3D Map Of Coronavirus Developed To Understand The Infection Mechanism
Scientists at the University of Minnesota have enlightened on an essential biological mechanism that might have helped the coronavirus to infect humans and spread rapidly by developing a 3D map of the virus.
The comprehensive study of the virus’s structure revealed that the club-like “spikes” that it uses to establish infections on to human cells is about 4 times more strong than those on the SARS – that caused an epidemic in 2002 and resulted in hundreds of death.
The result of the study suggests that coronavirus particles that are inhaled via the nose or mouth have a high probability of attaching to cells in the upper respiratory tract, implying that relatively only a few viruses are required to infect and rapidly replicate.
Researchers developed an atomic-scale 3D map of the virus’s spike protein and its matching partner on human cells, referred to as the ACE-2 receptor using X-ray crystallography.
The spike proteins on the virus’ surface adhere to ACE-2 receptors when it encounters a human cell, and if the cell possesses them, it enables the virus to access and replicate inside the human cell.
Dr. Fang Li, who ledthe US team, said, “The 3D map of the virus shows that compared to the Sars virus that caused an outbreak in 2002-2003, the new coronavirus has evolved new approach to bind to its human receptor, resulting in stronger binding.” “The strong binding of the virus to the human receptor can help it infect human cells as well as spread among other human beings”.
This 3D map of the coronavirus can be used by scientists to look for prospective drugs that can neutralize the infection before replication has increased and the disease has completely spread. Dr. Fang Li said, “If a drug (antibody-drug conjugate) can bind to the sites on the virus more frequently and strongly than the ACE-2 receptor, it will obstruct the virus from binding to the cells, making it a reliable drug to treat COVID-19 that has already taken many lives.” “The same sites can be used to develop vaccines to prevent future infections.
In this study, the researchers described exactly how they compared the structure of the coronavirus strains found in pangolins and bats with that of COVID-19 coronavirus. The study showed that both animal strains of coronavirus can bind to the exact same ACE-2 receptor in humans, supporting previous work that suggests either the human coronavirus came from pangolins that got infected by bats or directly from bats. Prior to infecting human beings, animal strains underwent crucial mutations that allowed the infection to spread even more rapidly in human beings. The research is published in the journal Nature.
Jonathan Ball, a professor of virology, Nottingham University said, “We know that the COVID-19 causing coronavirus, Sars-CoV-2, acts extremely in different ways to its relative SARS” (Professor Jonathan Ball was not associated with the research study). “SARS often replicates in the lungs but COVID-19 effectively infects the throat and the nose, triggering mild cold-like signs and symptoms.
He added, “The Sars-CoV-2 surface spike protein has the ability to bind more successfully to the cell-surface protein called ACE-2 present in humans, which works as the entrance for these viruses. This better binding may enable the virus to infect the nose and the throat much more effectively, where the levels of ACE-2 receptors are thought to be at a reduced level.”
He also stated, “The research used viral spike fragments and host ACE-2 receptor, and this is still theoretical and specific ramifications will certainly require validation with further research and testing.”
Author: Sruthi S