Publications by authors named "G Leser"
Influenza viruses are highly infectious and are the leading cause of human respiratory diseases and may trigger severe epidemics and occasional pandemics. Although antiviral drugs against influenza viruses have been developed, there is an urgent need to design new strategies to develop influenza virus inhibitors due to the increasing resistance of viruses toward currently available drugs. In this study, we examined the antiviral activity of natural compounds against the following influenza virus strains: A/WSN/33 (H1N1), A/Udorn/72 (H3N2), and B/Lee/40.
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- Parainfluenza virus 5 (PIV5) is an enveloped virus with a negative-strand RNA genome, and its replication is regulated by the phosphoprotein (P) interacting with the nucleoprotein (N) and RNA polymerase (L).
- The study reveals the crystal structure of unassembled PIV5 N in complex with a P-derived peptide, highlighting the structural organization of N into N-terminal and C-terminal domains and identifying a key RNA binding site.
- Findings show that the P peptide prevents N oligomerization and maintains N in an open form, crucial for RNA binding and release, which is vital for understanding paramyxovirus replication regulation.
Nipah virus is an emergent paramyxovirus that causes deadly encephalitis and respiratory infections in humans. Two glycoproteins coordinate the infection of host cells, an attachment protein (G), which binds to cell surface receptors, and a fusion (F) protein, which carries out the process of virus-cell membrane fusion. The G protein binds to ephrin B2/3 receptors, inducing G conformational changes that trigger F protein refolding.
View Article and Find Full Text PDFInfluenza virus assembles and buds at the plasma membrane of virus-infected cells. The viral proteins assemble at the same site on the plasma membrane for budding to occur. This involves a complex web of interactions among viral proteins.
View Article and Find Full Text PDFRespiratory syncytial virus (RSV) and human metapneumovirus (HMPV) are paramyxoviruses that are responsible for substantial human health burden, particularly in children and the elderly. The fusion (F) glycoproteins are major targets of the neutralizing antibody response and studies have mapped dominant antigenic sites in F. Here we grafted a major neutralizing site of RSV F, recognized by the prophylactic monoclonal antibody palivizumab, onto HMPV F, generating a chimeric protein displaying epitopes of both viruses.
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