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Researchers at the University of Minnesota created a 3D map of the ‘spike’ protein used to latch on to cells
New research has shed light on a crucial biological mechanism that may have helped the coronavirus to infect humans and spread rapidly around the world.
A detailed analysis of the virus’s structure shows that the club-like “spikes” that it uses to establish infections latch on to human cells about four times more strongly than those on the related Sars coronavirus, which killed hundreds of people in a 2002 epidemic.
The finding suggests that coronavirus particles that are inhaled through the nose or mouth have a high chance of attaching to cells in the upper respiratory tract, meaning that relatively few are needed for an infection to gain a foothold.
Scientists at the University of Minnesota used X-ray crystallography to create an atomic-scale 3D map of the virus’s spike protein and its corresponding partner on human cells, known as the ACE-2 receptor.
When the virus encounters a human cell, the spike proteins on its surface stick to ACE-2 receptors, if the cell possess them, and allow the virus to gain access and replicate.
“The 3D structure shows that compared to the virus that caused the 2002-2003 Sars outbreak, the new coronavirus has evolved new strategies to bind to its human receptor, resulting in tighter binding,” said Dr Fang Li, who led the US team. “The tight binding to the human receptor can help the virus infect human cells and spread among humans.”
The map of the virus will now be used by scientists to search for potential drugs that can neutralise the virus before replication has ramped up and the infection has taken hold. “If a new antibody drug can bind to those sites on the virus more strongly and frequently than the receptor, it will block the virus out of cells, making it a potentially effective treatment for viral infections,” Li said. The same sites can be used to shape work on vaccines to prevent future infections, he added.
Writing in the journal Nature, the researchers describe how they went on to compare the structure of the pandemic coronavirus with related strains found in bats and pangolins. They found that both animal strains could bind to the same human ACE-2 receptor, supporting previous work that suggests the human coronavirus came from bats either directly, or via pangolins that themselves became infected by bats. Before infecting humans, the animal strains picked up key mutations that allowed the virus to spread more easily in humans.
“We know that the Covid-19-causing coronavirus, Sars-CoV-2, behaves very differently to its relative Sars,” said Jonathan Ball, a professor of virology at Nottingham University, who was not involved in the study. “In particular, Sars-Cov-2 efficiently infects the throat and the nose, causing mild cold-like symptoms, whereas Sars almost always replicated in the lungs.
“This study provides an attractive reason for this difference: the Sars-CoV-2 surface spike protein is able to bind more efficiently to the cell-surface protein, called ACE-2, which acts as the doorway for these viruses to enter into the cell. This improved binding might allow the virus to infect the nose and the throat more efficiently, where the levels of ACE-2 are thought to be lower.”
“The study only used fragments of the virus spike and host ACE-2 protein, and this is still only a theory,” he added. “The exact implications will need validation through further experimentation.”
New research has shed light on a crucial biological mechanism that may have helped the coronavirus to infect humans and spread rapidly around the world.
A detailed analysis of the virus’s structure shows that the club-like “spikes” that it uses to establish infections latch on to human cells about four times more strongly than those on the related Sars coronavirus, which killed hundreds of people in a 2002 epidemic.
The finding suggests that coronavirus particles that are inhaled through the nose or mouth have a high chance of attaching to cells in the upper respiratory tract, meaning that relatively few are needed for an infection to gain a foothold.
Scientists at the University of Minnesota used X-ray crystallography to create an atomic-scale 3D map of the virus’s spike protein and its corresponding partner on human cells, known as the ACE-2 receptor.
When the virus encounters a human cell, the spike proteins on its surface stick to ACE-2 receptors, if the cell possess them, and allow the virus to gain access and replicate.
“The 3D structure shows that compared to the virus that caused the 2002-2003 Sars outbreak, the new coronavirus has evolved new strategies to bind to its human receptor, resulting in tighter binding,” said Dr Fang Li, who led the US team. “The tight binding to the human receptor can help the virus infect human cells and spread among humans.”
The map of the virus will now be used by scientists to search for potential drugs that can neutralise the virus before replication has ramped up and the infection has taken hold. “If a new antibody drug can bind to those sites on the virus more strongly and frequently than the receptor, it will block the virus out of cells, making it a potentially effective treatment for viral infections,” Li said. The same sites can be used to shape work on vaccines to prevent future infections, he added.
Writing in the journal Nature, the researchers describe how they went on to compare the structure of the pandemic coronavirus with related strains found in bats and pangolins. They found that both animal strains could bind to the same human ACE-2 receptor, supporting previous work that suggests the human coronavirus came from bats either directly, or via pangolins that themselves became infected by bats. Before infecting humans, the animal strains picked up key mutations that allowed the virus to spread more easily in humans.
“We know that the Covid-19-causing coronavirus, Sars-CoV-2, behaves very differently to its relative Sars,” said Jonathan Ball, a professor of virology at Nottingham University, who was not involved in the study. “In particular, Sars-Cov-2 efficiently infects the throat and the nose, causing mild cold-like symptoms, whereas Sars almost always replicated in the lungs.
“This study provides an attractive reason for this difference: the Sars-CoV-2 surface spike protein is able to bind more efficiently to the cell-surface protein, called ACE-2, which acts as the doorway for these viruses to enter into the cell. This improved binding might allow the virus to infect the nose and the throat more efficiently, where the levels of ACE-2 are thought to be lower.”
“The study only used fragments of the virus spike and host ACE-2 protein, and this is still only a theory,” he added. “The exact implications will need validation through further experimentation.”
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An interesting read.
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What about the eyes ? We hear thats the other route, but how easy/likely is it compared to the nose and mouth ?
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Yes, via your eyes is the third entry point.
No idea how it then makes its way to your throat from there which is the thrust of the article. |
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I heard some nutter on a news bulletin suggesting that masks were all you needed, and that if someone sneezed near you, "just close your eyes"
Bit like telling someone to duck if someone fires a gun at you, you'll be fine  |