“This finding can help us develop new antiviral and antifibrotic medicines to help treat pathogenic coronaviruses, and possibly other viruses or other situations where lung fibrosis occurs. “Since this receptor can block COVID-19 infection, and at the same time activate our body’s anti-virus response, and suppress our body’s fibrosis response, this is a really important new gene,” Professor Neely said. “When we studied how this new receptor works, we found that this receptor also controls antiviral responses, as well as fibrosis, and could link COVID-19 infection with lung fibrosis that occurs during long COVID,” Mr Waller said. Pastel pop art illustration of human lung generated using OpenAI’s DALL♾ 2 Implications of the research “We think this newly identified protein could be part of our body’s natural response to combating the infection creating a barrier that physically separates the virus from our lung cells most sensitive to COVID-19.” “When we stain the lungs of healthy tissue, we don't see much of LRRC15, but then in COVID-19 lungs, we see much more of the protein,” Dr Loo said. But the researchers found human lungs light up with LRRC15 after infection. LRRC15 is present in many locations such as lungs, skin, tongue, fibroblasts, placenta and lymph nodes. “Basically, the virus is coated in the other part of the Velcro, and while it's trying to get to the main receptor, it can get caught up in this mesh of LRRC15,” Mr Waller said. “We think it acts a bit like Velcro, molecular Velcro, in that it sticks to the spike of the virus and then pulls it away from the target cell types,” Dr Loo said. In the process, it prevents other vulnerable cells from becoming infected. It can, however, stick to the virus and immobilise it. But unlike ACE2, LRRC15 does not support infection. Like ACE2, LRRC15 is a receptor for coronavirus, meaning the virus can bind to it. Lung cells have high levels of ACE2 receptors, which is why the COVID-19 virus often causes severe problems in this organ of infected people. It primarily uses a protein called the angiotensin-converting enzyme 2 (ACE2) receptor to enter human cells. The COVID-19 virus infects humans by using a spike protein to attach to a specific receptor in our cells. “We can now use this new receptor to design broad acting drugs that can block viral infection or even suppress lung fibrosis.” What is LRRC15? “For me, as an immunologist, the fact that there's this natural immune receptor that we didn't know about, that's lining our lungs and blocks and controls virus, that's crazy interesting. We found that this new receptor acts by binding to the virus and sequestering it which reduces infection,” Professor Neely said. “Alongside two other groups, one at Oxford, the other at Brown and Yale in the USA, we found a new receptor in the LRRC15 protein that can stop SARS-CoV-2. The University study is one of three independent papers that reveal this specific protein’s interaction with COVID-19. It was led by Professor Greg Neely with his team members Dr Lipin Loo, a postdoctoral researcher, and PhD student Matthew Waller at the Charles Perkins Centre and the School of Life and Environmental Sciences. The study has been published in the journal PLOS Biology. The research opens up an entirely new area of immunology research around LRRC15 and offers a promising pathway to develop new drugs to prevent viral infection from coronaviruses like COVID-19 or deal with fibrosis in the lungs. This protein, the leucine-rich repeat-containing protein 15 (LRRC15), is an inbuilt receptor that binds the SARS-CoV-2 virus without passing on the infection. Right: Immunofluorescent staining shows expression of new SARS-CoV-2 spike-receptor LRRC15 (green) in post-mortem lung tissue section from individual with COVID-19
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