Structural basis of FpGalNase and its combination with FpGalNAcDeAc for efficient A-to-O blood group conversion.

ABSTRACT: Transfusion safety and blood typing continue to present significant challenges in clinical practice, including risks of incorrect blood transfusions and blood shortages. One promising solution is the enzymatic conversion of all red blood cell (RBC) types into universal O-type RBCs. However, the major obstacle to this strategy is the relatively low catalytic efficiency of the enzymes involved. In this study, we investigated two enzymes from Flavonifractor plautii, N-acetylgalactosamine deacetylase (FpGalNAcDeAc) and galactosaminidase (FpGalNase), which demonstrate synergistic activity in efficiently converting A-type RBCs to O-type. We optimized treatment conditions, achieving over 99% conversion in just five minutes using phosphate buffer saline and a 16 nM enzyme concentration. Additional

SUBMITTER: Zhou M 

PROVIDER: S-EPMC11762096 | biostudies-literature | 2025 Jan

REPOSITORIES: biostudies-literature