 virus infections, but only marginal protection against H3N2 virus infections was observed. Here we show that deletion of two host protease genes, Tmprss2 and Tmprss4, strongly reduced viral spread as well as lung pathology and resulted in increased survival after H3N2 virus infection. Thus, TMPRSS4 represents another host cell factor that is involved in cleavage activation of H3N2 influenza viruses in vivo.
has issue date	2016-04-14(xsd:dateTime)
bibo:doi	10.1128/jvi.02693-15
bibo:pmid	26889029
has license	cc-by
sha1sum (hex)	1bab633e4d3ab1ed30599369e8654c235256c5cd
schema:url	https://doi.org/10.1128/jvi.02693-15
resource representing a document's title	The Proteolytic Activation of (H3N2) Influenza A Virus Hemagglutinin Is Facilitated by Different Type II Transmembrane Serine Proteases
has PubMed Central identifier	PMC4836353
has PubMed identifier	26889029
schema:publication	J Virol
resource representing a document's body	covid:1bab633e4d3ab1ed30599369e8654c235256c5cd#body_text
is schema:about of	named entity 'H3N2' named entity 'body weight' named entity 'Tmprss2' named entity 'influenza' named entity 'additional' named entity 'lung' named entity 'knockout mice' named entity 'protease' covid:arg/1bab633e4d3ab1ed30599369e8654c235256c5cd named entity 'mice' named entity 'influenza' named entity 'cell types' named entity 'observed' named entity 'gene' named entity 'reduced' named entity 'virus' named entity 'H3N2' named entity 'body weight' named entity 'inhibits' named entity 'influenza virus' named entity 'H3N2' named entity 'trypsin' named entity 'knockout mice' named entity 'protease' named entity 'knockout mice' named entity 'TMPRSS4' named entity 'protease' named entity 'influenza virus' named entity 'mice' named entity 'TMPRSS2' named entity 'Tmprss2' named entity 'lung' named entity 'infectivity' named entity 'TMPRSS11d' named entity 'H3N2' named entity 'wild-type' named entity 'wild-type' named entity 'lungs' named entity 'infectivity' named entity 'wild-type' named entity 'macrophage inflammatory protein' named entity 'Affymetrix' named entity 'protein' named entity 'influenza' named entity 'cross-reactivity' named entity 'weight loss' named entity 'molecular mechanisms' named entity 'Tmprss4' named entity 'hepsin' named entity 'TMPRSS4' named entity 'nucleoprotein' named entity 'MCP1' named entity 'weight loss' named entity 'lung tissue' named entity 'Germany' named entity 'Tmprss2' named entity 'cleavage site' named entity 'life cycle' named entity 'bead' named entity 'paraffin blocks' named entity 'H3N2' named entity 'FFU' named entity 'cleavage site' named entity 'weight loss' named entity 'FFU' named entity 'University of Veterinary Medicine' named entity 'H1N1' named entity 'Tmprss2' named entity 'epithelial sodium channel' named entity 'proteases' named entity 'FFU'

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