27 Feb 2020
Trials of the combination drug on human pancreatic cancer cells in vitro and in a laboratory rodent model of the human disease have produced promising results.
John Bonner
Job Title
A virus responsible for the deaths of millions of farm animals could help save the lives of human patients with pancreatic cancer, a study has suggested.
The research – by professor of tumour biology John Marshall and his team at Queen Mary University of London – has used part of the protein coat of the foot-and-mouth disease (FMD) virus combined with a powerful toxin to locate and destroy pancreatic duct adenocarcinoma cells.
Trials of the combination drug on human pancreatic cancer cells in vitro and in a laboratory rodent model of the human disease have produced promising results, reported in the journal Theranostics.
Pancreatic cancer is the fourth most common form of fatal cancer in western society and its incidence is increasing.
Prof Marshall’s research focuses on integrins – a family of cell surface receptors with a critical role in many different cellular functions, such as growth and adhesion.
Due to this fundamental role in mammalian physiology, the protein structure is highly conserved, with only minor variations in the amino acid sequence of different species, such as humans, rodents and cattle.
Prof Marshall became interested in the foot-and-mouth virus a decade ago, when working with Terry Jackson, a virologist at the Institute of Animal Health’s Pirbright laboratory.
Dr Jackson had identified the specific protein marker on the surface of the bovine tongue that enables the virus to enter the host’s cells.
Prof Marshall said: “We realised we were both looking at the same integrin, known as αvβ6.
“So I got one of my PhD students to chop up the proteins on the virus cell coat to find which particular sequence was important in allowing the virus to bind to the host integrin molecule.”
Prof Marshall’s team identified a sequence of 20 amino acids that was the key section. Surprisingly, the team found it contained not just one, but two, separate binding sites.
