Computationally designed peptide blocks the entry of SARS-CoV, SARS-CoV-2, and MERS-CoV
It is essential to face some grim facts about the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) pathogen. The ongoing COVID-19 (coronavirus disease 2019) pandemic, started in December 2019, may last for many years. SARS-CoV-2, the causative agent of COVID-19, is the seventh member of the
Coronaviridae family known to infect humans.
The SARS-CoV and MERS-CoV (Middle East respiratory syndrome coronavirus), two other members of this family, are the causative agents of the recent outbreaks of the SARS and MERS epidemics. Despite the two-decades-long interaction with these viruses, there is no therapeutic solution against the SARS, COVID-19, and MERS; only supportive care.
During the process of SARS-CoV-2 infection, once the virus penetrates the host cell, two open reading frames, ORF1a and ORF1ab, are translated. ORF1ab is responsible for the production of 16 nonstructural proteins (nsp). Several viral proteases such as 3CLpro and PLpro (papain-like protease) produce 1-16 nsps. A new study has been published in bioRxiv preprint server, which deals with identifying drugs that are effective as PLpro inhibitors.
New polypeptide could provide universal protection against coronaviruses
Researchers in the United States have developed an inhibitor of the spike protein found on the novel severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) that limits its formation in host human cells that would otherwise be the source of newly generated virions.
The SARS-CoV-2 virus is the agent responsible for the ongoing coronavirus disease 2019 (COVID-19) pandemic and the spike protein is the main structure the virus relies on for host cell entry.
Importantly, the inhibitor was effective against the spike proteins of other coronaviruses, including SARS-CoV-1 and Middle East respiratory syndrome CoV (MERS-CoV).
Researchers in the United States have developed “chimeric” vaccines that provided cross-protection against different strains of sarbecovirus in mice, including the novel severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) that causes coronavirus disease 2019 (COVID-19).
Study addresses glycosylation concerns in SARS-CoV-2 vaccine design
An international team of researchers has found that glycosylation patterns are conserved across the native spike protein of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) – the agent that causes coronavirus disease 2019 (COVID-19) – and the recombinant spike proteins made in laboratories for use in vaccines.
The spike protein, which SARS-CoV-2 uses to bind to and infect cells, is the main target of neutralizing antibodies following natural infection with the virus or vaccination.
A central tenet in vaccine design is the presentation of native-like antigens that will induce protective immunity. The abundance of N-linked glycans across the SARS-CoV-2 spike protein is a potential source of heterogeneity between the many different vaccine candidates under investigation, says Max Crispin from the University of Southampton in the UK and colleagues.