Scandinavian researchers have made a breakthrough in the search for universal donor blood, it has been announced.
The work by researchers at the Technical University of Denmark (DTU) and Lund University, Sweden, has been described as a “decisive step forward”.
The team discovered of bacterial enzymes that remove sugars on the surface of red blood cells that make up the A and B antigens of the ABO blood groups.
“For the first time, the new enzyme cocktails not only remove the well-described A and B antigens, but also extended variants previously not recognized as problematic for transfusion safety,” said study co-leader Professor Maher Abou Hachem, from the DTU.
The team have published their findings in Nature Microbiology.
They are not the first group to find enzymes to remove the A and B antigens, but they say theirs are highly efficient. They were found in Akkermansia muciniphila, a bacterium found in the guts of most healthy humans. It breaks down mucus and is thought to help with body weight and metabolic markers.
Professor Abou Hachem said: “What is special about the mucosa is that bacteria, which are able to live on this material, often have tailor-made enzymes to break down mucosal sugar structures, which include blood group ABO antigens. This hypothesis turned out to be correct.”
Study co-leader Professor Martin Olsson, from Lund University, said: “Universal blood will create a more efficient utilisation of donor blood, and also avoid giving ABO-mismatched transfusions by mistake, which can otherwise lead to potentially fatal consequences in the recipient.
“When we can create ABO-universal donor blood, we will simplify the logistics of transporting and administering safe blood products, while at the same time minimising blood waste.”
Source:
Jensen M, Stenfelt L, Ricci Hagman J, Pichler MJ, Weikum J, Nielsen TS, Hult A, Morth JP, Olsson ML, Abou Hachem M. (2024) “Akkermansia muciniphila exoglycosidases target extended blood group antigens to generate ABO-universal blood.” Nature Microbiology, 29 April 2024, doi: 10.1038/s41564-024-01663-4.
Link: https://www.nature.com/articles/s41564-024-01663-4
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