hnRNPH1 Inhibits Influenza Virus Replication by Binding Viral RNA

Microorganisms, Journal Year: 2024, Volume and Issue: 13(1), P. 24 - 24

Published: Dec. 26, 2024

During the life cycle of influenza virus, viral RNPs (vRNPs) are transported to nucleus for replication. Given that a large number progeny RNA occupies nucleus, whether there is any host protein located in recognizes and inhibits replication remains largely unknown. In this study, explore role hnRNPH1 virus infection, we knocked down over-expressed proteins 293T cells, then infected cells with virus. The results showed H1N1 H9N2 viruses by restraining polymerase activity viruses. contains two recognition motifs (RRM1) RRM2. Further studies indicated specifically binds PB1, PA, NP genes. Mutation key residues tryptophan tyrosine RRM1 RRM2 abolished binding affinity suppression All suggested suppresses RNA.

Language: Английский

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Advances and Challenges in Antiviral Development for Respiratory Viruses

Pathogens, Journal Year: 2024, Volume and Issue: 14(1), P. 20 - 20

Published: Dec. 31, 2024

The development of antivirals for respiratory viruses has advanced markedly in response to the growing threat pathogens such as Influenzavirus (IAV), syncytial virus (RSV), and SARS-CoV-2. This article reviews advances challenges this field, highlighting therapeutic strategies that target critical stages viral replication cycle, including inhibitors entry, replication, assembly. In addition, innovative approaches inhibiting host cellular proteins reduce resistance repurposing existing drugs are explored, using bioinformatics tools optimize identification antiviral candidates. analysis also covers emerging technologies nanomedicine CRISPR gene editing, which promise improve stability efficacy treatments. While current offer valuable options, they face evolution need accessible treatments vulnerable populations. underscores importance continued innovation biotechnology overcome these limitations provide safe effective Combining traditional developing is essential order address diseases affect global health.

Language: Английский

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Decomposition of L-glutamine and accumulation of ammonium in cell culture media inhibit infectivity of influenza viruses

bioRxiv (Cold Spring Harbor Laboratory), Journal Year: 2024, Volume and Issue: unknown

Published: June 21, 2024

Abstract Cationic lysosomotropic molecules such as ammonium salts and chloroquine inhibit influenza A virus (IAV) infection in cell culture by counteracting endosomal acidification hampering viral-endosomal fusion. Here, we studied the effects of storage L-glutamine-supplemented media on accumulation inhibition IAV infection. The storage-related inhibitory effect was observed case DMEM OptiMEM media, but not RPMI medium, more pronounced for with pH-stable hemagglutinin. Our results highlight importance to consider potential presence virus-inhibiting agents and/or their production negative

Language: Английский

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Molecular dynamics investigation of the influenza hemagglutinin conformational changes in acidic pH

Published: July 10, 2024

The surface protein hemagglutinin (HA) of the influenza virus plays a pivotal role in facilitating viral infection by binding to sialic acid receptors on host cells. Its conformational state is pH-sensitive, impacting its receptor-binding ability and evasion immune response. In this study, we conducted extensive equilibrium microsecond-level all-atom molecular dynamics (MD) simulations HA explore influence low pH dynamics. Specifically, investigated impact protonation conserved histidine residues (His106

Language: Английский

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SARS-CoV-2 spike-based virus-like particles incorporate influenza H1/N1 antigens and induce dual immunity in mice

Vaccine, Journal Year: 2024, Volume and Issue: 42(26), P. 126463 - 126463

Published: Oct. 31, 2024

Language: Английский

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Molecular Dynamics Investigation of the Influenza Hemagglutinin Conformational Changes in Acidic pH

The Journal of Physical Chemistry B, Journal Year: 2024, Volume and Issue: 128(45), P. 11151 - 11163

Published: Nov. 4, 2024

The surface protein hemagglutinin (HA) of the influenza virus plays a pivotal role in facilitating viral infection by binding to sialic acid receptors on host cells. Its conformational state is pH-sensitive, impacting its receptor-binding ability and evasion immune response. In this study, we conducted extensive equilibrium microsecond-level all-atom molecular dynamics (MD) simulations HA explore influence low pH dynamics. Specifically, investigated impact protonation conserved histidine residues (H1062) located hinge region HA2. Our analysis encompassed comparisons between nonprotonated (NP), partially protonated (1P, 2P), fully (3P) conditions. findings reveal substantial pH-dependent alterations protein, affecting capability potential. Notably, form exhibits greater stability compared states. Conformational shifts central helices HA2 involve outward movement, counterclockwise rotation helices, fusion peptide release systems. Disruption hydrogen bonds drives release. Moreover, HA1 separation more likely system systems underscoring protonation. These insights shed light mechanisms may inform development novel antiviral drugs targeting pH-responsive drug delivery for influenza.

Language: Английский

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Decomposition of L-glutamine and accumulation of ammonium in cell culture media inhibit infectivity of influenza viruses

Virology, Journal Year: 2024, Volume and Issue: 602, P. 110314 - 110314

Published: Nov. 20, 2024

Language: Английский

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Synthesis and biological evaluation of substituted quinolines containing piperazine moieties against Influenza A virus

Bioorganic & Medicinal Chemistry Letters, Journal Year: 2024, Volume and Issue: unknown, P. 130081 - 130081

Published: Dec. 1, 2024

Language: Английский

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