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Volume 22
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10.3390/ijms22189761
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Article

Two Paralogous Gb3/CD77 Synthases in Birds Show Different Preferences for Their Glycoprotein and Glycosphingolipid Substrates

by
Anna Bereznicka
1,
Krzysztof Mikolajczyk
1,
Katarzyna Szymczak-Kulus
1,
Katarzyna Kapczynska
2,
Edyta Majorczyk
3,
Anna Modlinska
4,
Tomasz Piasecki
4,
Radoslaw Kaczmarek
1 and
Marcin Czerwinski
1,*
1
Laboratory of Glycobiology, Department of Immunochemistry, Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, 53-114 Wroclaw, Poland
2
Laboratory of Medical Microbiology, Department of Immunology of Infectious Diseases, Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, 53-114 Wroclaw, Poland
3
Faculty of Physical Education and Physiotherapy, Opole University of Technology, 45-758 Opole, Poland
4
Department of Epizootiology and Clinic of Birds and Exotic Animals, Wroclaw University of Environmental Sciences, 50-366 Wroclaw, Poland
*
Author to whom correspondence should be addressed.
Int. J. Mol. Sci. 2021, 22(18), 9761; https://doi.org/10.3390/ijms22189761
Submission received: 13 August 2021 / Revised: 6 September 2021 / Accepted: 6 September 2021 / Published: 9 September 2021
(This article belongs to the Special Issue Complex Carbohydrates and Glycoconjugates: Structure, Functions and Applications 2021)
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Abstract

Most glycosyltransferases show remarkable gross and fine substrate specificity, which is reflected in the old one enzyme-one linkage paradigm. While human Gb3/CD77 synthase is a glycosyltransferase that synthesizes the Galα1→4Gal moiety mainly on glycosphingolipids, its pigeon homolog prefers glycoproteins as acceptors. In this study, we characterized two Gb3/CD77 synthase paralogs found in pigeons (Columba livia). We evaluated their specificities in transfected human teratocarcinoma 2102Ep cells by flow cytofluorometry, Western blotting, high-performance thin-layer chromatography, mass spectrometry and metabolic labelling with 14C-galactose. We found that the previously described pigeon Gb3/CD77 synthase (called P) can use predominately glycoproteins as acceptors, while its paralog (called M), which we serendipitously discovered while conducting this study, efficiently synthesizes Galα1→4Gal caps on both glycoproteins and glycosphingolipids. These two paralogs may underlie the difference in expression profiles of Galα1→4Gal-terminated glycoconjugates between neoavians and mammals.
Keywords: Gb3/CD77 synthase; glycosyltransferase; Shiga toxin; birds Gb3/CD77 synthase; glycosyltransferase; Shiga toxin; birds

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MDPI and ACS Style

Bereznicka, A.; Mikolajczyk, K.; Szymczak-Kulus, K.; Kapczynska, K.; Majorczyk, E.; Modlinska, A.; Piasecki, T.; Kaczmarek, R.; Czerwinski, M. Two Paralogous Gb3/CD77 Synthases in Birds Show Different Preferences for Their Glycoprotein and Glycosphingolipid Substrates. Int. J. Mol. Sci. 2021, 22, 9761. https://doi.org/10.3390/ijms22189761

AMA Style

Bereznicka A, Mikolajczyk K, Szymczak-Kulus K, Kapczynska K, Majorczyk E, Modlinska A, Piasecki T, Kaczmarek R, Czerwinski M. Two Paralogous Gb3/CD77 Synthases in Birds Show Different Preferences for Their Glycoprotein and Glycosphingolipid Substrates. International Journal of Molecular Sciences. 2021; 22(18):9761. https://doi.org/10.3390/ijms22189761

Chicago/Turabian Style

Bereznicka, Anna, Krzysztof Mikolajczyk, Katarzyna Szymczak-Kulus, Katarzyna Kapczynska, Edyta Majorczyk, Anna Modlinska, Tomasz Piasecki, Radoslaw Kaczmarek, and Marcin Czerwinski. 2021. "Two Paralogous Gb3/CD77 Synthases in Birds Show Different Preferences for Their Glycoprotein and Glycosphingolipid Substrates" International Journal of Molecular Sciences 22, no. 18: 9761. https://doi.org/10.3390/ijms22189761

APA Style

Bereznicka, A., Mikolajczyk, K., Szymczak-Kulus, K., Kapczynska, K., Majorczyk, E., Modlinska, A., Piasecki, T., Kaczmarek, R., & Czerwinski, M. (2021). Two Paralogous Gb3/CD77 Synthases in Birds Show Different Preferences for Their Glycoprotein and Glycosphingolipid Substrates. International Journal of Molecular Sciences, 22(18), 9761. https://doi.org/10.3390/ijms22189761

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