Identification and Protein Engineering of Galactosidases for the Conversion of Blood Type B to Blood Type O Article Swipe
Christina Möller
,
Henrik Terholsen
,
Ole Schmöker
,
T. Le
,
Jan Wesche
,
Paula Schmiade
,
Esther Eppendorfer
,
Niklas Rimkus
,
Britta Girbardt
,
Dominique Böttcher
,
Gottfried J. Palm
,
Jens Hoppen
,
Michael Lammers
,
Andreas Greinacher
,
Konstanze Aurich
,
Uwe T. Bornscheuer
·
YOU?
·
· 2025
· Open Access
·
· DOI: https://doi.org/10.1002/cbic.202500072
YOU?
·
· 2025
· Open Access
·
· DOI: https://doi.org/10.1002/cbic.202500072
The supply of blood products such as red blood cells poses a challenge due to rising demand and declining donor numbers. Careful matching of blood products of different types is required. Only type O of the blood types A, B, AB and O can be received by any patient without transfusion incompatibilities. Therefore, O‐type blood can be considered “universal blood” and is especially needed in emergency situations. In this study, we focused on the conversion of the B antigen by enzymatic deglycosylation to generate the H antigen determining O‐type blood. For this, we characterized several previously unstudied α‐1,3‐galactosidases belonging to the GH110 family. Our findings revealed that the α‐1,3‐galactosidase from Pedobacter panaciterrae (PpaGal) exhibits superior efficiency compared to previously described galactosidases. We further increased the activity of PpaGal by 2.5‐fold using site‐directed mutagenesis. Moreover, we solved two crystal structures of PpaGal, one in the apo‐state and another in complex with d ‐galactose. The combination of our mutagenesis study with the solved crystal structures provides valuable information to guide further optimization of PpaGal or other B antigen converting enzymes paving the way for the easier production of universal blood from B‐type blood.
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- Type
- article
- Language
- en
- Landing Page
- https://doi.org/10.1002/cbic.202500072
- https://onlinelibrary.wiley.com/doi/pdfdirect/10.1002/cbic.202500072
- OA Status
- hybrid
- Cited By
- 2
- References
- 30
- Related Works
- 10
- OpenAlex ID
- https://openalex.org/W4408026458
All OpenAlex metadata
Raw OpenAlex JSON
- OpenAlex ID
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https://openalex.org/W4408026458Canonical identifier for this work in OpenAlex
- DOI
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https://doi.org/10.1002/cbic.202500072Digital Object Identifier
- Title
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Identification and Protein Engineering of Galactosidases for the Conversion of Blood Type B to Blood Type OWork title
- Type
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articleOpenAlex work type
- Language
-
enPrimary language
- Publication year
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2025Year of publication
- Publication date
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2025-03-01Full publication date if available
- Authors
-
Christina Möller, Henrik Terholsen, Ole Schmöker, T. Le, Jan Wesche, Paula Schmiade, Esther Eppendorfer, Niklas Rimkus, Britta Girbardt, Dominique Böttcher, Gottfried J. Palm, Jens Hoppen, Michael Lammers, Andreas Greinacher, Konstanze Aurich, Uwe T. BornscheuerList of authors in order
- Landing page
-
https://doi.org/10.1002/cbic.202500072Publisher landing page
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https://onlinelibrary.wiley.com/doi/pdfdirect/10.1002/cbic.202500072Direct link to full text PDF
- Open access
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YesWhether a free full text is available
- OA status
-
hybridOpen access status per OpenAlex
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https://onlinelibrary.wiley.com/doi/pdfdirect/10.1002/cbic.202500072Direct OA link when available
- Concepts
-
Blood type (non-human), Enzyme, Whole blood, Antigen, Biochemistry, Chemistry, Biology, ABO blood group system, ImmunologyTop concepts (fields/topics) attached by OpenAlex
- Cited by
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2Total citation count in OpenAlex
- Citations by year (recent)
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2025: 2Per-year citation counts (last 5 years)
- References (count)
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30Number of works referenced by this work
- Related works (count)
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10Other works algorithmically related by OpenAlex
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| abstract_inverted_index.B | 78, 175 |
| abstract_inverted_index.H | 86 |
| abstract_inverted_index.O | 34, 43 |
| abstract_inverted_index.a | 12 |
| abstract_inverted_index.d | 151 |
| abstract_inverted_index.A, | 39 |
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| abstract_inverted_index.B, | 40 |
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| abstract_inverted_index.by | 47, 80, 129 |
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| abstract_inverted_index.we | 71, 93, 135 |
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| abstract_inverted_index.this | 69 |
| abstract_inverted_index.type | 33 |
| abstract_inverted_index.with | 150, 159 |
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| abstract_inverted_index.types | 29, 38 |
| abstract_inverted_index.using | 131 |
| abstract_inverted_index.PpaGal | 128, 172 |
| abstract_inverted_index.blood. | 90, 191 |
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| abstract_inverted_index.paving | 179 |
| abstract_inverted_index.rising | 16 |
| abstract_inverted_index.solved | 136, 161 |
| abstract_inverted_index.study, | 70 |
| abstract_inverted_index.supply | 2 |
| abstract_inverted_index.Careful | 22 |
| abstract_inverted_index.PpaGal, | 141 |
| abstract_inverted_index.another | 147 |
| abstract_inverted_index.antigen | 79, 87, 176 |
| abstract_inverted_index.complex | 149 |
| abstract_inverted_index.crystal | 138, 162 |
| abstract_inverted_index.enzymes | 178 |
| abstract_inverted_index.family. | 103 |
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| abstract_inverted_index.patient | 49 |
| abstract_inverted_index.several | 95 |
| abstract_inverted_index.without | 50 |
| abstract_inverted_index.(PpaGal) | 113 |
| abstract_inverted_index.Abstract | 0 |
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| abstract_inverted_index.O‐type | 54, 89 |
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| abstract_inverted_index.blood” | 60 |
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| abstract_inverted_index.matching | 23 |
| abstract_inverted_index.numbers. | 21 |
| abstract_inverted_index.products | 5, 26 |
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| abstract_inverted_index.received | 46 |
| abstract_inverted_index.revealed | 106 |
| abstract_inverted_index.superior | 115 |
| abstract_inverted_index.valuable | 165 |
| abstract_inverted_index.Moreover, | 134 |
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| abstract_inverted_index.enzymatic | 81 |
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| abstract_inverted_index.unstudied | 97 |
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| abstract_inverted_index.considered | 58 |
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| abstract_inverted_index.situations. | 67 |
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| abstract_inverted_index.panaciterrae | 112 |
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| abstract_inverted_index.characterized | 94 |
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| abstract_inverted_index.deglycosylation | 82 |
| abstract_inverted_index.galactosidases. | 121 |
| abstract_inverted_index.site‐directed | 132 |
| abstract_inverted_index.incompatibilities. | 52 |
| abstract_inverted_index.α‐1,3‐galactosidase | 109 |
| abstract_inverted_index.α‐1,3‐galactosidases | 98 |
| cited_by_percentile_year.max | 97 |
| cited_by_percentile_year.min | 95 |
| countries_distinct_count | 1 |
| institutions_distinct_count | 16 |
| citation_normalized_percentile.value | 0.92559254 |
| citation_normalized_percentile.is_in_top_1_percent | False |
| citation_normalized_percentile.is_in_top_10_percent | True |