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Crystal structure of Bifidobacterium bifidum glycoside hydrolase family 110 α-galactosidase specific for blood group B antigen
Open accessPreprint — published as 10.5458/jag.jag.jag-2024_0005
Abstract
To overcome incompatibility issues and increase the possibility of blood transfusion, technologies that enable efficient conversion of A- and B-type red blood cells to the universal donor O-type is desirable. Although several blood type-converting enzymes have been identified, detailed understanding about their molecular functions is limited. α-Galactosidase from Bifidobacterium bifidum JCM 1254 (AgaBb), belonging to glycoside hydrolase (GH) 110 subfamily A, specifically acts on blood group B antigen. Here we present the crystal structure of AgaBb, including the catalytic GH110 domain and part of the C-terminal uncharacterized regions. Based on this structure, we deduced a possible binding mechanism of blood group B antigen to the active site. Site-directed mutagenesis confirmed that R270 and E380 recognize the fucose moiety in the B antigen. Thermal shift assay revealed that the C-terminal uncharacterized region significantly contributes to protein stability. This region is shared only among GH110 enzymes from B. bifidum and some Ruminococcus species. The elucidation of the molecular basis for the specific recognition of blood group B antigen is expected to lead to the practical application of blood group conversion enzymes in the future.
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Highly accurate protein structure prediction with AlphaFold
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Metadata
- Authors
- Kashima, T., Akama, M., Wakinaka, T., Arakawa, T., Ashida, H., & Fushinobu, S.
- Affiliations
- The University of Tokyo (JP)
- Yamasa Corporation (Japan) (JP)
- Tokyo University of Science (JP)
- Kindai University (JP)
- Collaborative Research Institute for Innovative Microbiology, The University of Tokyo (JP)
- Corresponding author
- Fushinobu, Shinya
- Venue
- Journal of Applied Glycoscience
- Publisher
- openRxiv
- Published
- 2024-03-04
- Volume
- 71
- Issue
- 3
- Pages
- 81-90
- ISSN
- 1344-7882 (ISSN-L)
- PMC
- PMC11368712
- OpenAlex
- W4400028579
- Cited by
- 2
- References
- 1
- Citations by year
- 2025: 1 · 2024: 1
- FWCI
- 0.27
- Type
- journal article
- Language
- en
- Open access
- diamond
- doi.org
- Licence
- cc-by-nc
- Locations
- Journal of Applied Glycoscience (publishedVersion, cc-by-nc)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- PubMed Central (publishedVersion, cc-by-nc)
- PubMed (publishedVersion)
- Funders
- Mizutani Foundation for Glycoscience
- Japan Agency for Medical Research and Development (JP22ama-( 121001)
- University of Oxford
- Japan Society for the Promotion of Science (24H02269, 18K05494, 19H00929, 23H00322, 22K05548, 23KJ1174, 19K05789, 24380053)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Health Sciences › Medicine › Hematology › Blood groups and transfusion
- Keywords
- Bifidobacterium bifidum, alpha-galactosidase, blood group B antigen, universal donor, protein stability, Ruminococcus, blood transfusion
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