Post-translational modifications (PTMs) are the modifications that occur to proteins after synthesis and are generated typically either by enzymatic mediation or autocatalytically and maybe reversible or irreversible. PTMs modulate protein function, folding, and trafficking through the attachment of small proteins, carbohydrates, lipids, or chemical groups to specific amino acids. One lesson learnt in virology is that PTMs of viral and cellular proteins actively regulate each step of a pathogen replication. The recent SARS-CoV-2 pandemic has recalled the attention on PTMs and virus replication cycle, and pathogenesis, highlighting the importance of PTMs in antiviral immune response, drug design and vaccine development.
During viral infections, PTMs play a multifaceted role that extends to all branches of the immune response. As an example, PTMs can alter proper T cell stimulation, protect neutralizing epitopes from the humoral response and dampen the interferon response. At the same time, PTMs can inactivate viral proteins or tag them for proteasomal degradation.
This Research Topic aims to advance research on virus pathogenesis, and inform novel pharmacological and vaccine approaches by examining PTMs at the virus-immune interface as central players in pathogenicity and evasion and, consequently, as potential pharmacological targets and immunogens.
We welcome the submission of Original Research, Review, Mini-Review, and Method articles that cover, but are not limited to, the following sub-topics:
• The influence of PTMs on viral infectivity and pathogenesis
• The effect of PTMs and PTM diversity on immune stimulation and disruption
• The role of PTMs in generating or regulating a neutralizing immune response
• How PTMs can inform vaccine or medical countermeasure development, with a for-ward-looking perspective on virus infection including SARS-CoV-2
• The roles of viral protein modification in viral infections using computational methods
Post-translational modifications (PTMs) are the modifications that occur to proteins after synthesis and are generated typically either by enzymatic mediation or autocatalytically and maybe reversible or irreversible. PTMs modulate protein function, folding, and trafficking through the attachment of small proteins, carbohydrates, lipids, or chemical groups to specific amino acids. One lesson learnt in virology is that PTMs of viral and cellular proteins actively regulate each step of a pathogen replication. The recent SARS-CoV-2 pandemic has recalled the attention on PTMs and virus replication cycle, and pathogenesis, highlighting the importance of PTMs in antiviral immune response, drug design and vaccine development.
During viral infections, PTMs play a multifaceted role that extends to all branches of the immune response. As an example, PTMs can alter proper T cell stimulation, protect neutralizing epitopes from the humoral response and dampen the interferon response. At the same time, PTMs can inactivate viral proteins or tag them for proteasomal degradation.
This Research Topic aims to advance research on virus pathogenesis, and inform novel pharmacological and vaccine approaches by examining PTMs at the virus-immune interface as central players in pathogenicity and evasion and, consequently, as potential pharmacological targets and immunogens.
We welcome the submission of Original Research, Review, Mini-Review, and Method articles that cover, but are not limited to, the following sub-topics:
• The influence of PTMs on viral infectivity and pathogenesis
• The effect of PTMs and PTM diversity on immune stimulation and disruption
• The role of PTMs in generating or regulating a neutralizing immune response
• How PTMs can inform vaccine or medical countermeasure development, with a for-ward-looking perspective on virus infection including SARS-CoV-2
• The roles of viral protein modification in viral infections using computational methods