Several highly pathogenic viruses, including SARS-CoV-2, share a conserved mechanism of infection via the fusion of the viral and host membranes employing a six-helix bundle (6-HB) heptad repeat.
Researchers from Universidade Federal de Minas Gerais have published details on the discovery of novel anti-SARS-CoV-2 compounds with robust antiviral activity.
The COVID-19 virus may keep mutating, but new findings from Korean researchers at the Institute of Basic Science (IBS) offer a silver lining: human immunity is adapting, too.
Researchers at ETH Zurich have identified a proteomic signature that could recognize long COVID six months after acute infection. Biologically, the signature indicated that the complement system remained active in patients with long COVID six months after infection. Translationally, it could lead to a diagnostic test for long COVID, and suggests that targeting the complement system could be a therapeutic approach to prevent or treat the disorder.
Exevir Bio BV has released new data demonstrating that its antibodies are highly potent in neutralizing currently circulating COVID-19 omicron variants.
Trawsfynydd Therapeutics Inc. has identified 3C-like proteinase (3CLpro; Mpro; nsp5) (SARS-CoV-2; COVID-19) inhibitors reported to be useful for the treatment of SARS-CoV-2 infection (COVID-19).
University of Alberta has divulged 3C-like proteinase (3CLpro; Mpro; nsp5) (SARS-CoV-2; COVID-19 virus) inhibitors reported to be useful for the treatment of viral infections.
University of Minnesota has divulged nonstructural protein 14 (NSP14) (SARS-CoV-2) inhibitors reported to be useful for the treatment of SARS-CoV-2 infection.
In a study published in Antiviral Research, researchers from the Max Planck Institute for Multidisciplinary Sciences and collaborators have presented optimized nanobodies targeting the receptor binding domain (RBD) of the SARS-CoV-2 spike protein.
The Nobel Prize-winning modification that prevents the innate immune system from recognizing injected mRNA as foreign and blocking transcription of the protein it encodes has been found on some occasions to cause ribosomal frameshifting.