HOUSTON: Scientists have figured out the structure of a molecule that uses the new coronavirus to make its genetic sequence appear to be part of the host itself, an advance that may lead to the development of new antiviral drugs against COVID-19.
According to the study, published in the journal Nature Communications, the nsp10 molecule modifies viral mRNAs (which are flat to make proteins) to mimic the host cell’s own mRNAs.
Researchers at the University of Texas Health Sciences Center at San Antonio (UT Health San Antonio) in the US said that by enabling this modification, nsp10 protects the virus from the host cell’s immune response.
“It is camouflage. Due to the modifications, which fool the cell, the resulting viral messenger RNA is now considered part of the cell’s code and not foreign,” said Yogesh Gupta, co-author of the UT Health San Antonio study.
Deciphering the 3D structure of nsp16 paves the way for the design of new drugs against the new coronavirus SARS-CoV-2 and other emerging coronavirus infections, the researchers said.
These drugs, Gupta said, can be designed to inhibit nsp16 from making the modifications, so that the host’s immune system rushes over the invading virus, recognizing it as foreign.
“Yogesh’s work uncovered the 3D structure of a key COVID-19 virus enzyme required for its replication and found a pocket that can be targeted to inhibit that enzyme. This is a critical advance in our understanding of the virus,” said co-author of the Robert Hromas study.
Based on the findings, the researchers have suggested structural sites on the SARS-CoV-2 nsp10 molecule that they say may be the target of antiviral development.
According to the study, published in the journal Nature Communications, the nsp10 molecule modifies viral mRNAs (which are flat to make proteins) to mimic the host cell’s own mRNAs.
Researchers at the University of Texas Health Sciences Center at San Antonio (UT Health San Antonio) in the US said that by enabling this modification, nsp10 protects the virus from the host cell’s immune response.
“It is camouflage. Due to the modifications, which fool the cell, the resulting viral messenger RNA is now considered part of the cell’s code and not foreign,” said Yogesh Gupta, co-author of the UT Health San Antonio study.
Deciphering the 3D structure of nsp16 paves the way for the design of new drugs against the new coronavirus SARS-CoV-2 and other emerging coronavirus infections, the researchers said.
These drugs, Gupta said, can be designed to inhibit nsp16 from making the modifications, so that the host’s immune system rushes over the invading virus, recognizing it as foreign.
“Yogesh’s work uncovered the 3D structure of a key COVID-19 virus enzyme required for its replication and found a pocket that can be targeted to inhibit that enzyme. This is a critical advance in our understanding of the virus,” said co-author of the Robert Hromas study.
Based on the findings, the researchers have suggested structural sites on the SARS-CoV-2 nsp10 molecule that they say may be the target of antiviral development.
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