VANCOUVER, British Columbia, April 29 (UPI) -- What if a patient needs type A blood, but all that's left in the blood bank is type B? It's a problem doctors have been trying to solve for a long time.
But until recently, all the potential solutions were inefficient and expensive. New research out of Canada, however, may offer an affordable fix -- a method for changing blood types.
The solution is just as much material as it is method -- an enzyme, one designed to siphon off the sugars, called antigens, in Type A and Type B blood, transforming them into something that resembles Type O blood. Type O blood, known as the "universal donor," can be safely given to patients with any blood type.
But the glycosidase enzymes, extracted from bacteria, has been around for several years now. What's new, is that researchers at the University of British Columbia figured out a way to synthesize a much more powerful and efficient sugar-eating enzyme.
"We produced a mutant enzyme that is very efficient at cutting off the sugars in A and B blood, and is much more proficient at removing the subtypes of the A-antigen that the parent enzyme struggles with," lead study author David Kwan, a chemist and postdoctoral fellow, explained in a press release.
Using a technique called directed evolution, Kwan and his colleagues manipulated the genes of the enzyme to create mutations. They then selected the mutations that were most effective at eating antigens. After five generations, the scientists had birthed an enzyme 170 times more efficient than the original.
The method isn't yet perfect. The enzyme can remove the vast majority of antigens, but in order for transformed blood to be used safely on human patients, all of the extra sugars need to be removed. Even small amounts of lingering antigens can cause the body to reject the new blood.
"The concept is not new but until now we needed so much of the enzyme to make it work that it was impractical," said co-author Steve Withers, a chemistry professor. "Now I'm confident that we can take this a whole lot further."
The new research was published in the Journal of the American Chemical Society.