ArticleNature microbiology2019
An enzymatic pathway in the human gut microbiome that converts A to universal O type blood.
Article in Nature microbiology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers, 1 of them a synthesis that pooled it.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
48 citing papers in PubMed, 1 synthesis or guideline pooled it, 112 citations in OpenAlex.
- Pooled it
- Discovery of a secretedGut microbes · 2026Article
- Engineering the Universal Donor: CRISPR-Mediated Blood Group Antigen Deletion and the Path Toward Truly Universal Red Blood Cells-A Narrative Review.Diagnostics (Basel, Switzerland) · 2026Review
- The butyrate-producing Gram-positive human gut bacterium, Hoskinsella mucinilytica, selectively targets host mucin N-acetylhexosamines.The Journal of biological chemistry · 2026Article
- Catalyzing Carbohydrate Cleavage: Glycosidases and Their Mechanisms.Chemical reviews · 2026Review
- Genetic mechanisms for estuarine carbohydrate degradation and linked transcriptional activity.Applied and environmental microbiology · 2026Article
- Unlocking Enzyme Discovery: Leveraging Multi-Omics, Machine Learning, and De Novo Design.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Immobilized Enzymes for ABO-Independent Blood Cell Transfusions.Chembiochem : a European journal of chemical biology · 2025Article
- Reshaping of a Glycoside Hydrolase Active Site through Expression-Compensated Droplet-Based Microfluidic Screening Provides Useful Tools for Glycomics.ACS central science · 2025Article
- Article
- A Bacteroides thetaiotaomicron genetic locus encodes activities consistent with mucin O-glycoprotein processing and N-acetylgalactosamine metabolism.Nature communications · 2025Article
- Evaluation of Canine Erythrocyte Surface Antigens and Morphological Alterations Induced by Trypsin Treatment.Animals : an open access journal from MDPI · 2025Article
- Carbohydrate-active enzymes from Akkermansia muciniphila break down mucin O-glycans to completion.Nature microbiology · 2025Article
- Structural basis of FpGalNase and its combination with FpGalNAcDeAc for efficient A-to-O blood group conversion.Experimental hematology & oncology · 2025Article
- Improving normothermic machine perfusion and blood transfusion through biocompatible blood silicification.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Activity-based metaproteomics driven discovery and enzymological characterization of potential α-galactosidases in the mouse gut microbiome.Communications chemistry · 2024Article
- Carbohydrate-active enzyme (CAZyme) discovery and engineeringRSC chemical biology · 2024Review
- Article
- Gut microorganism enzymes unlock universal blood.Nature microbiology · 2024Article
- Akkermansia muciniphila exoglycosidases target extended blood group antigens to generate ABO-universal blood.Nature microbiology · 2024Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Access to efficient enzymes that can convert A and B type red blood cells to 'universal' donor O would greatly increase the supply of blood for transfusions. Here we report the functional metagenomic screening of the human gut microbiome for enzymes that can remove the cognate A and B type sugar antigens. Among the genes encoded in our library of 19,500 expressed fosmids bearing gut bacterial DNA, we identify an enzyme pair from the obligate anaerobe Flavonifractor plautii that work in concert to efficiently convert the A antigen to the H antigen of O type blood, via a galactosamine intermediate. The X-ray structure of the N-acetylgalactosamine deacetylase reveals the active site and mechanism of the founding member of an esterase family. The galactosaminidase expands activities within the CAZy family GH36. Their ability to completely convert A to O of the same rhesus type at very low enzyme concentrations in whole blood will simplify their incorporation into blood transfusion practice, broadening blood supply.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.