ArticlePloS one2016
The Hemagglutinin of Bat-Associated Influenza Viruses Is Activated by TMPRSS2 for pH-Dependent Entry into Bat but Not Human Cells.
Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 26 citations in OpenAlex.
- Article
- H19 influenza A virus exhibits species-specific MHC class II receptor usage.Cell host & microbe · 2024Article
- The M2 proteins of bat influenza A viruses reveal atypical features compared to conventional M2 proteins.Journal of virology · 2023Article
- Novel Molecular Consortia of Cannabidiol with Nonsteroidal Anti-Inflammatory Drugs Inhibit Emerging Coronaviruses' Entry.Pathogens (Basel, Switzerland) · 2023Article
- Molecular Evidence of Orthomyxovirus Presence in Colombian Neotropical Bats.Frontiers in microbiology · 2022Article
- Bat Influenza Viruses: Current Status and Perspective.Viruses · 2021Review
- Bat-Borne Influenza A Viruses: An Awakening.Cold Spring Harbor perspectives in medicine · 2021Review
- Breaking the Convention: Sialoglycan Variants, Coreceptors, and Alternative Receptors for Influenza A Virus Entry.Journal of virology · 2020Review
- Polymorphisms in dipeptidyl peptidase 4 reduce host cell entry of Middle East respiratory syndrome coronavirus.Emerging microbes & infections · 2020Article
- Assessment of risk conferred by coding and regulatory variations ofJournal of genetics · 2020Article
- Inferring the Urban Transmission Potential of Bat Influenza Viruses.Frontiers in cellular and infection microbiology · 2020Review
- Entry of the bat influenza H17N10 virus into mammalian cells is enabled by the MHC class II HLA-DR receptor.Nature microbiology · 2019Article
- TMPRSS2 Is the Major Activating Protease of Influenza A Virus in Primary Human Airway Cells and Influenza B Virus in Human Type II Pneumocytes.Journal of virology · 2019Article
- Mutations in the Spike Protein of Middle East Respiratory Syndrome Coronavirus Transmitted in Korea Increase Resistance to Antibody-Mediated Neutralization.Journal of virology · 2019Article
- Tools to study pathogen-host interactions in bats.Virus research · 2018Review
- Unexpected Functional Divergence of Bat Influenza Virus NS1 Proteins.Journal of virology · 2018Article
- Novel insights into bat influenza A viruses.The Journal of general virology · 2017Article
- A Polymorphism within the Internal Fusion Loop of the Ebola Virus Glycoprotein Modulates Host Cell Entry.Journal of virology · 2017Article
- Virion Background and Efficiency of Virion Incorporation Determine Susceptibility of Simian Immunodeficiency Virus Env-Driven Viral Entry to Inhibition by IFITM Proteins.Journal of virology · 2017Article
- Synthetically derived bat influenza A-like viruses reveal a cell type- but not species-specific tropism.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
New World bats have recently been discovered to harbor influenza A virus (FLUAV)-related viruses, termed bat-associated influenza A-like viruses (batFLUAV). The internal proteins of batFLUAV are functional in mammalian cells. In contrast, no biological functionality could be demonstrated for the surface proteins, hemagglutinin (HA)-like (HAL) and neuraminidase (NA)-like (NAL), and these proteins need to be replaced by their human counterparts to allow spread of batFLUAV in human cells. Here, we employed rhabdoviral vectors to study the role of HAL and NAL in viral entry. Vectors pseudotyped with batFLUAV-HAL and -NAL were able to enter bat cells but not cells from other mammalian species. Host cell entry was mediated by HAL and was dependent on prior proteolytic activation of HAL and endosomal low pH. In contrast, sialic acids were dispensable for HAL-driven entry. Finally, the type II transmembrane serine protease TMPRSS2 was able to activate HAL for cell entry indicating that batFLUAV can utilize human proteases for HAL activation. Collectively, these results identify viral and cellular factors governing host cell entry driven by batFLUAV surface proteins. They suggest that the absence of a functional receptor precludes entry of batFLUAV into human cells while other prerequisites for entry, HAL activation and protonation, are met in target cells of human origin.
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