ArticleProceedings of the National Academy of Sciences of the United States of America2007
Functionally important glycosyltransferase gain and loss during catarrhine primate emergence.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers, 1 of them a synthesis that pooled it.
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Who cites it
42 citing papers in PubMed, 1 synthesis or guideline pooled it, 81 citations in OpenAlex.
- Association between ABO blood groups and COVID-19 infection, severity and demise: A systematic review and meta-analysis.Infection, genetics and evolution : journal of molecular epidemiology and evolutionary genetics in infectious diseases · 2020Pooled it
- CRISPR-mediated engineering of bovine satellite cells for Alpha-Gal Syndrome-compatible cultivated meat.bioRxiv : the preprint server for biology · 2026Article
- The Immunology of Alpha-Gal Syndrome: History, Tick Bites, IgE, and Delayed Anaphylaxis to Mammalian Meat.Immunological reviews · 2025Review
- Review
- Perioperative implications of patients with alpha gal allergies.Journal of clinical anesthesia · 2023Review
- Noninsect-Based Diet Leads to Structural and Functional Changes of Acidic Chitinase in Carnivora.Molecular biology and evolution · 2022Article
- Association of ABO and Rh blood groups with obstetric outcomes in SARS-CoV-2 infected pregnancies: A prospective study with a multivariate analysis.European journal of obstetrics, gynecology, and reproductive biology · 2021Observational
- Review
- Infection withVaccines · 2020Article
- Do Blood Group Antigens and the Red Cell Membrane Influence Human Immunodeficiency Virus Infection?Cells · 2020Review
- GGTA1/iGb3S Double Knockout Mice: Immunological Properties and Immunogenicity Response to Xenogeneic Bone Matrix.BioMed research international · 2020Article
- Diagnosis and Management of Patients with the α-Gal Syndrome.The journal of allergy and clinical immunology. In practice · 2020Review
- Tick Bites Induce Anti-α-Gal Antibodies in Dogs.Vaccines · 2019Article
- Galactose α-1,3-galactose phenotypes: Lessons from various patient populations.Annals of allergy, asthma & immunology : official publication of the American College of Allergy, Asthma, & Immunology · 2019Review
- Addition of αGal HyperAcute™ technology to recombinant avian influenza vaccines induces strong low-dose antibody responses.PloS one · 2017Article
- Galactose-α-1,3-Galactose: Atypical Food Allergen or Model IgE Hypersensitivity?Current allergy and asthma reports · 2017Review
- At least two Fc Neu5Gc residues of monoclonal antibodies are required for binding to anti-Neu5Gc antibody.Scientific reports · 2016Article
- Molecular Evolution of the Glycosyltransferase 6 Gene Family in Primates.Biochemistry research international · 2016Article
- Use of genetically-engineered pig donors in islet transplantation.World journal of transplantation · 2015Review
- Anaphylaxis to the carbohydrate side chain alpha-gal.Immunology and allergy clinics of North America · 2015Review
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
A glycosyltransferase, alpha1,3galactosyltransferase, catalyzes the terminal step in biosynthesis of Galalpha1,3Galbeta1-4GlcNAc-R (alphaGal), an oligosaccharide cell surface epitope. This epitope or antigenically similar epitopes are widely distributed among the different forms of life. Although abundant in most mammals, alphaGal is not normally found in catarrhine primates (Old World monkeys and apes, including humans), all of which produce anti-alphaGal antibodies from infancy onward. Natural selection favoring enhanced resistance to alphaGal-positive pathogens has been the primary reason offered to account for the loss of alphaGal in catarrhines. Here, we question the primacy of this immune defense hypothesis with results that elucidate the evolutionary history of GGTA1 gene and pseudogene loci. One such locus, GGTA1P, a processed (intronless) pseudogene (PPG), is present in platyrrhines, i.e., New World monkeys, and catarrhines but not in prosimians. PPG arose in an early ancestor of anthropoids (catarrhines and platyrrhines), and GGTA1 itself became an unprocessed pseudogene in the late catarrhine stem lineage. Strong purifying selection, denoted by low nonsynonymous substitutions per nonsynonymous site/synonymous substitutions per synonymous site values, preserved GGTA1 in noncatarrhine mammals, indicating that the functional gene product is subjected to considerable physiological constraint. Thus, we propose that a pattern of alternative and/or more beneficial glycosyltransferase activity had to first evolve in the stem catarrhines before GGTA1 inactivation could occur. Enhanced defense against alphaGal-positive pathogens could then have accelerated the replacement of alphaGal-positive catarrhines by alphaGal-negative catarrhines. However, we emphasize that positively selected regulatory changes in sugar chain metabolism might well have contributed in a major way to catarrhine origins.
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Registered trials
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