Alexander Hess
Contributing Writer
Often called the “Nobel Prize Factory,” the internationally renowned Molecular Biology Laboratory at the University of Cambridge, has made another potentially groundbreaking discovery.
Just last year the laboratory celebrated bringing home its fourteenth Nobel Prize since its foundation in 1947. Among its accolades are the discovery of the structure of DNA in 1953 by the famous duo Crick and Watson, and most recently in 2009 the elucidation of the structure of the ribosome, the primary protein “factory” in the cell.
The latest “eureka moment” to ring out from the fumehoods of this laboratory may just be a bona-fide treatment for the menace that is the common cold. This treatment, developed by Dr Leo James and his team, can also tackle many other viral ailments currently afflicting the world.
The winter vomiting virus (noravirus) and even rotavirus (which inflicts severe diarrhoea and kills thousands of children in developing countries) can literally be picked to pieces by the protein TRIM21.
Why has this protein, already well known to science, become the source of all this excitement? The answer is the discovery of how it operates inside the cell in conjunction with antibodies.
We have been led to believe until now that the action of antibodies were restricted to outside the cells, in the bloodstream, extra-cellular fluids, etc., seeking out foreign bodies and sticking to them, preparing them for attack and destruction by an army of white blood cells.
It has now been revealed that these antibodies can act inside the cell, contrary to what many of College’s first-year Science students learn in the prescribed biology textbooks.
It was previously thought that the immune system had no choice but to kill the wayward cell before the virus could replicate, become too ambitious and infect the other cells of the body.
It was revealed by James and his team that, “the antibody is attached to the virus and when the virus gets sucked inside the cell, the antibody stays attached, there is nothing in that process to make the antibody fall off.” These still-attached antibodies attract the attention of TRIM21, which naturally occurs within the cell.
It in turn attracts cylindrical proteins that inhabit the inside of the cell and attach themselves to the virus particle and proceed to rip the virus into tiny virus components.
“The beauty of it is that for every infection event, for every time a virus enters a cell, it is also an opportunity for the antibody in the cells to take the virus out,” James said.
One distinct possibility is that this TRIM21 protein could be delivered in a nasal spray, to attack the viruses directly and bring this piece of biological war-machinery to where it hurts.
“This is a way of boosting all the antibodies you’d be naturally making against the virus. The advantage is that you can use that one drug against potentially lots of viral infections,” states James.
In short, TRIM21 gives the infected cell a chance to fend off the virus by itself with its own biological machinery instead of the use of conventional drugs.
Sir Greg Winter, deputy director of the Laboratory of Molecular Biology, sums it up: “Antibodies are formidable molecular war machines; it now appears that they can continue to attack viruses within cells.
“This research is not only a leap in our understanding of how and where antibodies work, but more generally in our understanding of immunity and infection.”
Scientists believe the first clinical trials of new drugs based on the findings could begin within two to five years. It appears this celebrated laboratory has done it again.
