An introduction makes a big difference when we meet strangers. In olden times a chaperone would accompany a young lady in mixed company to facilitate social engagements. Scientists at Keck Medicine of University of Southern California have revisited the role of molecular chaperone GRP78. Apparently it can act as hijacked intermediary in COVID infections, and is therefore a gateway to explore.
Role of Molecular Chaperone GRP78 in Viral Infections
Chaperone GRP78 helps regulate the correct folding of proteins, especially when a cell is under stress according to Keck Medicine. This is the autonomous process whereby a biologically active protein comes together. However, in some cases viruses ‘hijack’ this benign system, so they can infect target human cells to reproduce and spread.
GRP78 serves as co-receptor and stabilizing agent between ACE2 gateways and SARS-CoV-2 causing COVID-19, in this involuntary role. Keck Medicine says this ‘enhances recognition of the virus’ spike protein, and allows more efficient viral entry into host cells’.
Moreover, the Kerk report in Journal of Biological Chemistry observes more infectious COVID-19 variants bind stronger to the molecular chaperone. But targeting it with compound hMAb59 could have ‘a broad spectrum anti-viral effect’, the team has found.
Why This Matters Greatly in the Struggle against COVID-19
Kerk School of Medicine agrees rapid distribution of vaccines is vital to limit the spread of the pandemic. However a number of challenges stand in the way of achieving herd immunity, over and above vaccine nay sayers.
These challenges include new mutations. And also people who are immune-suppressed, and thus unable to form an effective response to the vaccine.
We clearly need at least one more medical strategy to close these gaps. Targeting molecular chaperone GRP78 with the proposed hMAb59 pre-treatment, could be part of a COVID shot gun plan. But the next question is how do we go about implementing this finding?
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Preview Image: Targeting Molecular Chaperone GRP78
