Health
Prospects for COVID-19 drugs boosted by the discovery of a short form of coronavirus “entry point”
Colored scanning electron micrographs of apoptotic cells (green) strongly infected with SARS-COV-2 virus particles (yellow) isolated from patient samples. Image taken at the NIAID Integrated Research Facility (IRF) in Fort Detrick, Maryland. Credit: NIH / NIAID
The shadow of promising inhaled interferon beta COVID-19 therapy appears to increase levels of the ACE2 protein, an important entrance to coronavirus nasal and lung cells, but primarily increases levels of its short version. Cleared by discovery. A protein that the virus cannot bind to.
The virus that causes COVID-19, known as SARS-CoV-2, invades nasal and lung cells by binding spike proteins to the cell surface protein angiotensin converting enzyme 2 (ACE2).
Currently, a new short form of ACE2 has been identified by Professors Jane Lucas, Donna Davies, Gabrielle Wheway, and Vito Mennella of the University of Southampton and the NHS Foundation Trust at the University of Southampton Hospital.
Research published in Nature geneticsIndicates that there is a short form of ACE2 that lacks the SARS-CoV-2 binding site, similar to the long form of ACE2 used by SARS-CoV-2.
A naturally occurring antiviral protein called interferon Showed a promise In the treatment of COVID-19. However, previous studies have shown that interferon increases ACE2 levels. When the potential for such treatments is questioned and ACE2 increases, these drugs can actually exacerbate the effects of COVID-19.
However, this latest study shows that the increase in response to interferon is primarily short ACE2, which lacks a viral binding site. Interferons do not appear to boost the entry point of the virus, as the levels of longer forms of ACE2 remain unchanged, supporting their use in the treatment of COVID-19 patients.
This helps explain the very promising results of the inhalation test interferon Beta treatment of COVID-19 patients developed in Southampton by a team led by Professor Tom Wilkinson of the University of Southampton.
This study provides new insights into this short form of ACE2 and shows that it plays a very different role than the long form of ACE2, which serves as an entry point for SARS-CoV-2.
The short ACE2 does not have a SARS-CoV-2 binding site and cannot be used as a virus entry point. Instead, its regulation by interferon suggests that it may be involved in the body’s antiviral response.
Researchers have shown that short ACE2 does not increase in response to SARS-CoV-2 infection, so it is unlikely to be involved in the body’s immune response to COVID-19, but another common respiratory system. Increased in response to the virus.
These results allow researchers to distinguish between these two forms of ACE2. This knowledge can prove to be invaluable for developing more sophisticated treatments for COVID-19 patients.
Professor Jane Lucas, a professor of pediatric respiratory medicine at the University of Southampton, an honorary consultant at the Department of Pediatric Pulmonology at the University of Southampton Hospital, and one of the lead authors of the study, said:
“I was even more interested in managing when I was excited to discover a new form of ACE2 and realized that it could prevent SARS-CoV-2 in the respiratory tract rather than the site of infection. We believe it may have a significant impact. It is a COVID-19 infection and we are starting further research to investigate it further. ”
The novel ACE2 isoform is expressed in the human respiratory epithelium and is upregulated in response to interferon and RNA respiratory viral infections. Nature genetics (2021). DOI: 10.1038 / s41588-020-00759-x , www.nature.com/articles/s41588-020-00759-x
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