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Literature DB >> 31099738

Tmprss2 knock-out mice are resistant to H10 influenza A virus pathogenesis.

Ruth L O Lambertz¹, Ingo Gerhauser², Inga Nehlmeier³, Sarah R Leist¹, Heike Kollmus¹, Stefan Pöhlmann^3,4, Klaus Schughart^1,5,6.

Abstract

The surface protein haemagglutinin (HA) of influenza A viruses (IAV) needs to be cleaved by a host protease to become functional. Here, we investigated if IAV of the H10 subtype also requires TMPRSS2 for replication and pathogenesis in mice. We first showed in cell culture that TMPRSS2 is able to cleave H10-HA. When Tmprss2-/- deficient mice were infected with a re-assorted virus H10-HA, they did not lose body weight and no viral replication was observed in contrast to wild-type mice. Histopathological analysis showed that inflammatory lesions in the lung of Tmprss2-/- mice were reduced compared to wild-type mice. In addition, no viral antigen was detected in the lungs of Tmprss2-/- mice and no evidence for HA cleavage was observed. We conclude from these studies that TMPRSS2 activity is also essential for in vivo replication and pathogenesis of H10 IAV.

Entities: Gene Species

Keywords: H10; Influenza A virus; TMPRSS2; host protease

Mesh：

Substances：

Year: 2019 PMID： 31099738 DOI： 10.1099/jgv.0.001274

Source DB: PubMed Journal: J Gen Virol ISSN： 0022-1317 Impact factor: 3.891

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Cited

13 in total

1. Hemagglutinin Cleavability, Acid Stability, and Temperature Dependence Optimize Influenza B Virus for Replication in Human Airways.

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Journal: J Virol Date: 2019-12-12 Impact factor: 5.103

2. Transcriptome profiling and protease inhibition experiments identify proteases that activate H3N2 influenza A and influenza B viruses in murine airways.

Authors: Anne Harbig; Marco Mernberger; Linda Bittel; Stephan Pleschka; Klaus Schughart; Torsten Steinmetzer; Thorsten Stiewe; Andrea Nist; Eva Böttcher-Friebertshäuser
Journal: J Biol Chem Date: 2020-04-17 Impact factor: 5.157

3. Epipharyngeal Abrasive Therapy Down-regulates the Expression of Cav1.2: A Key Molecule in Influenza Virus Entry.

Authors: Kensuke Nishi; Shohei Yoshimoto; Soichiro Nishi; Tatsuro Nishi; Ryushiro Nishi; Toshiyuki Tsunoda; Hiromitsu Morita; Hiroaki Tanaka; Osamu Hotta; Susumu Yasumasu; Kenji Hiromatsu; Senji Shirasawa; Takashi Nakagawa; Takafumi Yamano
Journal: In Vivo Date: 2022 Sep-Oct Impact factor: 2.406

4. Host serine proteases TMPRSS2 and TMPRSS11D mediate proteolytic activation and trypsin-independent infection in group A rotaviruses.

Authors: Michihito Sasaki; Yukari Itakura; Mai Kishimoto; Koshiro Tabata; Kentaro Uemura; Naoto Ito; Makoto Sugiyama; Christida E Wastika; Yasuko Orba; Hirofumi Sawa
Journal: J Virol Date: 2021-03-24 Impact factor: 6.549

Review 10. A Review on Expression, Pathological Roles, and Inhibition of TMPRSS2, the Serine Protease Responsible for SARS-CoV-2 Spike Protein Activation.

Authors: Jyotirmoy Sarker; Pritha Das; Sabarni Sarker; Apurba Kumar Roy; A Z M Ruhul Momen
Journal: Scientifica (Cairo) Date: 2021-07-24

Tmprss2 knock-out mice are resistant to H10 influenza A virus pathogenesis.

1. Hemagglutinin Cleavability, Acid Stability, and Temperature Dependence Optimize Influenza B Virus for Replication in Human Airways.

2. Transcriptome profiling and protease inhibition experiments identify proteases that activate H3N2 influenza A and influenza B viruses in murine airways.

3. Epipharyngeal Abrasive Therapy Down-regulates the Expression of Cav1.2: A Key Molecule in Influenza Virus Entry.

4. Host serine proteases TMPRSS2 and TMPRSS11D mediate proteolytic activation and trypsin-independent infection in group A rotaviruses.

5. H2 influenza A virus is not pathogenic in Tmprss2 knock-out mice.

Review 6. Leveraging 3D Model Systems to Understand Viral Interactions with the Respiratory Mucosa.

7. The Emergence and Zoonotic Transmission of H10Nx Avian Influenza Virus Infections.

8. Hemagglutinins of Avian Influenza Viruses Are Proteolytically Activated by TMPRSS2 in Human and Murine Airway Cells.

Review 9. Animal Models for Influenza Research: Strengths and Weaknesses.

Review 10. A Review on Expression, Pathological Roles, and Inhibition of TMPRSS2, the Serine Protease Responsible for SARS-CoV-2 Spike Protein Activation.