It's hard to imagine a time when "coronaviruses" wasn't a household word For a long time, this family of Viruses had been ignored. The first coronaviruses to cause disease in humans was isolated in the 1960's and is believed to be ubiquitous among animals and birds.
Humans have been identified with seven coronaviruses.
Cold and seasonal respiratory infections are the most common health concerns. The 2003 outbreak of severe acute respiratory syndrome (SARS) in China and other parts of Asia propelled the virus onto the global stage. In 2012 there were cases of Middle East respiratory syndrome in Saudi Arabia.
The outbreaks were contained. Ordinary people don't pay much attention to coronaviruses diseases. For virologists, they focused their time and money on more pressing viruses. The causative agent of COVID-19 was SARS-coV-2.
Some researchers were still interested in coronaviruses. Viruses can change and cause new problems. Among them, we work at the University of the Western Cape. The structure of the building blocks of coronaviruses has been studied in our lab. coronaviruses reproduce, spread and cause disease by using spike, nucleocapsid, membrane, and envelope proteins.
In our most recent paper, we looked at the differences between the human coronaviruses that cause mild diseases like seasonal colds and the human coronaviruses that cause more severe diseases like Severe Acute Respiratory Syndrome (SRS). We argue that the answer lies with the envelopeProtein.
Due to its small size and the difficulty of studying it in laboratory settings, the envelope protein is one of the least studied coronaviruses. Two of us published a review paper in May of last year.
The paper has racked up nearly 2,000 citations, most of them coming after the outbreak of COVID-19, which was less a testament to our foresight than to the critical and previously underestimated role the envelopeprotein plays in human coronaviruses.
We were convinced that the key to the development of disease was the proteins that was once written off as a minor component of the virus. In the final assembly of the virus, it is important to form the envelope or wrapping that protects it when all of its components come together.
It plays a role in the emergence of the virus when it leaves the host cell, as well as in the development and progression of the infections.
It could be a clue to the severity of the disease.
Our research is showing that the structure of the envelope is related to the severity of a coronaviruses disease or the difference between a blocked nose and a collapsed lung.
We went to our most recent paper due to this. We collaborated with Ruben Cloete, of the South African National Bioinformatics Institute at the University of the Western Cape, to create full-length, 3D models of five human coronaviruses. We used a modelling program called MODELLER to explore theProtein in some detail.
We used a web server to make a simulation of how the envelopeProtein interacts with the human PALS-1Protein. The envelope proteins were able to bind to PALS-1 but the coronaviruses were able to bind more to PALS-1.
We believe that the answers may lie in the shape of the PBM, which sits at the tail end of the envelope. The PBM is a one-of-a-kind key that can be used to open a lock on a host cell protein. The disease is made worse by this key.
The coronaviruses that cause milder diseases may be different from the coronaviruses that cause more severe diseases.
It's too early to draw definitive conclusions, as more studies are needed to confirm the findings.
It shows some light on the inner workings of the coronaviruses. It could offer opportunities for the development of life saving treatments and vaccines.
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The authors were: Dewald Schoeman, University of the Western Cape, and Ruben Cloete, University of the Western Cape.
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